James H Hurley

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. pmc Molecular mechanisms of ubiquitin-dependent membrane traffic
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Annu Rev Biophys 40:119-42. 2011
  2. pmc The circuitry of cargo flux in the ESCRT pathway
    James H Hurley
    Laboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892
    J Cell Biol 185:185-7. 2009
  3. pmc Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    Thomas Wollert
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nature 464:864-9. 2010
  4. pmc Membrane budding
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Cell 143:875-87. 2010
  5. pmc Ubiquitin-binding domains
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Biochem J 399:361-72. 2006
  6. pmc The ESCRT complexes
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Crit Rev Biochem Mol Biol 45:463-87. 2010
  7. pmc The ESCRT complexes: structure and mechanism of a membrane-trafficking network
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, Maryland 20892 0580, USA
    Annu Rev Biophys Biomol Struct 35:277-98. 2006
  8. pmc Membrane budding and scission by the ESCRT machinery: it's all in the neck
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0580, USA
    Nat Rev Mol Cell Biol 11:556-66. 2010
  9. pmc Membrane binding domains
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Biochim Biophys Acta 1761:805-11. 2006
  10. doi request reprint MIT domainia
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Dev Cell 14:6-8. 2008

Detail Information

Publications84

  1. pmc Molecular mechanisms of ubiquitin-dependent membrane traffic
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Annu Rev Biophys 40:119-42. 2011
    ....
  2. pmc The circuitry of cargo flux in the ESCRT pathway
    James H Hurley
    Laboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892
    J Cell Biol 185:185-7. 2009
    ..A. Payne, D.J. Katzmann, and R. Piper. 2009. J. Cell Biol. 185:213-224) identify a new ubiquitin-binding site in ESCRT-I and provide evidence that the upstream ESCRT-I and -II complexes sort cargo in parallel rather than in series...
  3. pmc Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    Thomas Wollert
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nature 464:864-9. 2010
    ..The observations explain how the ESCRTs direct membrane budding and scission from the cytoplasmic side of the bud without being consumed in the reaction...
  4. pmc Membrane budding
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Cell 143:875-87. 2010
    ..This Review discusses progress toward understanding the structural and energetic bases of these different membrane-budding paradigms...
  5. pmc Ubiquitin-binding domains
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Biochem J 399:361-72. 2006
    ....
  6. pmc The ESCRT complexes
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Crit Rev Biochem Mol Biol 45:463-87. 2010
    ..This review will describe the structure and function of the six complexes noted above and summarize current knowledge of their mechanistic roles in cellular pathways and in disease...
  7. pmc The ESCRT complexes: structure and mechanism of a membrane-trafficking network
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, Maryland 20892 0580, USA
    Annu Rev Biophys Biomol Struct 35:277-98. 2006
    ..The structures and interactions of many of the components have been determined over the past three years, revealing mechanisms for membrane and cargo recruitment and for complex assembly...
  8. pmc Membrane budding and scission by the ESCRT machinery: it's all in the neck
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0580, USA
    Nat Rev Mol Cell Biol 11:556-66. 2010
    ..Recent studies of ultrastructures induced by ESCRT-III overexpression in cells and the in vitro reconstitution of the budding and scission reactions have led to breakthroughs in understanding these remarkable membrane reactions...
  9. pmc Membrane binding domains
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Biochim Biophys Acta 1761:805-11. 2006
    ..These domains use a combination of specific headgroup interactions, hydrophobic membrane penetration, electrostatic surface interactions, and shape complementarity to bind to specific subcellular membranes...
  10. doi request reprint MIT domainia
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Dev Cell 14:6-8. 2008
    ..Vps4 and Vta1 both contain MIT domains, which bind to "MIT-interacting motifs" (MIMs) of ESCRT-III proteins. As new MIT domain proteins are rapidly being identified, these studies will likely have relevance well beyond Vps4...
  11. doi request reprint Piecing together the ESCRTs
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Biochem Soc Trans 37:161-6. 2009
    ..Molecular simulations, hydrodynamic analysis, small-angle X-ray scattering and cryo-EM (electron microscopy) techniques have all been brought to bear on the ESCRT system over the last year...
  12. pmc Nipped in the bud: how the AMSH MIT domain helps deubiquitinate lysosome-bound cargo
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Structure 19:1033-5. 2011
    ..In this issue of Structure, Solomons et al. now reveal an extraordinarily high affinity complex between the "MIM4" region of one ESCRT-III subunit, CHMP3, and the MIT domain of AMSH...
  13. pmc ESCRT complexes and the biogenesis of multivesicular bodies
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Curr Opin Cell Biol 20:4-11. 2008
    ..A key role for deubiquitination in the regulation of the system has been demonstrated. One central question remains largely unanswered, which is how the ESCRTs actually promote the invagination of the endosomal membrane...
  14. pmc Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex
    Young Jun Im
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Dev Cell 14:902-13. 2008
    ..ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. These data provide a unifying structural and functional framework for the ESCRT-II complex...
  15. pmc Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins
    Gali Prag
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 102:2334-9. 2005
    ..This ability highlights the GAT domain as a hub for interactions with multiple partners in trafficking...
  16. pmc Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55
    Hyung Ho Lee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA
    Science 322:576-80. 2008
    ..Both ALIX and ESCRT-I are required for cytokinesis, which suggests that multiple CEP55 dimers are required for function...
  17. pmc Structural and functional organization of the ESCRT-I trafficking complex
    Michael S Kostelansky
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Cell 125:113-26. 2006
    ..The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners...
  18. ncbi request reprint Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism
    Yukio Kato
    Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nat Struct Biol 9:532-6. 2002
    ....
  19. ncbi request reprint Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase
    Gregory J Miller
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, United States Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Mol Cell 18:201-12. 2005
    ....
  20. pmc Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis
    Young Jun Im
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Dev Cell 17:234-43. 2009
    ..Docking of the ESCRT-II-VPS20(2) supercomplex reveals a convex membrane-binding surface, suggesting a hypothesis for negative membrane curvature induction in the nascent intralumenal vesicle...
  21. pmc The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting
    Gali Prag
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Dev Cell 12:973-86. 2007
    ..Coarse-grained Monte Carlo simulations of the Vps27/Hse1 complex on a membrane show how the complex binds cooperatively to lipids and ubiquitinated membrane proteins and acts as a scaffold for ubiquitination reactions...
  22. pmc Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9
    Daniel P Kloer
    Laboratory of Molecular Biology, NIDDK, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 285:7794-804. 2010
    ..This interaction is mediated by HPS4 and the switch I and II regions of Rab9. These characteristics indicate that BLOC-3 might function as a Rab9 effector in the biogenesis of LROs...
  23. pmc Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer
    Michael S Kostelansky
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Cell 129:485-98. 2007
    ..The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm...
  24. pmc Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag PTAP interaction
    Young Jun Im
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Structure 18:1536-47. 2010
    ..However, the mutant alleles did rescue downregulation of endogenous EGF receptor. This demonstrates that the PSAP motif is not rate determining in EGF receptor downregulation under normal conditions...
  25. pmc Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission
    Evzen Boura
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Structure 20:874-86. 2012
    ..The hybrid refinement used here is general and should be applicable to other dynamic multiprotein assmeblies...
  26. pmc Functional architecture of the retromer cargo-recognition complex
    Aitor Hierro
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nature 449:1063-7. 2007
    ..This extended structure presents multiple binding sites for the SNX complex and receptor cargo, and appears capable of flexing to conform to curved vesicular membranes...
  27. pmc Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    Sumana Raychaudhuri
    Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, United States Department of Health and Human Services, Bethesda, MD 20892, USA
    J Cell Biol 173:107-19. 2006
    ..Our findings argue that ORPs move sterols among cellular compartments and that sterol transport and intracellular distribution are regulated by PIPs...
  28. pmc Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5
    Sangho Lee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health NIH, Bethesda, Maryland 20892, USA
    Nat Struct Mol Biol 13:264-71. 2006
    ..The A20 zinc-finger diaromatic patch mediates ubiquitin-ligase activity by directly recruiting a ubiquitin-loaded ubiquitin-conjugating enzyme...
  29. ncbi request reprint Mechanism of ubiquitin recognition by the CUE domain of Vps9p
    Gali Prag
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA
    Cell 113:609-20. 2003
    ..Dimerization of the CUE domain allows both surfaces to contact a single ubiquitin molecule, providing a mechanism for high-affinity binding to monoubiquitin...
  30. pmc VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo
    Xuefeng Ren
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD, USA
    EMBO J 29:1045-54. 2010
    ..Mutational analysis of all the five ubiquitin-binding sites in yeast ESCRT-0 shows that cooperation between them is required for the sorting of the Lys63-linked polyubiquitinated cargo Cps1 to the vacuole...
  31. pmc A diacidic motif in human immunodeficiency virus type 1 Nef is a novel determinant of binding to AP-2
    O Wolf Lindwasser
    Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Building 18T, Room 101, National Institutes of Health, Bethesda, MD 20892, USA
    J Virol 82:1166-74. 2008
    ....
  32. pmc Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast
    Xuefeng Ren
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
    EMBO J 30:2130-9. 2011
    ..However, this site is non-essential for sorting of the ESCRT cargo Cps1. Taken together, these results show how a conserved motif/domain pair can evolve to use strikingly different binding modes in different organisms...
  33. ncbi request reprint Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3
    Gregory J Miller
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nat Struct Biol 10:599-606. 2003
    ....
  34. pmc Structural basis for viral late-domain binding to Alix
    Sangho Lee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health NIH, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nat Struct Mol Biol 14:194-9. 2007
    ..Overexpression of the V domain inhibits HIV-1 release from cells. This inhibition of release is reversed by mutations that block binding of the Alix V domain to p6...
  35. ncbi request reprint Structure of the ESCRT-II endosomal trafficking complex
    Aitor Hierro
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892 0580, USA
    Nature 431:221-5. 2004
    ..The structure suggests how ubiquitinated cargo could be passed between ESCRT components of the MVB pathway through the sequential transfer of ubiquitinated cargo from one complex to the next...
  36. pmc Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex
    Patricia V Burgos
    Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
    Dev Cell 18:425-36. 2010
    ....
  37. pmc Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor
    Silke Suer
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 100:4451-6. 2003
    ..We propose that the GAT domain is descended from the same ancestor as the syntaxin 1a N-terminal domain, and that both protein families share a common function in binding coiled-coil domain proteins...
  38. pmc Membrane scission by the ESCRT-III complex
    Thomas Wollert
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nature 458:172-7. 2009
    ..The minimum set of ESCRT-III and Vps4 proteins capable of multiple cycles of vesicle detachment corresponds to the ancient set of ESCRT proteins conserved from archaea to animals...
  39. pmc Structural basis for endosomal targeting by the Bro1 domain
    Jaewon Kim
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Dev Cell 8:937-47. 2005
    ..These results define a conserved mechanism whereby Bro1 domain-containing proteins are targeted to endosomes by Snf7 and its orthologs...
  40. pmc Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy
    Evzen Boura
    Laboratory of Molecular Biology and Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 108:9437-42. 2011
    ..These conformations provide reference points for the structural pathway by which ESCRT-I induces membrane buds...
  41. pmc Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B
    Dong Yang
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nat Struct Mol Biol 15:1278-86. 2008
    ..Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody and impair cytokinesis...
  42. pmc Dynamics of cholesterol exchange in the oxysterol binding protein family
    Bertram J Canagarajah
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    J Mol Biol 378:737-48. 2008
    ....
  43. pmc Structural mechanism for sterol sensing and transport by OSBP-related proteins
    Young Jun Im
    Laboratory of Molecular Biology, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nature 437:154-8. 2005
    ..On the basis of these observations, we propose a model in which sterol and membrane binding promote reciprocal conformational changes that facilitate a sterol transfer and signalling cycle...
  44. pmc Hybrid structural model of the complete human ESCRT-0 complex
    Xuefeng Ren
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA
    Structure 17:406-16. 2009
    ..Coarse-grained Monte Carlo simulations constrained by experimental RH values for ESCRT-0 reveal a dynamic ensemble of conformations well suited for diverse functions...
  45. pmc The clathrin adaptor complexes as a paradigm for membrane-associated allostery
    Bertram J Canagarajah
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Protein Sci 22:517-29. 2013
    ..The details of these mechanisms show how membrane docking and allosteric activation of AP complexes are intimately connected...
  46. pmc Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1
    Xuefeng Ren
    Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 152:755-67. 2013
    ..A third Arf1 interaction site near the N terminus of the γ subunit is important for recruitment, but not activation. These observations lead to a model for the recruitment and activation of AP-1 by Arf1...
  47. pmc SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis
    Benoît Renvoisé
    Cellular Neurology Unit, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke and Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Mol Biol Cell 21:3293-303. 2010
    ..These data suggest that Ist1 interaction is important for spartin recruitment to the midbody and that spartin participates in cytokinesis...
  48. pmc Structural basis for membrane targeting by the MVB12-associated β-prism domain of the human ESCRT-I MVB12 subunit
    Evzen Boura
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 109:1901-6. 2012
    ....
  49. ncbi request reprint Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase
    Gregory J Miller
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892 USA
    Mol Cell 15:703-11. 2004
    ..The unique helical domain of IP3K blocks access to the active site by membrane-bound phosphoinositides, explaining the structural basis for soluble inositol polyphosphate specificity...
  50. pmc Retromer
    Juan S Bonifacino
    Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, Building 18T Room 101, National Institutes of Health, Bethesda, MD 20892, USA
    Curr Opin Cell Biol 20:427-36. 2008
    ..Recent studies have implicated retromer in a broad range of physiological, developmental and pathological processes, underscoring the critical nature of retrograde transport mediated by this complex...
  51. pmc Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes
    Bartosz Różycki
    Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
    PLoS Comput Biol 8:e1002736. 2012
    ..Our membrane elasticity model thus sheds light on the energetics and possible mechanisms of ESCRT-induced membrane budding...
  52. pmc A HORMA domain in Atg13 mediates PI 3-kinase recruitment in autophagy
    Christine C Jao
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 110:5486-91. 2013
    ..These two Arg residues are essential for autophagy, suggesting that the Atg13 HORMA domain could function as a phosphoregulated conformational switch...
  53. pmc Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis
    Michael J Ragusa
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 151:1501-12. 2012
    ..The C-terminal EAT domain of Atg1 was shown to sense membrane curvature, dimerize, and tether lipid vesicles. These data suggest a structural mechanism for the organization of Atg9 vesicles into the early phagophore...
  54. ncbi request reprint Structure of a lipid droplet protein; the PAT family member TIP47
    Sabrina J Hickenbottom
    Laboratory of Cellular and Developmental Biology, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Structure 12:1199-207. 2004
    ..The structure suggests an analogy between PAT proteins and apolipoproteins in which helical repeats interact with lipid while the ordered C-terminal region is involved in protein:protein interactions...
  55. pmc Crystal structure and allosteric activation of protein kinase C βII
    Thomas A Leonard
    Laboratory of Molecular Biology, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 144:55-66. 2011
    ..Together, these results show how PKCβII is allosterically regulated in two steps, with the second step defining a novel protein kinase regulatory mechanism...
  56. pmc How Atg18 and the WIPIs sense phosphatidylinositol 3-phosphate
    Sulochanadevi Baskaran
    Laboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
    Autophagy 8:1851-2. 2012
    ..These three binding elements cooperate in function, as demonstrated by the incremental loss of function in Atg18 mutants impaired in combinations of the two phosphoinositide binding sites and the hydrophobic loop...
  57. pmc In vitro reconstitution of the ordered assembly of the endosomal sorting complex required for transport at membrane-bound HIV-1 Gag clusters
    Lars Anders Carlson
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 109:16928-33. 2012
    ..These findings define the minimal sets of components needed to complete ESCRT assembly at HIV-1 budding sites, and provide a starting point for in vitro structural and biophysical dissection of the system...
  58. ncbi request reprint Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains
    Saurav Misra
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 415:933-7. 2002
    ..The rigid spatial alignment of the three binding subsites leads to high specificity...
  59. pmc Structural role of the Vps4-Vta1 interface in ESCRT-III recycling
    Dong Yang
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
    Structure 18:976-84. 2010
    ..This suggests that Vta1 might not crosslink the two hexameric rings of Vps4, but rather stabilizes an array of Vps4-Vta1 complexes for ESCRT-III disassembly...
  60. ncbi request reprint Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
    Raymond C Trievel
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nat Struct Biol 10:545-52. 2003
    ..Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys...
  61. ncbi request reprint Endocytosis: driving membranes around the bend
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 111:143-6. 2002
    ..Structural analysis of the ENTH domain of the endocytic protein epsin has suggested a new mechanism, in which the ENTH domain pushes its way into membranes, thus bending them into shape...
  62. ncbi request reprint Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin
    Bertram Canagarajah
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA
    Cell 119:407-18. 2004
    ..Phospholipid binding to the C1 domain triggers the cooperative dissociation of these interactions, allowing the N terminus to move out of the active site and thereby activating the enzyme...
  63. pmc The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain
    Hang Shi
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
    Nat Struct Mol Biol 13:540-8. 2006
    ..Hydrophobic residues and a glycine in this loop are required for integration into the retromer complex and endosomal localization of human Vps26, and for the function of yeast Vps26 in carboxypeptidase Y sorting...
  64. pmc Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy
    Sulochanadevi Baskaran
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Mol Cell 47:339-48. 2012
    ..These observations thus provide a structural and mechanistic framework for one of the conserved central molecular recognition events in autophagy...
  65. pmc Proline-rich regions and motifs in trafficking: from ESCRT interaction to viral exploitation
    Xuefeng Ren
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Traffic 12:1282-90. 2011
    ..The known biology of PRM recognition in the ESCRT pathway seems, in principle, compatible with antiviral development, given our increasingly nuanced understanding of the relative weakness and robustness of the host and viral processes...
  66. pmc Regulation of protein kinases by lipids
    Thomas A Leonard
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Curr Opin Struct Biol 21:785-91. 2011
    ..Recently, structural studies on protein kinase C (PKC) have provided some of the first structural insights into the allosteric regulation of protein kinases by lipid second messengers...
  67. pmc Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission
    Natalie Elia
    Cell Biology and Metabolism Program, The Eunice Kennedy Shriver National Institute of Child Health and Development, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 108:4846-51. 2011
    ..That arrival of ESCRT-III and VPS4 correlates both spatially and temporally with the abscission event suggests a direct role for these proteins in cytokinetic membrane abscission...
  68. ncbi request reprint Structure and catalytic mechanism of a SET domain protein methyltransferase
    Raymond C Trievel
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 111:91-103. 2002
    ..The cofactor enters by a "back door" on the opposite side of the enzyme from substrate, promoting highly specific protein recognition and allowing addition of multiple methyl groups...
  69. pmc Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    Rittik Chaudhuri
    Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bldg 18T, Rm 101, National Institutes of Health, Bethesda, MD 20892, USA
    J Virol 81:3877-90. 2007
    ..Together, these results support a model in which HIV-1 Nef downregulates CD4 by promoting its accelerated endocytosis by a clathrin/AP2 pathway...
  70. ncbi request reprint Crystallization of the protein kinase Cdelta C1B domain
    Gongyi Zhang
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
    Methods Mol Biol 233:299-304. 2003
  71. pmc Two kinase family dramas
    Thomas A Leonard
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Cell 129:1037-8. 2007
    ..2007), this work highlights the diversity of mechanisms that nature has evolved within the kinase superfamily to regulate their activity through autoinhibition...
  72. pmc The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
    Timothy A Fritz
    Section on Biological Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 101:15307-12. 2004
    ....
  73. ncbi request reprint Structural genomics and signaling domains
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Trends Biochem Sci 27:48-53. 2002
    ..This article reviews the recent highlights of research on modular signaling domains, and the relative contributions and limitations of the various approaches being used...
  74. ncbi request reprint GAF domains: cyclic nucleotides come full circle
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0580, USA
    Sci STKE 2003:PE1. 2003
    ..Recent structural analysis of a cyclic GMP-binding GAF domain shows how conserved elements among the cyclic nucleotide-binding subgroup of GAF domains recognize the common chemical moieties in the two compounds...
  75. ncbi request reprint Structural analysis of protein kinase C: an introduction
    James H Hurley
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
    Methods Mol Biol 233:289-90. 2003
  76. pmc A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    Susan C Shih
    Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208 3500, USA
    EMBO J 22:1273-81. 2003
    ..Thus, we conclude that the CUE motif is an evolutionarily conserved monoubiquitin-binding domain that mediates intramolecular monoubiquitylation...
  77. pmc Phospholipase Cgamma/diacylglycerol-dependent activation of beta2-chimaerin restricts EGF-induced Rac signaling
    HongBin Wang
    Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104 6160, USA
    EMBO J 25:2062-74. 2006
    ..Our results represent the first direct evidence of divergence in DAG signaling downstream of a tyrosine-kinase receptor via a PKC-independent mechanism...
  78. ncbi request reprint An Alix fragment potently inhibits HIV-1 budding: characterization of binding to retroviral YPXL late domains
    Utpal M Munshi
    Virus Cell Interaction Section, HIV Drug Resistance Program, National Cancer Institute Frederick, Frederick, Maryland 21702 1201, USA
    J Biol Chem 282:3847-55. 2007
    ..This study identifies a novel Alix-derived dominant negative inhibitor of HIV-1 release and Gag processing and provides quantitative information on the interaction between Alix and viral late domains...
  79. ncbi request reprint Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2
    Yuling Chi
    Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA
    J Biol Chem 279:44987-95. 2004
    ....
  80. ncbi request reprint Normalization of nomenclature for peptide motifs as ligands of modular protein domains
    Rein Aasland
    Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway
    FEBS Lett 513:141-4. 2002
    ..This proposal will be reviewed in the future and will therefore be open for the inclusion of new rules, modifications and changes...
  81. ncbi request reprint Beyond Tsg101: the role of Alix in 'ESCRTing' HIV-1
    Ken Fujii
    Virus Cell Interaction Section, HIV Drug Resistance Program, National Cancer Institute, Frederick, Maryland 21702 1201, USA
    Nat Rev Microbiol 5:912-6. 2007
    ..Here, we focus on the use of host-cell factors during HIV-1 budding and highlight recent progress in our understanding of the role of one such factor, Alix, in both viral and cellular membrane budding and fission events...
  82. ncbi request reprint Polycistronic expression and purification of the ESCRT-II endosomal trafficking complex
    Aitor Hierro
    Methods Enzymol 403:322-32. 2005
    ....
  83. ncbi request reprint [3H]sildenafil binding to phosphodiesterase-5 is specific, kinetically heterogeneous, and stimulated by cGMP
    Jackie D Corbin
    Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, 702 Light Hall, Nashville, TN 37232 0615, USA
    Mol Pharmacol 63:1364-72. 2003
    ..The data also indicate that after physiological elevation, cGMP may directly stimulate the catalytic site by binding to the allosteric cGMP-binding sites of PDE5, thus causing negative feedback on this pathway...
  84. ncbi request reprint Leucine in the sky with diamonds
    James H Hurley
    Structure 11:1192-3. 2003