molecular chaperones

Summary

Summary: A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.

Top Publications

  1. Burkinshaw B, Strynadka N. Assembly and structure of the T3SS. Biochim Biophys Acta. 2014;1843:1649-63 pubmed publisher
    ..This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. ..
  2. Cuervo A, Wong E. Chaperone-mediated autophagy: roles in disease and aging. Cell Res. 2014;24:92-104 pubmed publisher
  3. Rajendran A, Endo M, Hidaka K, Tran P, Mergny J, Gorelick R, et al. HIV-1 nucleocapsid proteins as molecular chaperones for tetramolecular antiparallel G-quadruplex formation. J Am Chem Soc. 2013;135:18575-85 pubmed publisher
  4. Bichel K, Price A, Schaller T, Towers G, Freund S, James L. HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358. Retrovirology. 2013;10:81 pubmed publisher
    ..Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating. ..
  5. Doyle S, Genest O, Wickner S. Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol. 2013;14:617-29 pubmed publisher
    Protein quality control within the cell requires the interplay of many molecular chaperones and proteases. When this quality control system is disrupted, polypeptides follow pathways leading to misfolding, inactivity and aggregation...
  6. Patil S, Tran N, Geekiyanage H, Liu L, Chan C. Curcumin-induced upregulation of the anti-tau cochaperone BAG2 in primary rat cortical neurons. Neurosci Lett. 2013;554:121-5 pubmed publisher
    ..The present results demonstrate novel activity of polyphenol curcumin in up-regulating an anti-tau cochaperone BAG2 and thus, suggest probable benefit of curcumin against AD-associated tauopathy. ..
  7. Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Morera S, et al. High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex. Structure. 2013;21:1834-47 pubmed publisher
    ..The Tah1 C-terminal region is unfolded, and we demonstrate that it is essential for the recruitment of the Pih1 C-terminal domain and folds upon binding...
  8. Folwarczna J, Moravec T, Plchova H, Hoffmeisterova H, Cerovska N. Efficient expression of Human papillomavirus 16 E7 oncoprotein fused to C-terminus of Tobacco mosaic virus (TMV) coat protein using molecular chaperones in Escherichia coli. Protein Expr Purif. 2012;85:152-7 pubmed publisher
    ..To increase the ratio of soluble protein various molecular chaperones (TF, DnaK-DnaJ-GrpE, GroEL-GroES) were used...
  9. Kud J, Zhao Z, Du X, Liu Y, Zhao Y, Xiao F. SGT1 interacts with the Prf resistance protein and is required for Prf accumulation and Prf-mediated defense signaling. Biochem Biophys Res Commun. 2013;431:501-5 pubmed publisher
    ..tomato (Pst). These results suggest that, in both N. benthamiana and tomato, SGT1 contributes to the Prf-mediated defense responses by stabilizing Prf protein via its co-chaperone activity...

Scientific Experts

More Information

Publications62

  1. Cloutier P, Lavallée Adam M, Faubert D, Blanchette M, Coulombe B. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 2013;9:e1003210 pubmed publisher
    ..Overall, this report uncovers a new role for protein methylation as a regulatory pathway for molecular chaperones and defines a novel regulatory mechanism for the chaperone VCP, whose deregulation is causative of ..
  2. Siekierska A, De Baets G, Reumers J, Gallardo R, Rudyak S, Broersen K, et al. ?-Galactosidase aggregation is a determinant of pharmacological chaperone efficacy on Fabry disease mutants. J Biol Chem. 2012;287:28386-97 pubmed publisher
    ..g. via proteostatic regulator compounds that increase cellular chaperone expression...
  3. Tammineni P, Anugula C, Mohammed F, Anjaneyulu M, Larner A, Sepuri N. The import of the transcription factor STAT3 into mitochondria depends on GRIM-19, a component of the electron transport chain. J Biol Chem. 2013;288:4723-32 pubmed publisher
    ..A S727A mutation in STAT3 reduces its import and assembly even in the presence of GRIM-19. Together, our studies unveil a novel chaperone function for GRIM-19 in the recruitment of STAT3 into mitochondria. ..
  4. Orenstein S, Kuo S, Tasset I, Arias E, Koga H, Fernandez Carasa I, et al. Interplay of LRRK2 with chaperone-mediated autophagy. Nat Neurosci. 2013;16:394-406 pubmed publisher
    ..This newly described LRRK2 self-perpetuating inhibitory effect on CMA could underlie toxicity in Parkinson's disease by compromising the degradation of ?-synuclein, another Parkinson's disease-related protein degraded by this pathway. ..
  5. Calloni G, Chen T, Schermann S, Chang H, Genevaux P, Agostini F, et al. DnaK functions as a central hub in the E. coli chaperone network. Cell Rep. 2012;1:251-64 pubmed publisher
    ..Combined loss of DnaK and TF causes proteostasis collapse with disruption of GroEL function, defective ribosomal biogenesis, and extensive aggregation of large proteins. ..
  6. Locascio A, Blázquez M, Alabadi D. Dynamic regulation of cortical microtubule organization through prefoldin-DELLA interaction. Curr Biol. 2013;23:804-9 pubmed publisher
  7. Li K, Jiang T, Yu B, Wang L, Gao C, Ma C, et al. Transcription elongation factor GreA has functional chaperone activity. PLoS ONE. 2012;7:e47521 pubmed publisher
    ..These facts reveal that GreA has chaperone activity. Distinct from many molecular chaperones, GreA does not form stable complexes with unfolded substrates...
  8. Mahadevan K, Zhang H, Akef A, Cui X, Gueroussov S, Cenik C, et al. RanBP2/Nup358 potentiates the translation of a subset of mRNAs encoding secretory proteins. PLoS Biol. 2013;11:e1001545 pubmed publisher
    ..ALREX-elements thus act as nucleotide platforms to coordinate various steps of post-transcriptional regulation for the majority of mRNAs that encode secreted proteins. ..
  9. Boyd R, Lee G, Rybczynski P, Benjamin E, Khanna R, Wustman B, et al. Pharmacological chaperones as therapeutics for lysosomal storage diseases. J Med Chem. 2013;56:2705-25 pubmed publisher
    ..In this Perspective, we review several of the lysosomal diseases for which PCs have been studied and the SAR of the various classes of molecules. ..
  10. Vavassori S, Cortini M, Masui S, Sannino S, Anelli T, Caserta I, et al. A pH-regulated quality control cycle for surveillance of secretory protein assembly. Mol Cell. 2013;50:783-92 pubmed publisher
    ..The ERp44 assembly control cycle couples secretion fidelity and efficiency downstream of the calnexin/calreticulin and BiP-dependent quality control cycles. ..
  11. Kovacs D, Tompa P. Diverse functional manifestations of intrinsic structural disorder in molecular chaperones. Biochem Soc Trans. 2012;40:963-8 pubmed
  12. Moon C, Zaccai N, Fleming P, Gessmann D, Fleming K. Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm. Proc Natl Acad Sci U S A. 2013;110:4285-90 pubmed publisher
    ..Binding free energies of these outer membrane proteins with periplasmic chaperones support this energy sink hypothesis...
  13. Yang C, Rahimpour S, Lu J, Pacak K, Ikejiri B, Brady R, et al. Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones. Proc Natl Acad Sci U S A. 2013;110:966-71 pubmed publisher
    ..These findings provide insight into a possible therapeutic strategy for Gaucher disease and other genetic disorders by modifying molecular chaperone and protein degradation pathways. ..
  14. Cui T, Smith P, Fox J, Khalimonchuk O, Winge D. Late-stage maturation of the Rieske Fe/S protein: Mzm1 stabilizes Rip1 but does not facilitate its translocation by the AAA ATPase Bcs1. Mol Cell Biol. 2012;32:4400-9 pubmed publisher
    ..However, the Rip1 variants were not stably associated with the supercomplex. The induced supercomplex stabilization by the Rip1 N terminus was independent of Mzm1. ..
  15. Jansen G, Maattanen P, Denisov A, Scarffe L, Schade B, Balghi H, et al. An interaction map of endoplasmic reticulum chaperones and foldases. Mol Cell Proteomics. 2012;11:710-23 pubmed publisher
  16. Xue Y, Kowalska A, Grabowska K, Przybyt K, Cichewicz M, Del Rosario B, et al. Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol Cell Biol. 2013;33:1645-56 pubmed publisher
    ..This work sheds further light on the importance of histone chaperones as general regulators of transcription elongation. ..
  17. Leznicki P, High S. SGTA antagonizes BAG6-mediated protein triage. Proc Natl Acad Sci U S A. 2012;109:19214-9 pubmed publisher
    ..We speculate that a BAG6/SGTA cycle operates during protein maturation and quality control in the cytosol and that together these components dictate the fate of a specific subset of newly synthesized proteins. ..
  18. Numata Y, Morimura T, Nakamura S, Hirano E, Kure S, Goto Y, et al. Depletion of molecular chaperones from the endoplasmic reticulum and fragmentation of the Golgi apparatus associated with pathogenesis in Pelizaeus-Merzbacher disease. J Biol Chem. 2013;288:7451-66 pubmed publisher
    ..We propose that depletion of ER chaperones and GA fragmentation induced by mutant misfolded proteins contribute to the pathogenesis of inherited ER stress-related diseases and affect the disease severity...
  19. Malinovska L, Kroschwald S, Munder M, Richter D, Alberti S. Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol Biol Cell. 2012;23:3041-56 pubmed publisher
    ..the subcellular distribution of misfolded proteins as a function of the cytosolic concentrations of molecular chaperones and protein-sorting factors...
  20. Winkler J, Tyedmers J, Bukau B, Mogk A. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol. 2012;198:387-404 pubmed publisher
    ..Our findings indicate a conserved mechanism of Hsp70-Hsp100 cooperation at the surface of protein aggregates and prion fibrils. ..
  21. Kim Y, Hipp M, Bracher A, Hayer Hartl M, Hartl F. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem. 2013;82:323-55 pubmed publisher
    ..of proteome integrity, and protein homeostasis (proteostasis) critically depend on a complex network of molecular chaperones. Disruption of proteostasis is implicated in aging and the pathogenesis of numerous degenerative diseases...
  22. Germain D, Giugliani R, Hughes D, Mehta A, Nicholls K, Barisoni L, et al. Safety and pharmacodynamic effects of a pharmacological chaperone on ?-galactosidase A activity and globotriaosylceramide clearance in Fabry disease: report from two phase 2 clinical studies. Orphanet J Rare Dis. 2012;7:91 pubmed publisher
    ..It enhanced ?-Gal A activity and resulted in GL-3 substrate decrease in patients with responsive GLA mutations. Phase 3 studies are ongoing. ..
  23. Kirstein Miles J, Scior A, Deuerling E, Morimoto R. The nascent polypeptide-associated complex is a key regulator of proteostasis. EMBO J. 2013;32:1451-68 pubmed publisher
  24. Cho K, Searle K, Webb M, Yi H, Ferreira P. Ranbp2 haploinsufficiency mediates distinct cellular and biochemical phenotypes in brain and retinal dopaminergic and glia cells elicited by the Parkinsonian neurotoxin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Cell Mol Life Sci. 2012;69:3511-27 pubmed publisher
  25. Voos W. Chaperone-protease networks in mitochondrial protein homeostasis. Biochim Biophys Acta. 2013;1833:388-99 pubmed publisher
    ..This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids. ..
  26. Schreiner M, Niemann H. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Struct Biol. 2012;12:13 pubmed publisher
  27. Chambers J, Petrova K, Tomba G, Vendruscolo M, Ron D. ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load. J Cell Biol. 2012;198:371-85 pubmed publisher
    ..A kinetic model showed that buffering fluctuations in unfolded protein load with a recruitable pool of inactive chaperone is an efficient strategy to minimize both aggregation and costly degradation of unfolded proteins. ..
  28. Xu W, Mollapour M, Prodromou C, Wang S, Scroggins B, Palchick Z, et al. Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine. Mol Cell. 2012;47:434-43 pubmed publisher
    ..Finally, at completion of the chaperone cycle, Hsp90 Y627 phosphorylation induces dissociation of the client and remaining cochaperones. ..
  29. Venkatesh S, Smolle M, Li H, Gogol M, Saint M, Kumar S, et al. Set2 methylation of histone H3 lysine?36 suppresses histone exchange on transcribed genes. Nature. 2012;489:452-5 pubmed publisher
    ..By suppressing spurious cryptic transcripts from initiating within ORFs, this pathway is essential to maintain the accuracy of transcription by RNA polymerase?II. ..
  30. Yang Z, Hong J, Derkatch I, Liebman S. Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability. PLoS Genet. 2013;9:e1003236 pubmed publisher
    ..Thus, a mechanism by which heterologous Q/N-rich proteins impair prion propagation appears to be the loss of cytoplasmic Hsp104 and Sis1 available to sever [PSI(+)]. ..
  31. Dimant H, Ebrahimi Fakhari D, McLean P. Molecular chaperones and co-chaperones in Parkinson disease. Neuroscientist. 2012;18:589-601 pubmed publisher
    ..b>Molecular chaperones, molecules that can mediate the proper folding and refolding of client proteins, are vital to cell function ..
  32. Dow J, Gabel F, Sargent F, Palmer T. Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway. Biochem J. 2013;452:57-66 pubmed publisher
    ..It is possible that correct folding of Domain IV upon cofactor loading is the trigger for TorD release and subsequent export of TorA. ..
  33. Lee K, Hong T, Hahn J. Roles of 17-AAG-induced molecular chaperones and Rma1 E3 ubiquitin ligase in folding and degradation of Pendrin. FEBS Lett. 2012;586:2535-41 pubmed publisher
    ..facilitates the folding of Pendrin through heat shock transcription factor 1 (Hsf1)-dependent induction of molecular chaperones. Furthermore, we demonstrate that Rma1, an E3 ubiquitin ligase localized in the ER membrane, is involved in ..
  34. Kassube S, Stuwe T, Lin D, Antonuk C, Napetschnig J, Blobel G, et al. Crystal structure of the N-terminal domain of Nup358/RanBP2. J Mol Biol. 2012;423:752-65 pubmed publisher
    ..Together, these data suggest that the NTD contributes to mRNP remodeling events at the cytoplasmic face of the NPC. ..
  35. Kästle M, Grune T. Interactions of the proteasomal system with chaperones: protein triage and protein quality control. Prog Mol Biol Transl Sci. 2012;109:113-60 pubmed publisher
    ..Failure of one of the systems can be compensated partially by the upregulation of the other. Nevertheless, prolonged failure of the proteasome or chaperones results in protein aggregation and cellular dysfunction. ..
  36. Baker B, Nargund A, Sun T, Haynes C. Protective coupling of mitochondrial function and protein synthesis via the eIF2? kinase GCN-2. PLoS Genet. 2012;8:e1002760 pubmed publisher
    ..These findings are consistent with translational control and stress-dependent chaperone induction acting in complementary arms of the UPR(mt)...
  37. Sanchez E, Lobo T, Fox J, Zeviani M, Winge D, Fernandez Vizarra E. LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial Complex III assembly in human cells. Biochim Biophys Acta. 2013;1827:285-93 pubmed publisher
    ..Thus, LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1 insertion step, which enables formation of the mature and functional CIII enzyme. ..
  38. Samuel P, Prasanna Vadhana A, Kamatchi R, Antony A, Meenakshisundaram S. Effect of molecular chaperones on the expression of Candida antarctica lipase B in Pichia pastoris. Microbiol Res. 2013;168:615-20 pubmed publisher
    ..From these results, we conclude that overexpression of Kar2p is not required for the secretion of CalB. Also, our work confirmed the synergistic effect of Ssa1p and Ydj1p chaperones in the expression of CalB...
  39. Cammisa M, Correra A, Andreotti G, Cubellis M. Fabry_CEP: a tool to identify Fabry mutations responsive to pharmacological chaperones. Orphanet J Rare Dis. 2013;8:111 pubmed publisher
    ..In the absence of experimental data structural, functional and evolutionary analysis provides a prediction and the probability that a given mutation is responsive to the drug. ..
  40. Vincent C, Friedman J, Jeong K, Sutherland M, Vogel J. Identification of the DotL coupling protein subcomplex of the Legionella Dot/Icm type IV secretion system. Mol Microbiol. 2012;85:378-91 pubmed publisher
    ..Thus, in addition to their role as chaperones for Legionella type IV secretion system substrates, IcmS and IcmW perform a second function as part of the Dot/Icm type IV coupling protein subcomplex. ..
  41. Culjkovic Kraljacic B, Baguet A, Volpon L, Amri A, Borden K. The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation. Cell Rep. 2012;2:207-15 pubmed publisher
    ..eIF4E overcomes this inhibitory mechanism by indirectly reducing levels of RanBP2. More generally, these results suggest that reprogramming the NPC is a means by which oncogenes can harness the proliferative capacity of the cell. ..
  42. Carranza G, Castaño R, Fanarraga M, Villegas J, Goncalves J, Soares H, et al. Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics. Cell Mol Life Sci. 2013;70:357-71 pubmed publisher
    ..TBCB is also able to bind to the chaperonin complex CCT containing ?-tubulin, suggesting that it could escort tubulin to facilitate its folding and dimerization, recycling or degradation. ..
  43. Kishor A, Tandukar B, Ly Y, Toth E, Suarez Y, Brewer G, et al. Hsp70 is a novel posttranscriptional regulator of gene expression that binds and stabilizes selected mRNAs containing AU-rich elements. Mol Cell Biol. 2013;33:71-84 pubmed publisher
  44. Rallis A, Lu B, Ng J. Molecular chaperones protect against JNK- and Nmnat-regulated axon degeneration in Drosophila. J Cell Sci. 2013;126:838-49 pubmed publisher
    ..These results suggest that molecular chaperones are key in JNK- and Nmnat-regulated axonal protective functions.
  45. Warner Schmidt J, Schmidt E, Marshall J, Rubin A, Arango Lievano M, Kaplitt M, et al. Cholinergic interneurons in the nucleus accumbens regulate depression-like behavior. Proc Natl Acad Sci U S A. 2012;109:11360-5 pubmed publisher
  46. Li J, Richter K, Reinstein J, Buchner J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat Struct Mol Biol. 2013;20:326-31 pubmed publisher
    ..Thus, at distinct steps during the Hsp90 chaperone cycle, co-chaperones selectively trap statistically distributed Hsp90 conformers and thus turn Hsp90 into a deterministic machine. ..
  47. Garcia Carbonero R, Carnero A, Paz Ares L. Inhibition of HSP90 molecular chaperones: moving into the clinic. Lancet Oncol. 2013;14:e358-69 pubmed publisher
    ..We also discuss novel strategies and future perspectives on how to optimise the therapeutic potential of this exciting new class of drugs. ..
  48. Srinivasan S, Gillies A, Chang L, Thompson A, Gestwicki J. Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome. Mol Biosyst. 2012;8:2323-33 pubmed publisher
    In Escherichia coli, the molecular chaperones DnaK and DnaJ cooperate to assist the folding of newly synthesized or unfolded polypeptides. DnaK and DnaJ bind to hydrophobic motifs in these proteins and they also bind to each other...
  49. Lin D, Zimmermann S, Stuwe T, Stuwe E, Hoelz A. Structural and functional analysis of the C-terminal domain of Nup358/RanBP2. J Mol Biol. 2013;425:1318-29 pubmed publisher
    ..However, we demonstrate that the CTD is dispensable for nuclear envelope localization of Nup358, suggesting that the CTD does not interact with other nucleoporins. ..
  50. Lyu Z, Shao Q, Gao Y, Zhao X. Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp. PLoS ONE. 2012;7:e46068 pubmed publisher
  51. Burmann B, Hiller S. Solution NMR studies of membrane-protein-chaperone complexes. Chimia (Aarau). 2012;66:759-63 pubmed publisher
    The biosynthesis of the bacterial outer membrane depends on molecular chaperones that protect hydrophobic membrane proteins against aggregation while transporting them across the periplasm...
  52. Kuang Y, Charette N, Frazer J, Holland P, Attwood K, Dellaire G, et al. Dopamine receptor-interacting protein 78 acts as a molecular chaperone for CCR5 chemokine receptor signaling complex organization. PLoS ONE. 2012;7:e40522 pubmed publisher
    ..Our results demonstrate that modulation of the functions of a chaperone can affect signal transduction at the cell surface. ..
  53. Di Nunzio F, Danckaert A, Fricke T, Perez P, Fernandez J, Perret E, et al. Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration. PLoS ONE. 2012;7:e46037 pubmed publisher
    ..Our work shows the involvement of nucleoporins in diverse and functionally separable steps of HIV infection and nuclear import. ..