Mary Munson

Summary

Affiliation: University of Massachusetts Medical School
Country: USA

Publications

  1. ncbi request reprint The exocyst defrocked, a framework of rods revealed
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA
    Nat Struct Mol Biol 13:577-81. 2006
  2. ncbi request reprint To protect or reject
    Mary Munson
    Mary Munson is in the Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States
    elife 3:e03374. 2014
  3. pmc Conservation of helical bundle structure between the exocyst subunits
    Nicole J Croteau
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, United States of America
    PLoS ONE 4:e4443. 2009
  4. pmc Show me the MUN-y
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA
    Structure 19:1348-9. 2011
  5. ncbi request reprint A role for the syntaxin N-terminus
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Biochem J 418:e1-3. 2009
  6. pmc Watching proteins in motion
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01545, USA
    Genome Biol 10:316. 2009
  7. pmc Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
    Francesca Morgera
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Mol Biol Cell 23:337-46. 2012
  8. pmc Sec6p anchors the assembled exocyst complex at sites of secretion
    Jennifer A Songer
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Mol Biol Cell 20:973-82. 2009
  9. pmc The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p
    Melonnie L M Furgason
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Proc Natl Acad Sci U S A 106:14303-8. 2009
  10. ncbi request reprint Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p
    Mylavarapu V S Sivaram
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
    Biochemistry 44:6302-11. 2005

Collaborators

  • Nia J Bryant
  • Ming Li
  • Hiroshi Matsuo
  • Damien Devos
  • Reuben S Harris
  • Shigeki Miyamoto
  • Francesca Morgera
  • WILLIAM ROYER
  • Melonnie L M Furgason
  • Mylavarapu V S Sivaram
  • Margaret R Heider
  • Yibin Yang
  • Shivender M D Shandilya
  • Jennifer A Songer
  • Nicole J Croteau
  • Xiaojing Pan
  • Nicole Hermance
  • Fang Xia
  • Sarah Morrissey
  • Michelle A Kelliher
  • Angela Mabb
  • Pallavi Gandhi
  • Sara Simonson
  • Elena Harjes
  • Mohan Somasundaran
  • Ellen A Nalivaika
  • Celia A Schiffer
  • Phillip J Gross
  • Keisuke Shindo
  • Madhavi N L Nalam
  • Johnathan C Valesano
  • Takahide Kono
  • Scott G Shanks
  • Chris MacDonald
  • Sean P Ryder
  • Daniel N Brewer
  • David G Lambright
  • Sudharshan Eathiraj
  • Jennifer A Saporita
  • Angela J Boettcher

Detail Information

Publications15

  1. ncbi request reprint The exocyst defrocked, a framework of rods revealed
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA
    Nat Struct Mol Biol 13:577-81. 2006
    ..These rods may pack against one another to generate the framework of the complex. How this complex assembles, how it responds to various GTPases and how it is ultimately displaced to allow bilayer fusion are key questions for the future...
  2. ncbi request reprint To protect or reject
    Mary Munson
    Mary Munson is in the Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States
    elife 3:e03374. 2014
    ..A protein known for its role in dismantling faulty SNARE complexes can also help to maintain complexes that have formed properly during membrane fusion. ..
  3. pmc Conservation of helical bundle structure between the exocyst subunits
    Nicole J Croteau
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, United States of America
    PLoS ONE 4:e4443. 2009
    ..Characterization of several of these subunits has been hindered by lack of soluble protein for biochemical and structural studies...
  4. pmc Show me the MUN-y
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA
    Structure 19:1348-9. 2011
    ..The structure of the MUN domain of the synaptic protein Munc13-1 by Li et al., in this issue of Structure, shows that seemingly disparate regulators of SNARE-mediated membrane fusion are highly conserved at the structural level...
  5. ncbi request reprint A role for the syntaxin N-terminus
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Biochem J 418:e1-3. 2009
    ....
  6. pmc Watching proteins in motion
    Mary Munson
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01545, USA
    Genome Biol 10:316. 2009
    ..A report of the 23rd Protein Symposium 'Proteins in Motion', Boston, USA, 23-27 July 2009...
  7. pmc Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
    Francesca Morgera
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Mol Biol Cell 23:337-46. 2012
    ..Therefore, upon vesicle arrival, Sec6 is proposed to release Sec9 in favor of Sec6-exocyst assembly and to simultaneously recruit Sec1 to sites of secretion for coordinated SNARE complex formation and membrane fusion...
  8. pmc Sec6p anchors the assembled exocyst complex at sites of secretion
    Jennifer A Songer
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Mol Biol Cell 20:973-82. 2009
    ..Our results indicate that assembly and polarization of the exocyst are functionally separable events, and that Sec6p is required to anchor exocyst complexes at sites of secretion...
  9. pmc The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p
    Melonnie L M Furgason
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Proc Natl Acad Sci U S A 106:14303-8. 2009
    ..Furthermore, the Tlg2p N-peptide competes with the closed conformation for binding, suggesting a fundamental regulatory mechanism for SM-syntaxin interactions in SNARE assembly and membrane fusion...
  10. ncbi request reprint Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p
    Mylavarapu V S Sivaram
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
    Biochemistry 44:6302-11. 2005
    ..This direct interaction between the exocyst complex and the t-SNARE implicates the exocyst in SNARE complex regulation...
  11. ncbi request reprint The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
    Mylavarapu V S Sivaram
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA
    Nat Struct Mol Biol 13:555-6. 2006
    ..The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins...
  12. pmc Exorcising the exocyst complex
    Margaret R Heider
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA
    Traffic 13:898-907. 2012
    ..In this review, we discuss current knowledge of exocyst architecture, assembly, regulation and its roles in a variety of cellular trafficking pathways...
  13. pmc Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces
    Shivender M D Shandilya
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    Structure 18:28-38. 2010
    ..NMR solution data provides evidence that another interface, which coordinates a novel zinc site, also exists. Thus, the observed crystallographic interfaces of APOBEC3G may be important for both oligomerization and function...
  14. ncbi request reprint TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
    Xiaojing Pan
    Program in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, UMass Medical School, Two Biotech, 373 Plantation Street, Worcester, Massachusetts 01605, USA
    Nature 442:303-6. 2006
    ..Strong conservation of both catalytic fingers indicates that most TBC-domain GAPs may accelerate GTP hydrolysis by a similar dual-finger mechanism...
  15. pmc A cytosolic ATM/NEMO/RIP1 complex recruits TAK1 to mediate the NF-kappaB and p38 mitogen-activated protein kinase (MAPK)/MAPK-activated protein 2 responses to DNA damage
    Yibin Yang
    Departments of Cancer Biology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA
    Mol Cell Biol 31:2774-86. 2011
    ..These findings have translational implications and reveal RIP1 and TAK1 as potential therapeutic targets in chemoresistance...