Research Topics
Genomes and Genes | Mary MunsonSummaryAffiliation: University of Massachusetts Medical School Country: USA Publications
Research Grants
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Detail Information
Publications
The exocyst defrocked, a framework of rods revealedMary 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...
A role for the syntaxin N-terminusMary Munson
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA
Biochem J 418:e1-3. 2009....
Show me the MUN-yMary 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...
Watching proteins in motionMary 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...
Sec6p anchors the assembled exocyst complex at sites of secretionJennifer 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...
The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45pMelonnie 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...
Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1Francesca 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...
Conservation of helical bundle structure between the exocyst subunitsNicole 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...
The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse rolesMylavarapu 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...
Exorcising the exocyst complexMargaret 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...
Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfacesShivender 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...
TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanismXiaojing 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...
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 damageYibin 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...
Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9pMylavarapu 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...
Research Grants
- Structure and Function of the Exocyst ComplexMary Munson; Fiscal Year: 2009..Because these proteins are conserved from yeast to human neurons, this research will advance our knowledge of how secretion and growth are regulated in all eukaryotic cells. ..
- Structure and Function of the Exocyst ComplexMary Munson; Fiscal Year: 2010..In addition, our research will also lead to the development of many constructs, reagents and ideas that will be valuable tools for studying how the exocyst complex regulates secretion in all eukaryotic cells. ..
