Mary Munson PhD
Title | Professor |
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Institution | University of Massachusetts Medical School |
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Department | Biochemistry and Molecular Pharmacology |
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Address | University of Massachusetts Medical School 364 Plantation Street, LRB Worcester MA 01605
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Phone | 508-856-8318 |
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vCard | Download vCard |
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Institution | UMMS - School of Medicine |
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Department | Biochemistry and Molecular Pharmacology |
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Institution | UMMS - School of Medicine |
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Department | NeuroNexus Institute |
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Institution | UMMS - Graduate School of Biomedical Sciences |
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Department | Biochemistry and Molecular Pharmacology |
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Institution | UMMS - Graduate School of Biomedical Sciences |
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Department | Cell Biology |
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Institution | UMMS - Graduate School of Biomedical Sciences |
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Department | Interdisciplinary Graduate Program |
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Institution | UMMS - Graduate School of Biomedical Sciences |
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Department | Translational Science |
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Biography Washington University in St Louis, Saint Louis, MO, United States | AB | | Chemistry & Biology | Yale University, New Haven, CT, United States | PHD | | Molecular Biophysics & Biochem |
Overview Academic BackgroundMary Munson was a double major in Chemistry and Biology at Washington University(St. Louis), receiving her bachelor's degree in 1989. In 1996, she received her Ph.D.from Yale University in Molecular Biophysics and Biochemistry. She was a postdoctoral fellow in the Department of Molecular Biology at Princeton University, where she was awarded both American Heart Association and NIH postdoctoral fellowships. She joined the faculty of Biochemistry and Molecular Pharmacology in 2001. Regulation of vesicle targeting and fusionVesicle targeting and fusion are tightly regulated processes used by eukaryotic cells to transport cargo between membrane-bound subcellular compartments and to the plasma membrane for secretion. The proper function and specificity of these processes are crucial for maintenance of cellular integrity, normal growth, and for intercellular signaling events, such as neurotransmission. We are interested in understanding the mechanistic basis for regulation of the spatial and temporal specificity of vesicle fusion, at the correct site on the target membrane. Many questions remain to be answered. For example, what marks the site of fusion on the target membrane? What checks to make sure that the correct vesicle docks at the right place? How are the membrane fusion proteins regulated to ensure that the wrong vesicle does not fuse? Our aim is to answer questions such as these through a multifaceted approach that combines biochemical, structural and biophysical techniques with yeast genetics, microscopy and cell biological methods. We are investigating proteins that regulate exocytosis in the model organism Saccharomyces cerevisiae. Because these proteins are conserved from yeast to man, these studies will advance our understanding of how secretion is regulated in all eukaryotic cells.Our ResearchOur investigations mainly focus on the Exocyst complex (Fig. 1), a protein complex essential for vesicle trafficking (exocytosis) in all eukaryotes. The proteins that form the Exocyst complex localize to secretory vesicles and to sites of active secretion at bud tips and mother-bud necks. These proteins are essential for cell viability, show physical and genetic interactions with the the membrane fusion proteins (SNAREs) and with each other, and their temperature-sensitive mutants have secretory blocks and accumulate secretory vesicles. Our research has several aims: 1) biophysical and structural studies of the Exocyst proteins and their interactions with each other; 2) creation and testing of mutants in vivo, in order to elucidate the functions of the Exocyst proteins; 3) characterization of interactions between the Exocyst and other proteins required for exocytosis, such as the SNARE proteins, and regulators such as Sec1p and the small Rab GTPase Sec4p; and 4) genetic and proteomic identification of novel regulators of exocytosis and SNARE complex assembly. Additionally, we are characterizing the regulation of endocytosis by the Sec1-homolog Vps45p, through its interactions with the endosomal SNARE proteins. Figure 1.Current model for the architecture of the exocyst complex  Potential Rotation ProjectsResearch in the Munson lab is focused on biochemical/biophysical and cell biological characterization of proteins in the exocyst complex. Potential rotation projects include the following: Cloning of various exocyst protein domains and point mutations. These will be expressed in E. coli for biochemical/structural studies, and their functions tested in yeast.
Protein expression and purification. Develop purification strategies for several exocyst proteins and their domains, using chromatography methods such as ion exchange and gel filtration (Fig. 2).
Characterization of the purified exocyst proteins. Protein structure, stability, oligomerization state and protein:protein interactions will be monitored by such techniques as circular dichroism, analytical ultracentrifugation and gel filtration (Fig. 3).
Crystallography. We have determined the structure of the C-terminal domain of Sec6p (Fig. 4). Crystallization trials ofotherexocyst proteins and their domains are in progress.
Design and test functional exocyst mutants in yeast. Mutants will be characterized using a variety of biochemical, cell biological, and microscopic techniques.
Identify novel regulators of yeast exocytosis using a genetic screen. Mutants created in these screens are currently being tested and identified (Fig. 5). Their role in exocytosis will be explored

 
Bibliographic
Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications.
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Hakhverdyan Z, Molloy KR, Keegan S, Herricks T, Lepore DM, Munson M, Subbotin RI, Fenyö D, Aitchison JD, Fernandez-Martinez J, Chait BT, Rout MP. Dissecting the Structural Dynamics of the Nuclear Pore Complex. Mol Cell. 2020 Dec 08. PMID: 33333016.
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Orr RG, Furt F, Warner EL, Agar EM, Garbarino JM, Cabral SE, Dubuke ML, Butt AM, Munson M, Vidali L. Rab-E and its interaction with myosin XI are essential for polarized cell growth. New Phytol. 2020 Oct 23. PMID: 33098085.
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Munson M. Introduction. Protein Sci. 2020 May 19. PMID: 32428283.
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Martínez-Núñez L, Munson M. Retro Is Cool: Structure of the Versatile Retromer Complex. Structure. 2020 Apr 07; 28(4):387-389. PMID: 32268076.
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Ganesan SJ, Feyder MJ, Chemmama IE, Fang F, Rout MP, Chait BT, Shi Y, Munson M, Sali A. Integrative Structure and Function of the Yeast Exocyst Complex. Protein Sci. 2020 Apr 02. PMID: 32239688.
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Miaczynska M, Munson M. Membrane trafficking: vesicle formation, cargo sorting and fusion. Mol Biol Cell. 2020 Mar 15; 31(6):399-400. PMID: 32163346.
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Rossi G, Lepore D, Kenner L, Czuchra AB, Plooster M, Frost A, Munson M, Brennwald P. Exocyst structural changes associated with activation of tethering downstream of Rho/Cdc42 GTPases. J Cell Biol. 2020 Feb 03; 219(2). PMID: 31904797.
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Lepore DM, Martínez-Núñez L, Munson M. Exposing the Elusive Exocyst Structure. Trends Biochem Sci. 2018 Jul 25. PMID: 30055895.
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Yoon TY, Munson M. SNARE complex assembly and disassembly. Curr Biol. 2018 Apr 23; 28(8):R397-R401. PMID: 29689222.
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Parchure A, Munson M, Budnik V. Getting mRNA-Containing Ribonucleoprotein Granules Out of a Nuclear Back Door. Neuron. 2017 Nov 01; 96(3):604-615. PMID: 29096075.
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Boehm CM, Obado S, Gadelha C, Kaupisch A, Manna PT, Gould GW, Munson M, Chait BT, Rout MP, Field MC. The Trypanosome Exocyst: A Conserved Structure Revealing a New Role in Endocytosis. PLoS Pathog. 2017 Jan; 13(1):e1006063. PMID: 28114397.
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Dubuke ML, Munson M. The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation. Front Cell Dev Biol. 2016; 4:42. PMID: 27243006.
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Heider MR, Gu M, Duffy CM, Mirza AM, Marcotte LL, Walls AC, Farrall N, Hakhverdyan Z, Field MC, Rout MP, Frost A, Munson M. Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex. Nat Struct Mol Biol. 2016 Jan; 23(1):59-66. PMID: 26656853.
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Bombardier JP, Munson M. Three steps forward, two steps back: mechanistic insights into the assembly and disassembly of the SNARE complex. Curr Opin Chem Biol. 2015 Dec; 29:66-71. PMID: 26498108.
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Dubuke ML, Maniatis S, Shaffer SA, Munson M. The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes. J Biol Chem. 2015 Nov 20; 290(47):28245-56. PMID: 26446795.
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Munson M. Synaptic-vesicle fusion: a need for speed. Nat Struct Mol Biol. 2015 Jul; 22(7):509-11. PMID: 26150331.
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Munson M. To protect or reject. Elife. 2014; 3:e03374. PMID: 24940001.
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Heider MR, Munson M. Exorcising the exocyst complex. Traffic. 2012 Jul; 13(7):898-907. PMID: 22420621.
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Jin Y, Sultana A, Gandhi P, Franklin E, Hamamoto S, Khan AR, Munson M, Schekman R, Weisman LS. Myosin V transports secretory vesicles via a Rab GTPase cascade and interaction with the exocyst complex. Dev Cell. 2011 Dec 13; 21(6):1156-70. PMID: 22172676.
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Morgera F, Sallah MR, Dubuke ML, Gandhi P, Brewer DN, Carr CM, Munson M. Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1. Mol Biol Cell. 2012 Jan; 23(2):337-46. PMID: 22114349.
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Munson M. Show me the MUN-y. Structure. 2011 Oct 12; 19(10):1348-9. PMID: 22000505.
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Yang Y, Xia F, Hermance N, Mabb A, Simonson S, Morrissey S, Gandhi P, Munson M, Miyamoto S, Kelliher MA. 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. Mol Cell Biol. 2011 Jul; 31(14):2774-86. PMID: 21606198.
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Redfern RE, Daou MC, Li L, Munson M, Gericke A, Ross AH. A mutant form of PTEN linked to autism. Protein Sci. 2010 Oct; 19(10):1948-56. PMID: 20718038.
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Heuck A, Fetka I, Brewer DN, Hüls D, Munson M, Jansen RP, Niessing D. The structure of the Myo4p globular tail and its function in ASH1 mRNA localization. J Cell Biol. 2010 May 3; 189(3):497-510. PMID: 20439999.
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MacDonald C, Munson M, Bryant NJ. Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins. Biochem Soc Trans. 2010 Feb; 38(Pt 1):209-12. PMID: 20074061.
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Shandilya SM, Nalam MN, Nalivaika EA, Gross PJ, Valesano JC, Shindo K, Li M, Munson M, Royer WE, Harjes E, Kono T, Matsuo H, Harris RS, Somasundaran M, Schiffer CA. Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure. 2010 Jan 13; 18(1):28-38. PMID: 20152150.
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Munson M, Bolon DN. Watching proteins in motion. Genome Biol. 2009; 10(10):316. PMID: 19863776.
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Furgason ML, MacDonald C, Shanks SG, Ryder SP, Bryant NJ, Munson M. The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p. Proc Natl Acad Sci U S A. 2009 Aug 25; 106(34):14303-8. PMID: 19667197.
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Struthers MS, Shanks SG, MacDonald C, Carpp LN, Drozdowska AM, Kioumourtzoglou D, Furgason ML, Munson M, Bryant NJ. Functional homology of mammalian syntaxin 16 and yeast Tlg2p reveals a conserved regulatory mechanism. J Cell Sci. 2009 Jul 1; 122(Pt 13):2292-9. PMID: 19509055.
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Munson M, Bryant NJ. A role for the syntaxin N-terminus. Biochem J. 2009 Feb 15; 418(1):e1-3. PMID: 19159342.
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Croteau NJ, Furgason ML, Devos D, Munson M. Conservation of helical bundle structure between the exocyst subunits. PLoS One. 2009; 4(2):e4443. PMID: 19214222.
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Munson M. Tip20p reaches out to Dsl1p to tether membranes. Nat Struct Mol Biol. 2009 Feb; 16(2):100-2. PMID: 19190660.
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Songer JA, Munson M. Sec6p anchors the assembled exocyst complex at sites of secretion. Mol Biol Cell. 2009 Feb; 20(3):973-82. PMID: 19073882.
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Redfern RE, Redfern D, Furgason ML, Munson M, Ross AH, Gericke A. PTEN phosphatase selectively binds phosphoinositides and undergoes structural changes. Biochemistry. 2008 Feb 19; 47(7):2162-71. PMID: 18220422.
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Carr CM, Munson M. Tag team action at the synapse. EMBO Rep. 2007 Sep; 8(9):834-8. PMID: 17767192.
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Togneri J, Cheng YS, Munson M, Hughson FM, Carr CM. Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p. Proc Natl Acad Sci U S A. 2006 Nov 21; 103(47):17730-5. PMID: 17090679.
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Pan X, Eathiraj S, Munson M, Lambright DG. TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature. 2006 Jul 20; 442(7100):303-6. PMID: 16855591.
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Munson M, Novick P. The exocyst defrocked, a framework of rods revealed. Nat Struct Mol Biol. 2006 Jul; 13(7):577-81. PMID: 16826234.
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Sivaram MV, Furgason ML, Brewer DN, Munson M. The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Nat Struct Mol Biol. 2006 Jun; 13(6):555-6. PMID: 16699513.
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Sivaram MV, Saporita JA, Furgason ML, Boettcher AJ, Munson M. Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p. Biochemistry. 2005 Apr 26; 44(16):6302-11. PMID: 15835919.
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Munson M, Hughson FM. Conformational regulation of SNARE assembly and disassembly in vivo. J Biol Chem. 2002 Mar 15; 277(11):9375-81. PMID: 11777922.
This graph shows the total number of publications by year, by first, middle/unknown, or last author.
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Year | Publications |
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2002 | 1 | 2005 | 1 | 2006 | 4 | 2007 | 1 | 2008 | 2 | 2009 | 6 | 2010 | 4 | 2011 | 4 | 2012 | 1 | 2014 | 1 | 2015 | 4 | 2016 | 1 | 2017 | 2 | 2018 | 2 | 2020 | 7 |
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