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One or more keywords matched the following properties of Munson, Mary

Academic Background

Mary 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 fusion

Vesicle 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 Research

Our 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

Current model for the architecture of the exocyst complex

One or more keywords matched the following items that are connected to Munson, Mary
Item TypeName
Academic Article Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p.
Academic Article Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
Academic Article Tag team action at the synapse.
Academic Article Functional homology of mammalian syntaxin 16 and yeast Tlg2p reveals a conserved regulatory mechanism.
Academic Article The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.
Academic Article Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins.
Academic Article Conformational regulation of SNARE assembly and disassembly in vivo.
Academic Article Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.
Concept Qa-SNARE Proteins
Concept SNARE Proteins
Concept Qc-SNARE Proteins
Academic Article To protect or reject.
Academic Article Synaptic-vesicle fusion: a need for speed.
Academic Article The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes.
Academic Article Three steps forward, two steps back: mechanistic insights into the assembly and disassembly of the SNARE complex.
Academic Article The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation.
Academic Article SNARE complex assembly and disassembly.
Academic Article Exposing the Elusive Exocyst Structure.
Academic Article Exocyst structural changes associated with activation of tethering downstream of Rho/Cdc42 GTPases.
Academic Article Membrane trafficking: vesicle formation, cargo sorting and fusion.
Search Criteria
  • SNARE Proteins