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

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