YEAST TWO-HYBRID INTERACTIONS WITH EXOCYST SUBUNIT DOMAINS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Polarized exocytosis at specific sites on the plasma membrane requires a conserved, eight-subunit protein complex called the exocyst. Exocyst assembly at sites of secretion is essential for tethering the vesicle to the plasma membrane, prior to SNARE¿¿mediated membrane fusion. Our goal is the molecular characterization of the yeast exocyst subunits individually and in combination in order to elucidate the function of the exocyst complex. Towards this end, we have biochemically and structurally characterized domains of several of the exocyst subunits. We will use these individual domains to test for novel interactions using the yeast two-hybrid assay.