STRUCTURAL STUDIES FOR THE EXOCYST COMPLEX

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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. Cell polarity in eukaryotes is maintained through the targeted delivery of vesicles to distinct locations on the cell membrane and requires that the vesicle recognize the target membrane with which it will fuse. This recognition is mediated by large protein complexes. Such complexes have been identified in various compartments within the cell, including the Golgi apparatus, vacuoles, and endosomes, as well as on the plasma membrane. In the budding yeast Saccharomyces cerevisiae, a multiprotein complex called the exocyst tethers secretory vesicles to the plasma membrane. The lab is interested in exocyst assembly and function. Since we cannot yet prepare sufficient quantities of assembled exocyst for crystallization, we have started structural studies on individual subunits. Currently, we have crystallized the exo70 subunit, one of the first exocyst components to localize to the site of exocytosis, around which the entire multimeric complex will assemble.