Event Title
Identification of novel interactors of SEC15 via genetic suppressor screen using a 2µ-plasmid Sacchromyces cerevisiae genomic library
Faculty Mentor
Yen Kang France
Keywords
Yen Kang France
Abstract
The Exocyst complex, a highly conserved protein complex, mediates the tethering of secretory vesicles to the plasma membrane and is necessary for a plethora of cellular processes including cell migration, asymmetric cell division, differentiation, insulin exocytosis, GLUT4 trafficking, and oncogenesis. This secretory pathway is ubiquitously important, but its complexity and regulation has not been fully elucidated. Sec15p, a member of the Exocyst complex, plays many important roles within the post-Golgi secretory pathway, but the functions of Sec15p at a mechanistic level are unclear. Using the knowledge that Sec15p overproduction is toxic to cells, we performed a classical genetic screen using a multi copy plasmid genomic library in the model system, Sacchromyces cerevisiae, to identify novel suppressors that can alleviate toxicity of Sec15p overexpression when cooverexpressed. The identification of novel suppressors of Sec15p will not only give insight into the roles of Sec15p, but also the regulation of the Exocyst complex.
Session Name:
Poster Presentation Session #2 - Poster #44
Start Date
4-4-2014 12:15 PM
End Date
4-4-2014 1:00 PM
Location
HSB 3rd Floor Student Commons
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Identification of novel interactors of SEC15 via genetic suppressor screen using a 2µ-plasmid Sacchromyces cerevisiae genomic library
HSB 3rd Floor Student Commons
The Exocyst complex, a highly conserved protein complex, mediates the tethering of secretory vesicles to the plasma membrane and is necessary for a plethora of cellular processes including cell migration, asymmetric cell division, differentiation, insulin exocytosis, GLUT4 trafficking, and oncogenesis. This secretory pathway is ubiquitously important, but its complexity and regulation has not been fully elucidated. Sec15p, a member of the Exocyst complex, plays many important roles within the post-Golgi secretory pathway, but the functions of Sec15p at a mechanistic level are unclear. Using the knowledge that Sec15p overproduction is toxic to cells, we performed a classical genetic screen using a multi copy plasmid genomic library in the model system, Sacchromyces cerevisiae, to identify novel suppressors that can alleviate toxicity of Sec15p overexpression when cooverexpressed. The identification of novel suppressors of Sec15p will not only give insight into the roles of Sec15p, but also the regulation of the Exocyst complex.