Determining the Function of the RGCt Domain of IQG1 in Budding Yeast
Department
Biological Sciences
Major
Biological Sciences
Research Advisor
Shannon, Katie
Advisor's Department
Biological Sciences
Funding Source
Opportunities for Undergraduate Experience Program (OURE)
Abstract
Cytokinesis is the final step in cell division, when the mother cell divides into two daughter cells. In budding yeast, IQG1 is an extracellular scaffolding protein that is required for formation and contraction of the actin ring during cytokinesis. The Ras GAP C-terminus domain (RGCt) is one of the four domains found in IQG1. This domain is highly conserved in IQGAP family members, but the function of this domain in budding yeast is currently unknown. Based on data from the human homolog, we suspected that this domain would be required for binding to actin-nucleating proteins called formins; however, our preliminary data shows that this is not the case. Deletion of the RGCt domain is lethal to yeast cells, so its function is essential. To determine binding partners for this domain, we will purify a His-tagged RGCt protein from bacteria, incubate with yeast extracts, and identify candidate interacting proteins by western blotting and novel interactions using mass spectrometry.
Biography
Kelsey Crossen is a junior majoring in Biological Sciences with minors in Chemistry and Psychology. She has been an undergraduate researcher in Dr. Katie Shannon’s Cytokinesis Lab since February 2013. Kelsey is the secretary and a lab instructor for S&T’s International Genetically Engineered Machine Team, a member of Phi Sigma Biological Sciences Honors Fraternity, and works for the Bio Sci department as a grader and as the BioConnection writer. After graduating from S&T next year, she plans to enter graduate school to study Microbiology or Cell Biology.
Research Category
Sciences
Presentation Type
Poster Presentation
Document Type
Poster
Location
Upper Atrium/Hall
Presentation Date
16 Apr 2014, 9:00 am - 11:45 am
Determining the Function of the RGCt Domain of IQG1 in Budding Yeast
Upper Atrium/Hall
Cytokinesis is the final step in cell division, when the mother cell divides into two daughter cells. In budding yeast, IQG1 is an extracellular scaffolding protein that is required for formation and contraction of the actin ring during cytokinesis. The Ras GAP C-terminus domain (RGCt) is one of the four domains found in IQG1. This domain is highly conserved in IQGAP family members, but the function of this domain in budding yeast is currently unknown. Based on data from the human homolog, we suspected that this domain would be required for binding to actin-nucleating proteins called formins; however, our preliminary data shows that this is not the case. Deletion of the RGCt domain is lethal to yeast cells, so its function is essential. To determine binding partners for this domain, we will purify a His-tagged RGCt protein from bacteria, incubate with yeast extracts, and identify candidate interacting proteins by western blotting and novel interactions using mass spectrometry.
