Title

How do mutations affecting Iqg1 phosphorylation alter protein-protein interactions?

Presenter Information

Caitlin Siehr

Department

Biological Sciences

Major

Biological Sciences

Research Advisor

Shannon, Katie

Advisor's Department

Biological Sciences

Funding Source

Opportunities for Undergraduate Research Experience

Abstract

Iqg1 is a protein involved in cytokinesis in budding yeast. It is required for the assembly and contraction of the actin ring, which then divides the two cells. In previous studies, Iqg1 has been shown to interact with a myosin light chain, Mlc1, and the formin proteins Bni1 and Bnr1. The overall objective of my research is to determine how mutations affecting Iqg1 phosphorylation alter protein-protein interactions. My research began last semester as I prepared yeast extracts from three different strains; wild type, a mutant that prevents Iqg1 phosphorylation, and a mutant that mimics Iqg1 phosphorylation. I used these extracts to perform GST-pull down experiments and conducted western blots to determine the results. I found that the mutant IQG1 alleles do not affect the binding of Iqg1 to Mlc1. I am currently performing similar experiments with formin fragments. The eukaryotic yeast cell is very similar to human cells, including the conserved interaction between human IQGAP1 and formin proteins. By studying cytokinesis in yeast cells, the results could yield a better understanding of cytokinesis in other cells.

Biography

Caitlin Siehr is a freshman at Missouri University of Science and Technology pursuing a Bachelor’s of Science in Biological Sciences. She is a member of iGEM, SCRUBS, and Helix. She also works at a local grocery store in her free time. Upon graduating, she plans to continue her education in graduate school.

Research Category

Sciences

Presentation Type

Poster Presentation

Document Type

Poster

Location

Upper Atrium/Hall

Presentation Date

15 Apr 2015, 9:00 am - 11:45 am

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Apr 15th, 9:00 AM Apr 15th, 11:45 AM

How do mutations affecting Iqg1 phosphorylation alter protein-protein interactions?

Upper Atrium/Hall

Iqg1 is a protein involved in cytokinesis in budding yeast. It is required for the assembly and contraction of the actin ring, which then divides the two cells. In previous studies, Iqg1 has been shown to interact with a myosin light chain, Mlc1, and the formin proteins Bni1 and Bnr1. The overall objective of my research is to determine how mutations affecting Iqg1 phosphorylation alter protein-protein interactions. My research began last semester as I prepared yeast extracts from three different strains; wild type, a mutant that prevents Iqg1 phosphorylation, and a mutant that mimics Iqg1 phosphorylation. I used these extracts to perform GST-pull down experiments and conducted western blots to determine the results. I found that the mutant IQG1 alleles do not affect the binding of Iqg1 to Mlc1. I am currently performing similar experiments with formin fragments. The eukaryotic yeast cell is very similar to human cells, including the conserved interaction between human IQGAP1 and formin proteins. By studying cytokinesis in yeast cells, the results could yield a better understanding of cytokinesis in other cells.