Location
Innovation Lab Atrium
Start Date
4-2-2025 10:00 AM
End Date
4-2-2025 11:30 AM
Presentation Date
2 April 2025, 10:00am - 11:30am
Biography
Schneider biography:
Lindsay Schneider is a sophomore at Missouri S&T, pursuing a major in Biological Sciences and a minor in Chemistry. In addition to her work in Dr. Shannon's research lab, Lindsay serves as a PRO Leader for the New Student Programs department, where she organizes events to help incoming students transition to university life. She is also the Public Relations Chair for the campus's International Genetically Engineered Machines (iGEM) design team, where she plays an active role in promoting and fundraising for the group. Lindsay is a proud member of the Phi Sigma Biological Honor Society, the S&T Honors Program, and the SCRUBS pre-health club. While Lindsay is still exploring her future, she is passionate about pursuing a career that involves hands-on work with people and offers opportunities to travel.
Ham biography:
Alexis Ham is a senior at Missouri S&T, pursuing a major in Biological Sciences with a minor in Chemistry. Prior to attending S&T, she graduated from East Central College with an Associate of Science in Biotechnology, where she was an active member of the Phi Theta Kappa Honor Society. In addition to her work in Dr. Shannon's lab, Alexis serves as the Treasurer of the Phi Sigma Biological Sciences Honor Society. After earning her degree from S&T, she plans to continue her studies in graduate school at S&T and aspires to build a career in healthcare.
Meeting Name
2025 - Miners Solving for Tomorrow Research Conference
Department(s)
Biological Sciences
Second Department
Chemistry
Document Type
Poster
Document Version
Final Version
File Type
event
Language(s)
English
Rights
© 2025 The Authors, All rights reserved
Included in
Biochemistry, Biophysics, and Structural Biology Commons, Cell and Developmental Biology Commons
Characterization of an Iqg1 Phosphorylation Mutant
Innovation Lab Atrium
Comments
Advisor: Katie Shannon
Abstract:
Cytokinesis, the final stage of cell division, in budding yeast requires the Iqg1 protein. We have previously shown that preventing phosphorylation of Iqg1 disrupts the timing of actin ring formation and myosin contraction. To understand more about the role of phosphorylation in regulating actomyosin ring function, we have created a mutation in the Iqg1 protein that changes a serine to a threonine, allowing the protein to be phosphorylated but not dephosphorylated. This mutation causes a defect in cytokinesis. To better understand the mechanism, the phenotype of this mutant will be analyzed. Using immunofluorescence and live cell imaging, we will determine if the timing of actomyosin ring assembly and contraction are altered. Since humans have three homologs of IQG1, understanding the function of this protein in yeast cells will allow a better understanding of cytokinesis in all eukaryotic cells.