Location
Havener Center, Miner Lounge / Wiese Atrium, 1:30pm-3:30pm
Start Date
4-1-2026 1:30 PM
End Date
4-1-2026 3:30 PM
Presentation Date
April 1, 2026; 1:30pm-3:30pm
Description
Iqg1 plays crucial roles in cytokinesis, including the assembly, contraction, and disassembly of the actomyosin ring, as well as the coordination of contraction and septation. Given that cytokinesis must occur post-mitosis, Iqg1 is regulated by the cell cycle. This study explores hypotheses regarding Iqg1 regulation: it’s binding to action is negatively influenced by the cyclin-dependent kinase (CDK) Cdc28 and positively influenced by dephosphorylation via Cdc14. Newly developed yeast degron tagged strains allow for rapid depletion of specific proteins. Iqg1 mutations that alter serine to threonine, which allows phosphorylation but not dephosphorylation, in the degron strain allow testing of mutant phenotypes. Cytokinesis, the process of cell division via a contractile actomyosin ring, involves the recruitment of filamentous action (F-actin) and myosin II. Budding yeast serves as a model to investigate the molecular mechanisms of actomyosin ring assembly and contraction. Iqg1 is essential for actin localization at the cytokinesis site and is regulated by phosphorylation and dephosphorylation. Mutations in Iqg1 that prevent dephosphorylation result in cytokinesis defects, analyzed through actin ring formation. Given that human homologs of Iqg1 are implicated in cancer and cytokinesis failure can lead to aneuploidy in tumor cells, this research may identify new chemotherapy targets.
Biography
Jenna Mueller is a 3rd year student majoring in Biological Sciences with a Chemistry minor. She will begin her master’s degree in Biological Sciences at S&T in the fall. Along with working in Dr. Shannon’s research lab, Jenna is a pole vaulter on the S&T Track and Field team, works in Dr. Yazdi’s lab on tumor microenvironment reprogramming, and is the Vice President of the International Genetically Engineered Machines (iGEM) design team on campus. Jenna aspires to pursue a career in R&D or biotechnology, focusing on cell and molecular biology or therapeutics. Outside of academics and athletics, she enjoys hiking, reading, and watching movies.
Meeting Name
2026 - 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
© 2026 The Authors, All rights reserved
Included in
Biochemistry, Biophysics, and Structural Biology Commons, Cell and Developmental Biology Commons, Chemistry Commons
The Effects of Preventing Dephosphorylation of lqg1 on Cytokinesis
Havener Center, Miner Lounge / Wiese Atrium, 1:30pm-3:30pm
Iqg1 plays crucial roles in cytokinesis, including the assembly, contraction, and disassembly of the actomyosin ring, as well as the coordination of contraction and septation. Given that cytokinesis must occur post-mitosis, Iqg1 is regulated by the cell cycle. This study explores hypotheses regarding Iqg1 regulation: it’s binding to action is negatively influenced by the cyclin-dependent kinase (CDK) Cdc28 and positively influenced by dephosphorylation via Cdc14. Newly developed yeast degron tagged strains allow for rapid depletion of specific proteins. Iqg1 mutations that alter serine to threonine, which allows phosphorylation but not dephosphorylation, in the degron strain allow testing of mutant phenotypes. Cytokinesis, the process of cell division via a contractile actomyosin ring, involves the recruitment of filamentous action (F-actin) and myosin II. Budding yeast serves as a model to investigate the molecular mechanisms of actomyosin ring assembly and contraction. Iqg1 is essential for actin localization at the cytokinesis site and is regulated by phosphorylation and dephosphorylation. Mutations in Iqg1 that prevent dephosphorylation result in cytokinesis defects, analyzed through actin ring formation. Given that human homologs of Iqg1 are implicated in cancer and cytokinesis failure can lead to aneuploidy in tumor cells, this research may identify new chemotherapy targets.
Comments
Advisor: Katie Shannon, shannonk@mst.edu