Date of Completion
2023
Document Type
Honors College Thesis
Department
Molecular Physiology and Biophysics
Thesis Type
Honors College, College of Arts and Science Honors
First Advisor
Jason Stumpff
Second Advisor
Alicia Ebert
Keywords
kinesin, mitosis, KIF18A, motor protein, cancer, alpha-4 helix
Abstract
Kinesins are an important group of motor proteins that share a conserved motor domain and are crucial in the process of mitosis. KIF18A is a multi-talented mitotic kinesin that promotes chromosome alignment and maintains spindle shape. However, how KIF18A is regulated to perform its diverse roles within the cell is not well understood. To investigate potential mechanisms of regulation, a phosphorylation site in the motor domain, on the highly conserved S284 residue, was analyzed to determine how this modification affects KIF18A’s function. This residue is located on the alpha-4 helix, which is an important area for microtubule binding and nucleotide gating, thus potentially making it a good site for regulation. It was found that mutations at S284 lead to altered localization of KIF18A, chromosome unalignment, and spindle malformation. Given the conserved nature of S284, this research provides insight into mechanisms regulating both KIF18A and other kinesin family members.
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Recommended Citation
Budington, Olivia Anne, "The Effects of Mutations in a Highly Conserved Site on the Alpha-4 Helix of KIF18A" (2023). UVM Honors College Senior Theses. 532.
https://scholarworks.uvm.edu/hcoltheses/532