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The Effects of Mutations in a Highly Conserved Site on the Alpha-4 Helix of KIF18A
Budington, Olivia Anne
Budington, Olivia Anne
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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.
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2023-01-01