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Permanent link (DOI): https://doi.org/10.7939/R33F4KZ7R

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Regulation of Caenorhabditis elegans MCAK by Aurora Kinase Phosphorylation Open Access

Descriptions

Other title
Subject/Keyword
kinesin
microtubule dynamics
phosphorylation
C. elegans
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Han, Xue
Supervisor and department
Srayko, Martin (Biological Sciences)
Examining committee member and department
Campbell, Shelagh (Biological Sciences)
Waskiewicz, Andrew (Biological Sciences)
Chan, Gordon (Oncology)
Sharp, David (Physiology and Biophysics, Albert Einstein College of Medicine)
Department
Department of Biological Sciences
Specialization
Molecular Biology and Genetics
Date accepted
2014-09-05T09:00:13Z
Graduation date
2014-11
Degree
Doctor of Philosophy
Degree level
Doctoral
Abstract
Regulation of microtubule dynamics is essential for many cellular processes, including proper assembly and function of the mitotic spindle. One mechanism for temporal and spatial regulation of microtubule dynamics is provided by the kinesin-13 microtubule depolymerizing enzymes, among which MCAK is the most extensively studied. Vertebrates MCAK locates to chromatin, kinetochores, spindle poles, microtubule tips, and the cytoplasm, implying that the regulation of MCAK activity and subcellular targeting is complex. It has been established that MCAK activity and subcellular localization is regulated by Aurora kinase phosphorylation. However, the in vivo regulatory mechanism is highly complex and is still not fully understood. In this thesis I describe the function and regulation of KLP-7, the C. elegans kinesin-13 homologue. KLP-7 locates to chromosomes and spindle poles during meiosis and mitosis, and to the chromosomal passenger complex region in meiosis. Loss of KLP-7 results in meiotic and mitotic defects that are consistent with an increase in the amount of microtubules in the cytoplasmic and spindle regions of meiotic embryos, and an increase in the number of microtubules emanating from centrosomes. I found that KLP-7 protein is phosphorylated in vivo and in vitro. Finally, by performing a structure-function analysis I identified S546 as a putative Aurora kinase site essential for KLP-7 activity in vivo.
Language
English
DOI
doi:10.7939/R33F4KZ7R
Rights
This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for the purpose of private, scholarly or scientific research. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
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