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Investigating Post-translational modifications of kinesin


EMSL Project ID
28090

Abstract

Molecular motor-based transport is essential for numerous cellular functions, and much of it is carried out by the molecular motor kinesin. Impaired or altered kinesin function is implicated in many diseases, especially neruodegenerative diseases such as Alzheimer. While transport is critical, and highly regulated in vivo, exactly how this regulation occurs is not well understood. However, kinesin is a phosphoprotein in vivo, may be subject to other post-translational modifications as well. Past work shows that changes in kinesin's state of phosphorylation alter its function, though the details are not at all understood. Using kinases known to be important for regulated kinesin function in vivo, in vitro we have been able to observe significant changes in kinesin activity due to kinase treatment. The development of a functional in vitro assay sets the stage for a molecular-level understanding of how the kinases alter function, but to do so, we need to know exactly at which residues the kinesin is being phosphorylated. Guided by such mapping, we can then generate recombinant kinesin protein with specific sites altered to directly test the importance of phosphorylation of specific residues.

Project Details

Project type
Exploratory Research
Start Date
2008-02-25
End Date
2009-03-01
Status
Closed

Team

Principal Investigator

Steven Gross
Institution
University of California, Irvine