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Cytoskeleton (Hoboken). 2013 Sep;70(9):476-93. doi: 10.1002/cm.21135. Epub 2013 Oct 8.

The molecular basis for kinesin functional specificity during mitosis.

Author information

1
Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, Scotland, United Kingdom.

Abstract

Microtubule-based motor proteins play key roles during mitosis to assemble the bipolar spindle, define the cell division axis, and align and segregate the chromosomes. The majority of mitotic motors are members of the kinesin superfamily. Despite sharing a conserved catalytic core, each kinesin has distinct functions and localization, and is uniquely regulated in time and space. These distinct behaviors and functional specificity are generated by variations in the enzymatic domain as well as the non-conserved regions outside of the kinesin motor domain and the stalk. These flanking regions can directly modulate the properties of the kinesin motor through dimerization or self-interactions, and can associate with extrinsic factors, such as microtubule or DNA binding proteins, to provide additional functional properties. This review discusses the recently identified molecular mechanisms that explain how the control and functional specification of mitotic kinesins is achieved.

KEYWORDS:

kinesin; microtubules; mitosis; motors; regulation

PMID:
24039047
PMCID:
PMC4065354
DOI:
10.1002/cm.21135
[Indexed for MEDLINE]
Free PMC Article

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