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. © 2013 Wiley Periodicals, Inc.

Highlights

  • The Molecular Basis for Kinesin Functional Specificity During MitosisWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, Scotland, United Kingdom

  • Microtubules are essential players in mitosis [Mitchison and Kirschner, 1984; Goshima and Scholey, 2010]

  • I review the intrinsic and extrinsic factors that provide specificity to mitotic kinesins and the underlying mechanisms for their correct targeting and function, focusing on the kinesin proteins that play a role during mitosis

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Summary

The Molecular Basis for Kinesin Functional Specificity During Mitosis

Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, Scotland, United Kingdom. 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 selfinteractions, and can associate with extrinsic factors, such as microtubule or DNA binding proteins, to provide additional functional properties.

Introduction
Identification and Structural Characterization of the Kinesins
Phylogenetic Organization and Functional Diversity of Kinesins
Functional Diversity of the Motor and Neck Domains
Oligomerization and
Specification of Kinesin Function by
Kinesins and Microtubule Associated Proteins
Chromokinesin Interactions with DNA
Kinesin Interactions with Nuclear Import Machinery
Interactions of Kinesins with Other Proteins to Modulate their Activity
Mitotic Kinesins as Recruitment Hubs
Phosphorylation May Regulate Kinesin Affinity for Microtubules
Phosphorylation Can Inhibit Intramolecular Interactions
Phosphorylation to Regulate Kinesin Localization
Conclusions

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