Unknown

Dataset Information

0

The molecular basis for kinesin functional specificity during mitosis.


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.

SUBMITTER: Welburn JP 

PROVIDER: S-EPMC4065354 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

The molecular basis for kinesin functional specificity during mitosis.

Welburn Julie P I JP  

Cytoskeleton (Hoboken, N.J.) 20130901 9


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  ...[more]

Similar Datasets

| S-EPMC1271808 | biostudies-literature
| S-EPMC4905186 | biostudies-other
| S-EPMC2993330 | biostudies-literature
| S-EPMC8247599 | biostudies-literature
| S-EPMC3974339 | biostudies-other
| S-EPMC3172266 | biostudies-literature
| S-EPMC3755979 | biostudies-literature
| S-EPMC1839003 | biostudies-literature
| S-EPMC3534820 | biostudies-literature
| S-EPMC7361990 | biostudies-literature