Lucky 13-microtubule depolymerisation by kinesin-13 motors.
The kinesin-13 class of motors catalyses microtubule depolymerisation by bending tubulins at microtubule ends. Depolymerisation activity is intrinsic to the kinesin-13 motor core but the activity of the core alone is very low compared with that of constructs that also contain a conserved neck sequence. The full-length dimeric motor is an efficient depolymeriser and also diffuses along the microtubule lattice, which helps it to find microtubule ends. Current evidence supports the idea of a generic mechanism for kinesin-13-catalysed depolymerisation. However, the activity of kinesin-13 motors is precisely localised and regulated in vivo to enable a wide range of cellular roles. The proteins are involved in global control of microtubule dynamics. They also localise to mitotic and meiotic spindles, where they contribute to formation and maintenance of spindle bipolarity, chromosomal congression, attachment correction and chromatid separation. In interphase cells, intricate and subtle mechanisms appear to allow kinesin-13 motors to act on specific populations of microtubules. Such carefully controlled localisation and regulation makes these kinesins efficient, multi-tasking molecular motors.
Moores
Carolyn A
CA
School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK. c.moores@mail.cryst.bbk.ac.uk
Milligan
Ronald A
RA
D000595:Amino Acid Sequence; D000818:Animals; D002455:Cell Division; D019281:Dimerization; D006801:Humans; D007399:Interphase; D016547:Kinesins / Q000737:chemistry / Q000502:physiology*; D008870:Microtubules / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011108:Polymers / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014404:Tubulin / Q000502:physiology
C417670:KIF13A protein, human; D011108:Polymers; D014404:Tubulin; C504977:KIF13B protein, rat; D016547:Kinesins