Full-length dimeric MCAK is a more efficient microtubule depolymerase than minimal domain monomeric MCAK.

Abstract:

:MCAK belongs to the Kinesin-13 family, whose members depolymerize microtubules rather than translocate along them. We defined the minimal functional unit of MCAK as the catalytic domain plus the class specific neck (MD-MCAK), which is consistent with previous reports. We used steady-state ATPase kinetics, microtubule depolymerization assays, and microtubule.MCAK cosedimentation assays to compare the activity of full-length MCAK, which is a dimer, with MD-MCAK, which is a monomer. Full-length MCAK exhibits higher ATPase activity, more efficient microtubule end binding, and reduced affinity for the tubulin heterodimer. Our studies suggest that MCAK dimerization is important for its catalytic cycle by promoting MCAK binding to microtubule ends, enhancing the ability of MCAK to recycle for multiple rounds of microtubule depolymerization, and preventing MCAK from being sequestered by tubulin heterodimers.

journal_name

Mol Biol Cell

authors

Hertzer KM,Ems-McClung SC,Kline-Smith SL,Lipkin TG,Gilbert SP,Walczak CE

doi

10.1091/mbc.e05-08-0821

keywords:

subject

Has Abstract

pub_date

2006-02-01 00:00:00

pages

700-10

issue

2

eissn

1059-1524

issn

1939-4586

pii

E05-08-0821

journal_volume

17

pub_type

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