Journal
MOLECULAR CELL
Volume 11, Issue 2, Pages 445-457Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(03)00049-2
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Funding
- NIAMS NIH HHS [AR40593, R01 AR040593, R37 AR040593] Funding Source: Medline
- NIGMS NIH HHS [GM53654A, R01 GM059231, GM59231] Funding Source: Medline
- PHS HHS [T326M07270] Funding Source: Medline
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MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead destabilize microtubules. We show that MCAK is an ATPase that catalytically depolymerizes microtubules by accelerating, 100-fold, the rate of dissociation of tubulin from microtubule ends. MCAK has one high-affinity binding site per protofilament end, which, when occupied, has both the depolymerase and ATPase activities. MCAK targets protofilament ends very rapidly (on-rate 54 muM(-1).s(-1)), perhaps by diffusion along the microtubule lattice and, once there, removes similar to20 tubulin dimers at a rate of 1 s(-1). We propose that up to 14 MCAK dimers assemble at the end of a microtubule to form an ATP-hydrolyzing complex that processively depolymerizes the microtubule.
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