The Kinesin-Related Protein MCAK Is a Microtubule Depolymerase that Forms an ATP-Hydrolyzing Complex at Microtubule Ends

• Autores: David L. Coy, Andrew W. Hunter, Michael Caplow
• Localización: Molecular cell, ISSN 1097-2765, Vol. 12, Nº 2, 2003, pág. 445
• Idioma: inglés
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• Resumen

  • 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 μM−1·s−1), perhaps by diffusion along the microtubule lattice, and, once there, removes ∼20 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.