The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends

Andrew W. Hunter, Michael Caplow, David L. Coy, William O. Hancock, Stefan Diez, Linda Wordeman, Jonathon Howard

Research output: Contribution to journalArticle

253 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)445-457
Number of pages13
JournalMolecular cell
Volume11
Issue number2
DOIs
StatePublished - Feb 1 2003

Fingerprint

Kinesin
Microtubules
Adenosine Triphosphate
Proteins
Tubulin
Adenosine Triphosphatases
Binding Sites

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Hunter, Andrew W. ; Caplow, Michael ; Coy, David L. ; Hancock, William O. ; Diez, Stefan ; Wordeman, Linda ; Howard, Jonathon. / The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. In: Molecular cell. 2003 ; Vol. 11, No. 2. pp. 445-457.
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The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. / Hunter, Andrew W.; Caplow, Michael; Coy, David L.; Hancock, William O.; Diez, Stefan; Wordeman, Linda; Howard, Jonathon.

In: Molecular cell, Vol. 11, No. 2, 01.02.2003, p. 445-457.

Research output: Contribution to journalArticle

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