| C-terminus of mitotic centromere-associated kinesin (MCAK) inhibits its lattice-stimulated ATPase activity. | |
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MedLine Citation:
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PMID: 15250824 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Mitotic centromere-associated kinesin (MCAK) is a microtubule (MT)-destabilizing molecular motor. In the present study we show that the final 8 amino acids of the C-terminus of MCAK inhibit lattice-stimulated ATPase activity of the motor. Surprisingly, loss of this C-terminal 'tail' (MCAK-Q710) leads to more rapid depolymerization of MTs relative to full-length MCAK (wt-MCAK). Biochemical and microscopic assays revealed that MCAK-Q710 bound to the MT lattice with higher apparent affinity as compared with wt-MCAK. End-stimulated depolymerization was similar for both enzymes. These data suggest that lattice-bound MCAK can increase the rate of MT depolymerization, but at an energy cost. The function of the C-terminus of MCAK may be to selectively inhibit lattice-stimulated ATPase activity, resulting in limited interactions of the motor with the MT lattice. This increases the coupling between ATP hydrolysis and tubulin dimer release, but it also limits MT depolymerization. |
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Authors:
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Ayana Moore; Linda Wordeman |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Biochemical journal Volume: 383 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2004 Oct |
Date Detail:
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Created Date: 2004-10-07 Completed Date: 2005-03-21 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 227-35 Citation Subset: IM |
Affiliation:
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Department of Physiology and Biophysics, University of Washington School of Medicine, 1959 NE Pacific St., Box 357290, Seattle, WA 98195, USA. atmoore@u.washington.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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metabolism Animals CHO Cells Cattle Cells, Cultured Centromere / metabolism Cricetinae Dimerization Hydrolysis Kinesin / chemistry*, genetics, metabolism* Kinetics Microtubules / chemistry, metabolism Rhodamines / metabolism Sequence Deletion Tubulin / chemistry, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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1 F31 GM65061/GM/NIGMS NIH HHS; GM53654A/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Rhodamines; 0/Tubulin; 0/mitotic centromere-associated kinesin, hamster; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Kinesin |
| Comments/Corrections | |
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