The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly.

The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Research Abstract Details 

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The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Abstract Text:

Stephanie C Ems-McClung,Kathleen M Hertzer,Xin Zhang,Mill W Miller,Claire E Walczak,

Spindle assembly and accurate chromosome segregation require the proper regulation of microtubule dynamics. MCAK, a Kinesin-13, catalytically depolymerizes microtubules, regulates physiological microtubule dynamics, and is the major catastrophe factor in egg extracts. Purified GFP-tagged MCAK domain mutants were assayed to address how the different MCAK domains contribute to in vitro microtubule depolymerization activity and physiological spindle assembly activity in egg extracts. Our biochemical results demonstrate that both the neck and the C-terminal domain are necessary for robust in vitro microtubule depolymerization activity. In particular, the neck is essential for microtubule end binding, and the C-terminal domain is essential for tight microtubule binding in the presence of excess tubulin heterodimer. Our physiological results illustrate that the N-terminal domain is essential for regulating microtubule dynamics, stimulating spindle bipolarity, and kinetochore targeting; whereas the C-terminal domain is necessary for robust microtubule depolymerization activity, limiting spindle bipolarity, and enhancing kinetochore targeting. Unexpectedly, robust MCAK microtubule (MT) depolymerization activity is not needed for sperm-induced spindle assembly. However, high activity is necessary for proper physiological MT dynamics as assayed by Ran-induced aster assembly. We propose that MCAK activity is spatially controlled by an interplay between the N- and C-terminal domains during spindle assembly.

The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Publishing Authors By Initials

SC Ems-McClung,KM Hertzer,X Zhang,MW Miller,CE Walczak,

For similar animals: chordata: vertebrates: amphibia: anura: pipidae: xenopus: xenopus laevis research abstracts see: animals: chordata: vertebrates: amphibia: anura: pipidae: xenopus: xenopus laevis research

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The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular biology of the cell

VOLUME: 18

Page Numbers: 282-94

Journal Abbreviation: Mol. Biol. Cell

ISSN: 1059-1524

DAY: 8

MONTH: 11

YEAR: 2006

The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Information

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LANGUAGE: eng

NlmUniqueID: 9201390

The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Keywords Mesh Terms:

KEYWORDS: Xenopus laevis

MESH TERMS: metabolism

Chemical & Substance for Abstract: The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Information

Substance Name: Kinesin

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly.

AFFILIATION: Medical Science Program, Indiana University, Bloomington, IN 47405, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R15GM073688-01

ACRONYM: GM

MEDLINETA: Mol Biol Cell

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