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

ABSTRACT: 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

SUBMITTER: Ems-McClung SC 

PROVIDER: S-EPMC1751331 | biostudies-literature | 2007 Jan

REPOSITORIES: biostudies-literature