Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin

J Biol Chem. 2001 Sep 14;276(37):34753-8. doi: 10.1074/jbc.M106626200. Epub 2001 Jul 20.

Abstract

Mitotic centromere-associated kinesin (MCAK) is a microtubule depolymerizer that is consistent with its role in promoting chromosome segregation during mitosis. Here we show that the conserved motor domain of MCAK is necessary but not sufficient for microtubule depolymerization in cells or in vitro. The addition of only 30 amino acids N-terminal to the motor restores depolymerization activity. Furthermore, dimerization studies revealed that the smallest functional MCAK deletion constructs are monomers. These results define a highly conserved domain within MCAK and related (KIN I) kinesins that is critical for depolymerization activity and show that this depolymerization is not dependent on MCAK dimerization.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • Cricetinae
  • Dimerization
  • Kinesins / chemistry*
  • Kinesins / physiology
  • Microtubules / metabolism*
  • Molecular Sequence Data

Substances

  • mitotic centromere-associated kinesin, hamster
  • Kinesins