Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network

  Advanced Search  

2009NatureAmerica,Inc.Allrightsreserved. nature structural & molecular biology advance online publication

Summary: ©2009NatureAmerica,Inc.Allrightsreserved.
nature structural & molecular biology advance online publication
a rt i c l e s
The kinesin-13 protein mitotic centromere­associated kinesin
(MCAK) can both rapidly depolymerize microtubules1­3 and also
provide its own means of transportation to microtubule ends, where
the action of depolymerization takes place4. This is especially benefi-
cial in living cells, where microtubule ends may be relatively sparse
compared to microtubule lattice and are predominantly located at
the cell periphery. Here, for the first time to our knowledge, we pre-
cisely quantify the relative functional benefits of two important struc-
tural features of MCAK, which are common features of microtubule
motors: dimerization and the positively charged neck. We show that
features that improve one function may impede another.
The MCAK neck is an -helical ~60-amino-acid region located
adjacent to the kinesin motor domain5,6. A high concentration of
lysine and arginine residues confers a charge of about +5 on the neck
at neutral pH. The positive charges in the neck are essential for MCAK
to depolymerize microtubules under physiological conditions5.
However, the mechanistic role of this structural element is entirely


Source: Asbury, Chip - Department of Physiology and Biophysics, University of Washington at Seattle


Collections: Biology and Medicine