Mitotic regulation of microtubule cross-linking activity of CENP-E kinetochore protein

See allHide authors and affiliations

Science  15 Jul 1994:
Vol. 265, Issue 5170, pp. 394-398
DOI: 10.1126/science.8023161


CENP-E is a kinesin-like protein that is transiently bound to kinetochores during early mitosis, becomes redistributed to the spindle midzone at anaphase, and is degraded after cytokinesis. At anaphase, CENP-E may cross-link the interdigitating microtubules in the spindle midzone through a motor-like binding site at the amino terminus and a 99-amino acid carboxyl-terminal domain that bound microtubules in a distinct manner. Phosphorylation of the carboxyl terminus by the mitotic kinase maturation promoting factor (MPF) inhibited microtubule-binding activity before anaphase. Thus, MPF suppresses the microtubule cross-linking activity of CENP-E until anaphase, when its activity is lost.

Stay Connected to Science