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Science 15 July 1994:
Vol. 265. no. 5170, pp. 394 - 398
DOI: 10.1126/science.8023161
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Articles

Science, Vol 265, Issue 5170, 394-398
Copyright © 1994 by American Association for the Advancement of Science

articles

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

H Liao, G Li, and TJ Yen

Fox Chase Cancer Center, Philadelphia, PA 19111.

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.


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