Mitotic regulation of microtubule cross-linking activity of CENP-E kinetochore protein.
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.
Fox Chase Cancer Center, Philadelphia, PA 19111.
H
H
Liao
G
G
Li
T J
TJ
Yen
D000705:Anaphase; D001483:Base Sequence; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D002875:Chromosomes / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007399:Interphase; D016200:Maturation-Promoting Factor / Q000378:metabolism; D008677:Metaphase; D008870:Microtubules / Q000378:metabolism*; D008938:Mitosis; D008969:Molecular Sequence Data; D010766:Phosphorylation; D008941:Spindle Apparatus / Q000378:metabolism*; D014162:Transfection
D002868:Chromosomal Proteins, Non-Histone; C068688:centromere protein E; D016200:Maturation-Promoting Factor