MITOTIC REGULATION OF MICROTUBULE CROSS-LINKING ACTIVITY OF CENP-E KINETOCHORE PROTEIN
MITOTIC REGULATION OF MICROTUBULE CROSS-LINKING ACTIVITY OF CENP-E KINETOCHORE PROTEIN
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DOI：
10.1126/science.8023161
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发表时间：
1994-07-15
期刊：
影响因子：
56.9
通讯作者：
YEN, TJ
中科院分区：
文献类型：
--
作者：
LIAO, H;LI, G;YEN, TJ
CENP-E是一种驱动蛋白样蛋白，在有丝分裂早期与动粒短暂结合，在后期重新分布到纺锤体中间区，并在胞质分裂后降解。在分裂后期，CENP-E可以通过氨基末端的马达样结合位点和以不同方式结合微管的99个氨基酸的羧基末端结构域来交联纺锤体中区的交错微管。有丝分裂激酶成熟促进因子（MPF）的羧基端磷酸化抑制微管结合活性后期前。因此，MPF抑制CENP-E的微管交联活性，直到后期，此时其活性丧失。
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.