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MITOSIS-SPECIFIC PHOSPHORYLATION OF CALDESMON - POSSIBLE MOLECULAR MECHANISM OF CELL ROUNDING DURING MITOSIS
被引:43
作者:
YAMASHIRO, S
MATSUMURA, F
机构:
[1] Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey
来源:
关键词:
D O I:
10.1002/bies.950131103
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
One of the profound changes in cellular morphology during mitosis is a massive alteration in the organization of microfilament cytoskeleton. It has been recently discovered that nonmuscle caldesmon, an actin and calmodulin binding microfilament-associated protein of relative molecular mass M(r) = 83000, is dissociated from microfilaments during mitosis, apparently as a consequence of mitosis-specific phosphorylation. cdc2 kinase, which is a catalytic subunit of MPF (maturation or mitosis promoting factor), is found to be responsible for the mitosis-specific phosphorylation of caldesmon. Because caldesmon is implicated in the regulation of actin myosin interactions and/or microfilament organization, these results suggest that cdc2 kinase directly affects microfilament re-organization during mitosis.
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页码:563 / 568
页数:6
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