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Mitosis-specific phosphorylation of caldesmon: Possible molecular mechanism of cell rounding during mitosis

✍ Scribed by Shigeko Yamashiro; Fumio Matsumura

Publisher: John Wiley and Sons
Year: 1991
Tongue: English
Weight: 757 KB
Volume: 13
Category: Article
ISSN: 0265-9247
DOI: 10.1002/bies.950131103

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✦ Synopsis

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 Mr =83 000, 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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