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Mitosis‐specific phosphorylation of caldesmon: Possible molecular mechanism of cell rounding during mitosis
Author(s) -
Yamashiro Shigeko,
Matsumura Fumio
Publication year - 1991
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950131103
Subject(s) - caldesmon , mitosis , microfilament , microbiology and biotechnology , biology , mdia1 , cytoskeleton , calmodulin , biochemistry , cell , enzyme
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.