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Vol. 12, Issue 1, 239-250, January 2001
Department of Molecular Biology and Biochemistry, Rutgers
University, Nelson Labs, Busch Campus, Piscataway, New Jersey 08855
Caldesmon is phosphorylated by cdc2 kinase during mitosis,
resulting in the dissociation of caldesmon from microfilaments. To
understand the physiological significance of phosphorylation, we
generated a caldesmon mutant replacing all seven cdc2 phosphorylation sites with Ala, and examined effects of expression of the caldesmon mutant on M-phase progression. We found that microinjection of mutant
caldesmon effectively blocked early cell division of
Xenopus embryos. Similar, though less effective,
inhibition of cytokinesis was observed with Chinese hamster ovary (CHO)
cells microinjected with 7th mutant. When mutant caldesmon was
introduced into CHO cells either by protein microinjection or by
inducible expression, delay of M-phase entry was observed. Finally, we
found that 7th mutant inhibited the disassembly of microfilaments
during mitosis. Wild-type caldesmon, on the other hand, was much less
potent in producing these three effects. Because mutant caldesmon did
not inhibit cyclin B/cdc2 kinase activity, our results suggest that alterations in microfilament assembly caused by caldesmon
phosphorylation are important for M-phase progression.
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