Regulation of caldesmon activity by Cdc2 kinase plays an important role in maintaining membrane cortex integrity during cell division |
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Authors: | Y Li D Wessels T Wang J L-C Lin D R Soll J J-C Lin |
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Institution: | (1) Department of Biological Sciences, University of Iowa, 138 Biology Building, Iowa City, Iowa 52242-1324 (USA), Fax: +1 319 335 1069, e-mail: Jim-Lin@uiowa.edu, US |
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Abstract: | To study the mitosis-specific phosphorylation of caldesmon (CaD), we generated a mutant of the C-terminal fragment (amino
acids 244–538) of human fibroblast CaD (CaD39-6F), as well as a mutant of the full-length CaD (CaD-6F), in which all six potential
phosphorylation sites for Cdc2 kinase were abolished. The mitotic CaD39-6F-overexpressing cells required more time to progress
from anaphase start to 50% cytokinesis, exhibited larger size, and abnormally formed numerous small blebs. In contrast, overexpression
of the wild-type C-terminal fragment of CaD (CaD39) did not result in abnormal bleb formation, but led to larger size and
prolonged the time requirement between anaphase start and 50% cytokinesis. Similar abnormal blebs were also observed in the
CaD-6F-overexpressing cells. CaD-6F-overexpressing cells did not show larger size but required more time to progress from
anaphase start to 50% cytokinesis. These results suggest that mitosis-specific phosphorylation of CaD plays a role in inhibiting
bleb formation and that the N-terminal fragment of CaD is required for cell size determination.
Received 4 September 2002; received after revision 25 November 2002; accepted 4 December 2002 |
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Keywords: | , Mitosis-specific phosphorylation, phosphorylation-defective mutant, blebbing, 2D and 3D dynamic image analysis,,,,,,microfilament, cytokinesis, |
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