| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.57211092 |
| We also have found that the inhibition of the binding between actin and caldesmon either by Ca ( 2+ ) / calmodulin or by phosphorylation with cdc 2 kinase reverses the inhibitory effect of caldesmon on Arp2 / 3 induced actin polymerization . 0.57211092^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Mitosis specific phosphorylation by cdc 2 kinase causes nonmuscle caldesmon to dissociate from microfilaments ( Yamashiro , S . , Yamakita , Y . , Ishikawa , R . , and Matsumura , F . ( 1990 ) Nature 344 , 675 678 ; Yamashiro , S . , Yamakita , Y . , Hosoya , H . , and Matsumura , F . ( 1991 ) Nature 349 , 169 172 ) . ^^^ Actin bound caldesmon can be phosphorylated by cdc 2 kinase , which results in the dissociation of caldesmon from F actin . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| The phosphorylation of caldesmon by cdc 2 kinase also eliminated the microtubule binding activity . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| 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 . cdc 2 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 cdc 2 kinase directly affects microfilament re organization during mitosis . . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| We now report that cdc 2 kinase phosphorylates caldesmon in vitro principally at the same sites as those phosphorylated in vivo during mitosis , and that phosphorylation reduces the binding affinity of caldesmon for both actin and calmodulin . ^^^ Because caldesmon inhibits actomyosin ATPase , our results suggest that cdc 2 kinase directly causes microfilament reorganization during mitosis . . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of caldesmon by cdc 2 kinase . ^^^ In this study we have demonstrated that smooth muscle caldesmon is phosphorylated in vitro by cdc 2 kinase from mitotic phase HeLa cells to 1 . 2 mol of phosphate / mol of caldesmon . ^^^ Our finding supports the model that phosphorylation of caldesmon by cdc 2 kinase at mitosis may contribute to the disassembly of the microfilament bundles during prophase . . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of rat non muscle caldesmon by cdc 2 kinase causes reduction in most of caldesmon ' s properties , including caldesmon ' s binding to actin , myosin , and calmodulin , as well as its inhibition of actomyosin ATPase . ^^^ We have generated and characterized the COOH terminus of caldesmon mutants lacking mitosis specific phosphorylation sites , because the COOH terminal half of caldesmon contains all 7 putative Ser or Thr sites for cdc 2 kinase . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Mitosis specific phosphorylation by cdc 2 kinase causes nonmuscle caldesmon to dissociate from microfilaments during prometaphase . ( Yamashiro , S . , Y . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Caldesmon phosphatase was identified in chicken gizzard smooth muscle by using as substrates caldesmon phosphorylated at different sites by protein kinase C , Ca2+ / calmodulin dependent protein kinase 2 and cdc 2 kinase . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Furthermore , as phosphorylation of caldesmon by cdc 2 kinase inhibits actin binding of caldesmon , phosphorylation can also control actin binding of fascin in the presence of TM . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Mutant Caldesmon lacking cdc 2 phosphorylation sites delays M phase entry and inhibits cytokinesis . ^^^ Caldesmon is phosphorylated by cdc 2 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 cdc 2 phosphorylation sites with Ala , and examined effects of expression of the caldesmon mutant on M phase progression . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Regulation of caldesmon activity by Cdc 2 kinase plays an important role in maintaining membrane cortex integrity during cell division . ^^^ 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 ( CaD 39 6F ) , as well as a mutant of the full length CaD ( CaD 6F ) , in which all six potential phosphorylation sites for Cdc 2 kinase were abolished . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| We also show that cdc 2 increases cell migration via specific association with cyclin B 2 , and we unravel a novel pathway of cell motility that involves , downstream of cdc 2 , caldesmon . cdc 2 and caldesmon are shown here to localize in membrane ruffles in motile cells . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| Caldesmon is a substrate of cdc 2 kinase and Erk1 / 2 MAPK , and phosphorylation by either of these kinases reverses the inhibitory effects of caldesmon . ^^^ Cdc 2 mediated caldesmon phosphorylation and the resulting dissociation of caldesmon from actin filaments are essential for M phase progression during mitosis . ^^^ |
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| Interacting proteins: Q05682 and P06493 |
Pubmed |
SVM Score :0.0 |
| The same sites in l CaD are also phosphorylated when cells are stimulated to migrate , whereas in dividing cells l CaD is phosphorylated more extensively , presumably by cdc 2 kinase . ^^^ |
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