Mitosis-Dependent Phosphorylation and Activation of LIM-Kinase 1
| Autor: | Toshikazu Nakamura, Tomoyuki Sumi, Kunio Matsumoto |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Biophysics
Mitosis Arp2/3 complex macromolecular substances Protein Serine-Threonine Kinases Biochemistry Lim kinase Cyclin-dependent kinase Roscovitine Humans Enzyme Inhibitors Phosphorylation Cytoskeleton Molecular Biology biology Chemistry Nocodazole Cell Cycle Lim Kinases Actin remodeling Cell Biology Cofilin Actin cytoskeleton Actins Cyclin-Dependent Kinases Cell biology DNA-Binding Proteins Enzyme Activation Purines biology.protein MDia1 Protein Kinases HeLa Cells |
| Zdroj: | Biochemical and Biophysical Research Communications. 290:1315-1320 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2002.6346 |
| Popis: | LIM-kinases (LIMK1 and LIMK2) regulate actin cytoskeletal reorganization through phosphorylation of cofilin, an actin-depolymerizing factor of actin filaments. Here, we describe a detailed analysis of the cell-cycle-dependent activity of endogenous LIMK1. When HeLa cells were synchronized at prometaphase by nocodazole-treatment, LIMK1 was hyperphosphorylated, and its activity toward cofilin phosphorylation was markedly increased. During cell cycle progression, LIMK1 activity was low in interphase but reached a maximal level during mitosis. Activation of LIMK1 during mitosis was abrogated by roscovitine, a specific inhibitor of cyclin-dependent kinases (CDKs), suggesting that activation of CDKs directly or indirectly participates in LIMK1 activation. These results strongly suggest that LIMK1 may play an important role in the cell cycle progression through regulation of actin cytoskeletal rearrangements. |
| Databáze: | OpenAIRE |
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