Rho/ROCK and Cdk5 effects on phosphorylation of a β-thymosin repeat protein in Hermissenda
| Autor: | Pramod K. Dash, Juan-Juan Xue-Bian, Terry Crow, Lian-Ming Tian |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
rho GTP-Binding Proteins
Pyridines Biophysics GTPase Protein Serine-Threonine Kinases Biology Nervous System Biochemistry chemistry.chemical_compound Lysophosphatidic acid RHO protein GDP dissociation inhibitor Animals Phosphorylation Molecular Biology Rho-associated protein kinase rho-Associated Kinases Kinase Microfilament Proteins Intracellular Signaling Peptides and Proteins Cyclin-Dependent Kinase 5 Cell Biology Phosphoproteins Amides Butyrophenones Molecular biology Cyclin-Dependent Kinases Cell biology Thymosin chemistry Mollusca MDia1 Lysophospholipids Signal transduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 323:395-401 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2004.08.103 |
| Popis: | Rho GTPases acting through effector proteins regulate actin dynamics and cytoskeletal structure. In Hermissenda Csp24 is a cytoskeletal-related protein that contributes to the development of intermediate-term memory, and is homologous to other β-thymosin-like repeat proteins containing multiple actin-binding domains. We have examined the role of Rho GTPase activity and its downstream target ROCK, and cyclin-dependent kinase 5 (Cdk5) on the phosphorylation of Csp24 using 32PO4 labeling of proteins separated with 2-D PAGE. The ROCK inhibitor Y-27632 significantly increased Csp24 phosphorylation, and the Rho activator lysophosphatidic acid (LPA) or the Cdk5 inhibitor butyrolactone significantly decreased Csp24 phosphorylation. Pretreatment with Y-27632 before LPA application significantly reduced the decreased phosphorylation of Csp24 normally detected in nervous systems exposed to LPA. Using a pull-down assay we found that LPA treatments activated Rho and exposure to 5-HT decreased Rho activity. Our results indicate that the Rho/ROCK and Cdk5 signaling pathways contribute to the regulation of Csp24 phosphorylation. |
| Databáze: | OpenAIRE |
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