Effect of serine/threonine protein kinases and protein phosphatases inhibitors on mitosis progression in a synchronized tobacco BY-2 culture
| Autor: | A. Azmi, Jean-Pierre Verbelen, Kris Vissenberg, Ya. B. Blume, Ya. A. Sheremet, Emets Ai |
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| Rok vydání: | 2012 |
| Předmět: |
Serine/threonine-specific protein kinase
Cell Biology Polo-like kinase Serine threonine protein kinase Biology Agricultural and Biological Sciences (miscellaneous) AKT3 Cell biology Biochemistry Mitogen-activated protein kinase Genetics biology.protein Protein phosphorylation Human medicine Casein kinase 1 c-Raf |
| Zdroj: | Cytology and genetics |
| ISSN: | 1934-9440 0095-4527 |
| DOI: | 10.3103/s009545271202003x |
| Popis: | In order to investigate the role of various serine/threonine protein kinases and protein phosphatases in the regulation of mitosis progression in plant cells, the influence of cyclin(olomoucine) and Ca2+/calmodulin-dependent (W7) protein kinases inhibitors, as well as protein kinase C inhibitors (H7 and staurosporine), and a protein phosphatases inhibitor (okadaic acid) on mitosis progression in synchronized tobacco BY-2 cells has been studied. It was found that BY-2 culture treatment with inhibitors of cyclin-dependent protein kinases and protein kinase C caused a prophase delay, reduced the mitotic index, and displaced the mitotic peak as compared with control cells. Inhibition of Ca2+/calmodulin-dependent protein kinases enhanced the cells entry into prophase and delayed their exit from mitosis. Meanwhile inhibition of serine/threonine protein phosphatases insignificantly enhances synchronized BY-2 cells entering into all phases of mitosis. |
| Databáze: | OpenAIRE |
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