Phosphoregulation of tropomyosin is crucial for actin cable turnover and division site placement
| Autor: | Holly R. Brooker, Juan Ramon Hernandez-Fernaud, Daniel P. Mulvihill, Taishi Kanamaru, Darius Vasco Köster, Saravanan Palani, Anton Kamnev, Jonathan B. A. Millar, Alexandra M. E. Jones, Mohan K. Balasubramanian, Tomoyuki Hatano |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
macromolecular substances
Tropomyosin Microfilament Serine Protein filament 03 medical and health sciences QH301 Report Schizosaccharomyces Myocyte Actin-binding protein Phosphorylation QH426 Actin Research Articles 030304 developmental biology 0303 health sciences biology 030302 biochemistry & molecular biology Cell Biology musculoskeletal system QP Actins 3. Good health Cell biology biology.protein tissues |
| Zdroj: | The Journal of Cell Biology Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | Palani et al. reveal a new mechanism by which the F-actin binding protein tropomyosin is regulated. They find that phosphorylation of tropomyosin reduces its affinity for F-actin, allowing the competing Adf1 to bind and sever actin filaments. Tropomyosin is a coiled-coil actin binding protein key to the stability of actin filaments. In muscle cells, tropomyosin is subject to calcium regulation, but its regulation in nonmuscle cells is not understood. Here, we provide evidence that the fission yeast tropomyosin, Cdc8, is regulated by phosphorylation of a serine residue. Failure of phosphorylation leads to an increased number and stability of actin cables and causes misplacement of the division site in certain genetic backgrounds. Phosphorylation of Cdc8 weakens its interaction with actin filaments. Furthermore, we show through in vitro reconstitution that phosphorylation-mediated release of Cdc8 from actin filaments facilitates access of the actin-severing protein Adf1 and subsequent filament disassembly. These studies establish that phosphorylation may be a key mode of regulation of nonmuscle tropomyosins, which in fission yeast controls actin filament stability and division site placement. |
| Databáze: | OpenAIRE |
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