Phosphoregulation of tropomyosin is crucial for actin cable turnover and division site placement.

Autor:	Palani S; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK s.palani@warwick.ac.uk., Köster DV; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK., Hatano T; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK., Kamnev A; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK., Kanamaru T; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK., Brooker HR; School of Biosciences, University of Kent, Canterbury, Kent, UK., Hernandez-Fernaud JR; School of Life Sciences, University of Warwick, Coventry, UK., Jones AME; School of Life Sciences, University of Warwick, Coventry, UK., Millar JBA; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK., Mulvihill DP; School of Biosciences, University of Kent, Canterbury, Kent, UK., Balasubramanian MK; Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK M.K.Balasubramanian@warwick.ac.uk.
Jazyk:	angličtina
Zdroj:	The Journal of cell biology [J Cell Biol] 2019 Nov 04; Vol. 218 (11), pp. 3548-3559. Date of Electronic Publication: 2019 Oct 09.
DOI:	10.1083/jcb.201809089
Abstrakt:	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. (© 2019 Palani et al.)
Databáze:	MEDLINE
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