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

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Palani, Saravanan, Köster, Darius, Hatano, Tomoyuki, Kamnev, Anton, Kanamaru, Taishi, Brooker, Holly R., Hernandez-Fernaud, Juan Ramon, Jones, Alexandra M. E., Millar, Jonathan B. A., Mulvihill, Daniel P. and Balasubramanian, Mohan K. (2019) Phosphoregulation of tropomyosin is crucial for actin cable turnover and division site placement. Journal of Cell Biology, 218 (11). pp. 3548-3559. doi:10.1083/jcb.201809089

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Official URL: http://dx.doi.org/10.1083/jcb.201809089

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Abstract

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.

Item Type: Journal Article
Subjects: Q Science > QH Natural history > QH426 Genetics
Q Science > QP Physiology
Divisions: Faculty of Science > Life Sciences (2010- )
Faculty of Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Tropomyosins, Biochemistry, Cell division, Cell cycle -- Research
Journal or Publication Title: Journal of Cell Biology
Publisher: Rockefeller University Press
ISSN: 0021-9525
Official Date: 4 November 2019
Dates:
DateEvent
4 November 2019Published
9 October 2019Available
30 August 2019Accepted
Volume: 218
Number: 11
Page Range: pp. 3548-3559
DOI: 10.1083/jcb.201809089
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
WT101885MAWellcome Trusthttp://dx.doi.org/10.13039/100010269
203276/Z/16/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
WM130042[RS] Royal Societyhttp://dx.doi.org/10.13039/501100000288
ERC-2014-ADG no. 671083European Research Councilhttp://dx.doi.org/10.13039/501100000781
MR/K001000/1Medical Research Councilhttp://dx.doi.org/10.13039/501100000265

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