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

Palani, Saravanan, Köster, Darius V., Hatano, Tomoyuki, Kamnev, Anton, Kanamaru, Taishi, Brooker, Holly, Hernandez-Fernaud, Juan Ramon, Jones, Alexandra M.E., Millar, Jonathan B.A., Mulvihill, Daniel P., and others. (2019) Phosphoregulation of tropomyosin is crucial for actin cable turnover and division site placement. Journal of Cell Biology, 218 (11). p. 3548. ISSN 0021-9525. E-ISSN 1540-8140. (doi:10.1083/jcb.201809089)

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Abstract

Tropomyosin is a coiled-coil actin binding protein key to the stability of actin filaments. Whereas, in muscle cells, tropomyosin is subject to calcium regulation, its regulation in non-muscle 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 non-muscle tropomyosins, which in fission yeast controls actin filament stability and division site placement.

Item Type: Article
DOI/Identification number: 10.1083/jcb.201809089
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Dan Mulvihill
Date Deposited: 10 Sep 2019 07:43 UTC
Last Modified: 25 Nov 2019 13:06 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/75989 (The current URI for this page, for reference purposes)
Mulvihill, Daniel P.: https://orcid.org/0000-0003-2502-5274
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