The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast.

Coulton, A.T. and East, D.A. and Galinska-Rakoczy, Agnieszka and Lehman, W. and Mulvihill, D.P. (2010) The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. Journal of Cell Science, 123 . pp. 3235-3243. ISSN 0021-9533 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1242/jcs.069971

Abstract

Tropomyosin (Tm) is a conserved dimeric coiled-coil protein, which forms polymers that curl around actin filaments in order to regulate actomyosin function. Acetylation of the Tm N-terminal methionine strengthens end-to-end bonds, which enhances actin binding as well as the ability of Tm to regulate myosin motor activity in both muscle and non-muscle cells. In this study we explore the function of each Tm form within fission yeast cells. Electron microscopy and live cell imaging revealed that acetylated and unacetylated Tm associate with distinct actin structures within the cell, and that each form has a profound effect upon the shape and integrity of the polymeric actin filament. We show that, whereas Tm acetylation is required to regulate the in vivo motility of class II myosins, acetylated Tm had no effect on the motility of class I and V myosins. These findings illustrate a novel Tm-acetylation-state-dependent mechanism for regulating specific actomyosin cytoskeletal interactions.

Item Type: Article
Subjects: Q Science > QH Natural history > QH426 Genetics
Q Science > QH Natural history > QH301 Biology
Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Cell & Developmental Biology Group
Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Dan Mulvihill
Date Deposited: 11 Sep 2010 08:53
Last Modified: 30 Nov 2011 12:33
Resource URI: http://kar.kent.ac.uk/id/eprint/25500 (The current URI for this page, for reference purposes)
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