Tropomyosin-mediated Regulation of Cytoplasmic Myosins

Manstein, Dietmar J. and Mulvihill, Daniel P. (2016) Tropomyosin-mediated Regulation of Cytoplasmic Myosins. Traffic, 17 (8). pp. 872-877. ISSN 1398-9219. (doi:https://doi.org/10.1111/tra.12399) (Full text available)

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http://www.dx.doi.org/10.1111/tra.12399

Abstract

The ability of the actin-based cytoskeleton to rapidly reorganize is critical for maintaining cell organization and viability. The plethora of activities in which actin polymers participate require different biophysical properties, which can vary significantly between the different events that often occur simultaneously at separate cellular locations. In order to modify the biophysical properties of an actin polymer for a particular function, the cell contains diverse actin-binding proteins that modulate the growth, regulation and molecular interactions of actin-based structures according to functional requirements. In metazoan and yeast cells, tropomyosin is a key regulator of actin-based structures. Cells have the capacity to produce multiple tropomyosin isoforms, each capable of specifically associating as copolymers with actin at distinct cellular locations to fine-tune the functional properties of discrete actin structures. Here, we present a unifying theory in which tropomyosin isoforms critically define the surface landscape of copolymers with cytoplasmic β- or γ-actin. Decoration of filamentous actin with different tropomyosin isoforms determines the identity and modulates the activity of the interacting myosin motor proteins. Conversely, changes in the nucleotide state of actin and posttranslational modifications affect the composition, morphology, subcellular localization and allosteric coupling of the associated actin-based superstructures.

Item Type: Article
Uncontrolled keywords: actin; allostery; cytoskeleton; isoforms; multigene family; myosin; protein complex; tropomyosin
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 25 May 2016 15:17 UTC
Last Modified: 22 May 2017 09:30 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/55694 (The current URI for this page, for reference purposes)
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