Tropomyosin - master regulator of actin filament function in the cytoskeleton.

Gunning, Peter W. and Hardeman, Edna C. and Lappalainen, Pekka and Mulvihill, Daniel P. (2015) Tropomyosin - master regulator of actin filament function in the cytoskeleton. Journal of Cell Science, 128 (16). pp. 2965-2974. ISSN 0021-9533. (doi:https://doi.org/10.1242/jcs.172502) (Full text available)

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Abstract

Tropomyosin (Tpm) isoforms are the master regulators of the functions of individual actin filaments in fungi and metazoans. Tpms are coiled-coil parallel dimers that form a head-to-tail polymer along the length of actin filaments. Yeast only has two Tpm isoforms, whereas mammals have over 40. Each cytoskeletal actin filament contains a homopolymer of Tpm homodimers, resulting in a filament of uniform Tpm composition along its length. Evidence for this ‘master regulator’ role is based on four core sets of observation. First, spatially and functionally distinct actin filaments contain different Tpm isoforms, and recent data suggest that members of the formin family of actin filament nucleators can specify which Tpm isoform is added to the growing actin filament. Second, Tpms regulate whole-organism physiology in terms of morphogenesis, cell proliferation, vesicle trafficking, biomechanics, glucose metabolism and organ size in an isoform-specific manner. Third, Tpms achieve these functional outputs by regulating the interaction of actin filaments with myosin motors and actin-binding proteins in an isoform-specific manner. Last, the assembly of complex structures, such as stress fibers and podosomes involves the collaboration of multiple types of actin filament specified by their Tpm composition. This allows the cell to specify actin filament function in time and space by simply specifying their Tpm isoform composition.

Item Type: Article
Uncontrolled keywords: Actin cytoskeleton ; Isoforms ; Tropomyosin
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 17 Aug 2015 08:28 UTC
Last Modified: 26 May 2016 09:32 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/50202 (The current URI for this page, for reference purposes)
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