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Polymorphism in tropomyosin structure and function

Janco, Miro, Suphamungmee, Worawit, Li, Xiaochuan, Lehman, William, Lehrer, Sherwin S., Geeves, Michael A. (2013) Polymorphism in tropomyosin structure and function. Journal of Muscle Research and Cell Motility, 34 (3-4). pp. 177-187. ISSN 0142-4319. (doi:10.1007/s10974-013-9353-x) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:37097)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1007/s10974-013-9353-x

Abstract

Tropomyosins (Tm) in humans are expressed from four distinct genes and by alternate splicing >40 different Tm polypeptide chains can be made. The functional Tm unit is a dimer of two parallel polypeptide chains and these can be assembled from identical (homodimer) or different (heterodimer) polypeptide chains provided both chains are of the same length. Since most cells express multiple isoforms of Tm, the number of different homo and heterodimers that can be assembled becomes very large. We review the mechanism of dimer assembly and how preferential assembly of some heterodimers is driven by thermodynamic stability. We examine how in vitro studies can reveal functional differences between Tm homo and heterodimers (stability, actin affinity, flexibility) and the implication for how there could be selection of Tm isomers in the assembly on to an actin filament. The role of Tm heterodimers becomes more complex when mutations in Tm are considered, such as those associated with cardiomyopathies, since mutations can appear in only one of the chains.

Item Type: Article
DOI/Identification number: 10.1007/s10974-013-9353-x
Uncontrolled keywords: Heterodimers and homodimers Tropomyosin isoforms Coiled-coils Actin Cardiomyopathy mutations
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 02 Dec 2013 14:07 UTC
Last Modified: 05 Nov 2024 10:21 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/37097 (The current URI for this page, for reference purposes)

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