Tropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro.

ABSTRACT: Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [1]. Tropomyosins are coiled-coil dimers that form head-to-tail polymers along actin filaments and regulate interactions of other proteins, including actin-depolymerizing factor (ADF)/cofilins and myosins, with actin [2-5]. In mammals, >40 tropomyosin isoforms can be generated through alternative splicing from four tropomyosin genes. Different isoforms display non-redundant functions and partially non-overlapping localization patterns, for example within the stress fiber network [6, 7]. Based on cell biological studies, it was thus proposed that tropomyosin isoforms may specify the functional properties of different actin filament populations [2]. To test this hypothesis, we analyzed the pro

SUBMITTER: Gateva G 

PROVIDER: S-EPMC5344678 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature