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Tropomyosin‐Mediated Regulation of Cytoplasmic Myosins
Author(s) -
Manstein Dietmar J.,
Mulvihill Daniel P.
Publication year - 2016
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12399
Subject(s) - tropomyosin , biology , microbiology and biotechnology , actin binding protein , actin , myosin , actin remodeling , cytoplasm , mdia1 , actin cytoskeleton , cytoskeleton , biochemistry , cell
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.