Tropomyosin-binding properties modulate competition between tropomodulin isoforms

Mert Colpan; Natalia A Moroz; Kevin T Gray; Dillon A Cooper; Christian A Diaz; Alla S Kostyukova

doi:10.1016/j.abb.2016.04.006

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Tropomyosin-binding properties modulate competition between tropomodulin isoforms

Journal article

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Tropomyosin-binding properties modulate competition between tropomodulin isoforms

Mert Colpan, Natalia A Moroz, Kevin T Gray, Dillon A Cooper, Christian A Diaz and Alla S Kostyukova

Archives of biochemistry and biophysics, Vol.600, pp.23-32

06/15/2016

DOI: https://doi.org/10.1016/j.abb.2016.04.006

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https://hdl.handle.net/2376/103927

PMCID: PMC5079755

PMID: 27091317

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https://doi.org/10.1016/j.abb.2016.04.006View

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Abstract

Tropomodulin - chemistry

Tropomodulin - ultrastructure

Protein Isoforms - chemistry

Protein Binding

Tropomyosin - ultrastructure

Structure-Activity Relationship

Protein Isoforms - ultrastructure

Tropomyosin - chemistry

Binding Sites

The formation and fine-tuning of cytoskeleton in cells are governed by proteins that influence actin filament dynamics. Tropomodulin (Tmod) regulates the length of actin filaments by capping the pointed ends in a tropomyosin (TM)-dependent manner. Tmod1, Tmod2 and Tmod3 are associated with the cytoskeleton of non-muscle cells and their expression has distinct consequences on cell morphology. To understand the molecular basis of differences in the function and localization of Tmod isoforms in a cell, we compared the actin filament-binding abilities of Tmod1, Tmod2 and Tmod3 in the presence of Tpm3.1, a non-muscle TM isoform. Tmod3 displayed preferential binding to actin filaments when competing with other isoforms. Mutating the second or both TM-binding sites of Tmod3 destroyed its preferential binding. Our findings clarify how Tmod1, Tmod2 and Tmod3 compete for binding actin filaments. Different binding mechanisms and strengths of Tmod isoforms for Tpm3.1 contribute to their divergent functional capabilities.

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Title: Tropomyosin-binding properties modulate competition between tropomodulin isoforms
Creators: Mert Colpan - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States. Electronic address: mert.colpan@wsu.edu
Natalia A Moroz - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States
Kevin T Gray - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States
Dillon A Cooper - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States
Christian A Diaz - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States
Alla S Kostyukova - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States. Electronic address: alla.kostyukova@wsu.edu
Publication Details: Archives of biochemistry and biophysics, Vol.600, pp.23-32
Academic Unit: Plant Pathology, Department of; Chemical Engineering and Bioengineering, School of
Publisher: United States
Grant note: R01 GM081688 / NIGMS NIH HHS T32 GM008336 / NIGMS NIH HHS
Identifiers: 99900547088401842
Language: English
Resource Type: Journal article