Alteration of tropomyosin-binding properties of tropomodulin-1 affects its capping ability and localization in skeletal myocytes

Natalia A. Moroz, Stefanie M. Novak, Ricardo Azevedo, Mert Colpan, Vladimir N. Uversky, Carol Gregorio, Alla S. Kostyukova

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Background: Tropomodulin is a tropomyosin-dependent actin-capping protein. Results: Mutations intropomodulin-1 that reduce its affinity for tropomyosin (R11K, D12N, Q144K) reduced inhibition of actin pointed-end polymerization in vitro and decreased assembly of tropomodulin-1 in skeletal myocytes. Conclusion: The tropomyosin-binding ability of tropomodulin-1 directly influences its actin filament regulatory activity. Significance: Creating a tool for studying the roles of different tropomodulin isoforms in living cells.

Original languageEnglish (US)
Pages (from-to)4899-4907
Number of pages9
JournalJournal of Biological Chemistry
Volume288
Issue number7
DOIs
StatePublished - Feb 15 2013

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Tropomodulin
Tropomyosin
Skeletal Muscle Fibers
Actins
Actin Capping Proteins
Actin Cytoskeleton
Polymerization
Protein Isoforms
Cells
Mutation

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Alteration of tropomyosin-binding properties of tropomodulin-1 affects its capping ability and localization in skeletal myocytes. / Moroz, Natalia A.; Novak, Stefanie M.; Azevedo, Ricardo; Colpan, Mert; Uversky, Vladimir N.; Gregorio, Carol; Kostyukova, Alla S.

In: Journal of Biological Chemistry, Vol. 288, No. 7, 15.02.2013, p. 4899-4907.

Research output: Contribution to journalArticle

Moroz, Natalia A. ; Novak, Stefanie M. ; Azevedo, Ricardo ; Colpan, Mert ; Uversky, Vladimir N. ; Gregorio, Carol ; Kostyukova, Alla S. / Alteration of tropomyosin-binding properties of tropomodulin-1 affects its capping ability and localization in skeletal myocytes. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 7. pp. 4899-4907.
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AU - Gregorio, Carol

AU - Kostyukova, Alla S.

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