Tropomodulin function and thin filament assembly in cardiac myocytes

Carol Gregorio, Velia M. Fowler

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The regulation of thin filament length is a fundamental property of all striated muscles. Tropomodulin is an actin and tropomyosin binding protein that is exclusively associated with the free (pointed) ends of thin filaments. In vitro and in vivo studies reveal that tropomodulin is an actin filament pointed end capping protein, which is required to maintain the final length of thin filaments and is essential for contractile activity in embryonic chick cardiac myocytes. Understanding the mechanisms of thin filament assembly, as well as determining the roles of proteins modulating actin filament dynamics, is important for future considerations of the molecular bases for myopathies seen in various types of heart disease.

Original languageEnglish (US)
Pages (from-to)136-141
Number of pages6
JournalTrends in Cardiovascular Medicine
Volume6
Issue number4
DOIs
StatePublished - May 1996
Externally publishedYes

Fingerprint

Tropomodulin
Actin Cytoskeleton
Cardiac Myocytes
Microfilament Proteins
Tropomyosin
Striated Muscle
Muscular Diseases
Heart Diseases
Proteins

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine

Cite this

Tropomodulin function and thin filament assembly in cardiac myocytes. / Gregorio, Carol; Fowler, Velia M.

In: Trends in Cardiovascular Medicine, Vol. 6, No. 4, 05.1996, p. 136-141.

Research output: Contribution to journalArticle

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