Journal
BIOCHEMISTRY-MOSCOW
Volume 76, Issue 13, Pages 1507-1527Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0006297911130098
Keywords
tropomyosin; coiled-coil proteins; regulation of muscle contraction
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Funding
- Russian Foundation for Basic Research [09-04-00266, 09-04-00339]
- Russian Academy of Science Presidium
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This review concerns the structure and functions of tropomyosin (TM), an actin-binding protein that plays a key role in the regulation of muscle contraction. The TM molecule is a dimer of alpha-helices, which form a coiled-coil. Recent views on the TM structure are analyzed, and special attention is concentrated on those structural traits of the TM molecule that distinguish it from the other coiled-coil proteins. Modern data are presented on TM functional properties, such as its interaction with actin and ability to move on the surface of actin filaments, which underlies the regulation of the actin-myosin interaction upon contraction of skeletal and cardiac muscles. Also, part of the review is devoted to analysis of the effects of mutations in TM genes associated with muscle diseases (myopathies) on the structure and functions of TM.
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