The troponin complex and regulation of muscle contraction - PubMed (original) (raw)
Review
The troponin complex and regulation of muscle contraction
C S Farah et al. FASEB J. 1995 Jun.
Abstract
In a wide variety of cellular settings, from organelle transport to muscle contraction, Ca2+ binding to members of the EF hand family of proteins controls the interaction between actin and different myosins that are responsible for generating movement. In vertebrate skeletal and cardiac muscle the Ca(2+)-binding protein troponin C (TnC) is one subunit of the ternary troponin complex which, through its association with actin and tropomyosin on the thin filament, inhibits the actomyosin interaction at submicromolar Ca2+ concentrations and stimulates the interaction at micromolar Ca2+ concentrations. Because TnC does not interact directly with actin or tropomyosin, the Ca(2+)-binding signal must be transmitted to the thin filament via the other two troponin subunits: troponin I (TnI), the inhibitory subunit, and troponin T (TnT), the tropomyosin-binding subunit. Thus, the troponin complex is a Ca(2+)-sensitive molecular switch and the structures of and interactions between its components have been of great interest for many years. Although the crystal structure of TnC has been known for almost a decade, the molecular structures of TnI and TnT are not known and therefore convincing models of the organization of the troponin complex and the Ca(2+)-induced changes in its structure have not been forthcoming. Recent advances on a wide variety of fronts including 1) the bacterial expression and characterization of mutants of TnC, TnI, and TnT; 2) cross-linking and fluorescence studies; and 3) the determination of the crystal and nuclear magnetic resonance structures of synthetic and recombinant troponin fragments and complexes between EF hand proteins and their target peptides have provided new insights into the nature of the interactions between troponin subunits. This review discusses these recent advances with the aim of critically assessing molecular models of the nature of the Ca(2+)-induced structural transition in troponin.
Similar articles
- Structural basis for Ca2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin.
Murakami K, Yumoto F, Ohki SY, Yasunaga T, Tanokura M, Wakabayashi T. Murakami K, et al. J Mol Biol. 2005 Sep 9;352(1):178-201. doi: 10.1016/j.jmb.2005.06.067. J Mol Biol. 2005. PMID: 16061251 - A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction.
Potter JD, Sheng Z, Pan BS, Zhao J. Potter JD, et al. J Biol Chem. 1995 Feb 10;270(6):2557-62. doi: 10.1074/jbc.270.6.2557. J Biol Chem. 1995. PMID: 7852318 - Structural interactions responsible for the assembly of the troponin complex on the muscle thin filament.
Reinach FC, Farah CS, Monteiro PB, Malnic B. Reinach FC, et al. Cell Struct Funct. 1997 Feb;22(1):219-23. doi: 10.1247/csf.22.219. Cell Struct Funct. 1997. PMID: 9113410 Review. - Regulation of contraction in striated muscle.
Gordon AM, Homsher E, Regnier M. Gordon AM, et al. Physiol Rev. 2000 Apr;80(2):853-924. doi: 10.1152/physrev.2000.80.2.853. Physiol Rev. 2000. PMID: 10747208 Review.
Cited by
- Correlating calcium binding, Förster resonance energy transfer, and conformational change in the biosensor TN-XXL.
Geiger A, Russo L, Gensch T, Thestrup T, Becker S, Hopfner KP, Griesinger C, Witte G, Griesbeck O. Geiger A, et al. Biophys J. 2012 May 16;102(10):2401-10. doi: 10.1016/j.bpj.2012.03.065. Epub 2012 May 15. Biophys J. 2012. PMID: 22677394 Free PMC article. - Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C.
Davis JP, Norman C, Kobayashi T, Solaro RJ, Swartz DR, Tikunova SB. Davis JP, et al. Biophys J. 2007 May 1;92(9):3195-206. doi: 10.1529/biophysj.106.095406. Epub 2007 Feb 9. Biophys J. 2007. PMID: 17293397 Free PMC article. - Using lanthanide ions to align troponin complexes in solution: order of lanthanide occupancy in cardiac troponin C.
Gay GL, Lindhout DA, Sykes BD. Gay GL, et al. Protein Sci. 2004 Mar;13(3):640-51. doi: 10.1110/ps.03412704. Protein Sci. 2004. PMID: 14978304 Free PMC article. - Maximum likelihood methods for detecting adaptive evolution after gene duplication.
Bielawski JP, Yang Z. Bielawski JP, et al. J Struct Funct Genomics. 2003;3(1-4):201-12. J Struct Funct Genomics. 2003. PMID: 12836699 Review. - The molecular genetic basis for hypertrophic cardiomyopathy.
Marian AJ, Roberts R. Marian AJ, et al. J Mol Cell Cardiol. 2001 Apr;33(4):655-70. doi: 10.1006/jmcc.2001.1340. J Mol Cell Cardiol. 2001. PMID: 11273720 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous