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Gene Review

Tmod1  -  tropomodulin 1

Rattus norvegicus

Synonyms: E-Tmod, Erythrocyte tropomodulin, Tmod, Tropomodulin-1
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High impact information on Tmod1

  • Administration of the calcineurin inhibitors cyclosporin and FK506 prevented disease in mice that were genetically predisposed to develop HCM as a result of aberrant expression of tropomodulin, myosin light chain-2, or fetal beta-tropomyosin in the heart [1].
  • Immunoblotting of supernatants and pellets obtained after extraction of myosin from myofibrils also indicates that tropomodulin remains associated with the thin filaments [2].
  • Tropomodulin is a new, 40.6-kD tropomyosin-binding protein from the human erythrocyte membrane skeleton that binds to one end of erythrocyte tropomyosin and blocks head-to-tail association of tropomyosin molecules along actin filaments [2].
  • Here we show that rat psoas skeletal muscle contains tropomodulin based on immunoreactivity, identical apparent mobility on SDS gels, and ability to bind muscle tropomyosin [2].
  • Tropomodulin is a 40.6-kD protein that colocalizes with actin filament pointed ends in skeletal muscle [3].

Biological context of Tmod1


Anatomical context of Tmod1

  • Peptide sequencing as well as immunoblotting showed that one of the two proteins is identical to tropomodulin, a tropomyosin-binding protein originally identified in erythrocytes [4].
  • Tropomodulin (Tmod) is a cytoskeletal actin-capping protein that interacts with tropomyosin at the pointed end of actin filaments [5].
  • E-Tmod is an isoform that expresses predominantly in cardiac cells and slow skeletal muscle fibers [5].
  • 1.2-1.6 copies of muscle tropomodulin are present per thin filament in myofibrils, supporting the possibility that one or two tropomodulin molecules may be associated with the two terminal tropomyosin molecules at the pointed end of each thin filament [2].
  • Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development [3].

Associations of Tmod1 with chemical compounds


Analytical, diagnostic and therapeutic context of Tmod1


  1. Prevention of cardiac hypertrophy in mice by calcineurin inhibition. Sussman, M.A., Lim, H.W., Gude, N., Taigen, T., Olson, E.N., Robbins, J., Colbert, M.C., Gualberto, A., Wieczorek, D.F., Molkentin, J.D. Science (1998) [Pubmed]
  2. Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle. Fowler, V.M., Sussmann, M.A., Miller, P.G., Flucher, B.E., Daniels, M.P. J. Cell Biol. (1993) [Pubmed]
  3. Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development. Sussman, M.A., Sakhi, S., Barrientos, P., Ito, M., Kedes, L. Circ. Res. (1994) [Pubmed]
  4. N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin. Watakabe, A., Kobayashi, R., Helfman, D.M. J. Cell. Sci. (1996) [Pubmed]
  5. Cytoplasmic nuclear transfer of the actin-capping protein tropomodulin. Kong, K.Y., Kedes, L. J. Biol. Chem. (2004) [Pubmed]
  6. Tropomodulin increases the critical concentration of barbed end-capped actin filaments by converting ADP.P(i)-actin to ADP-actin at all pointed filament ends. Weber, A., Pennise, C.R., Fowler, V.M. J. Biol. Chem. (1999) [Pubmed]
  7. Identification, expression analysis and polymorphism of a novel RLTPR gene encoding a RGD motif, tropomodulin domain and proline/leucine-rich regions. Matsuzaka, Y., Okamoto, K., Mabuchi, T., Iizuka, M., Ozawa, A., Oka, A., Tamiya, G., Kulski, J.K., Inoko, H. Gene (2004) [Pubmed]
  8. Identification and characterization of tropomodulin and tropomyosin in the adult rat lens. Woo, M.K., Fowler, V.M. J. Cell. Sci. (1994) [Pubmed]
  9. Neural tropomodulin: developmental expression and effect of seizure activity. Sussman, M.A., Sakhi, S., Tocco, G., Najm, I., Baudry, M., Kedes, L., Schreiber, S.S. Brain Res. Dev. Brain Res. (1994) [Pubmed]
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