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Gene Review

Myom1  -  myomesin 1

Mus musculus

Synonyms: D430047A17Rik, Myomesin family member 1, Myomesin-1, Skelemin, skelemin
 
 
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High impact information on Myom1

  • Cells transiently expressing skelemin C2 motifs, which contain the integrin binding site, failed to form integrin clusters or to spread on a substrate for beta1- and beta3-integrins [1].
  • Dynamic modulation of cytoskeletal proteins linking integrins to signaling complexes in spreading cells. Role of skelemin in initial integrin-induced spreading [1].
  • Skelemin, a protein shown recently to interact with beta1- and beta3-integrin in vitro, colocalized with integrin in calpain-induced clusters but was absent from focal adhesions [1].
  • This study suggests the presence of a skelemin-like protein in non-muscle cells and provides evidence that it may be involved in linking integrins to the cytoskeleton [2].
  • Full-length skelemin interacted with integrin in intact cells as demonstrated by the colocalization of hemagglutinin-tagged skelemin in Chinese hamster ovary (CHO) cells containing alphaIIbbeta3-integrin and by the finding that microinjection of C2 motif 4 of skelemin into C2C12 mouse myoblast cells caused spread cells to round up [2].
 

Biological context of Myom1

  • Anti-skelemin antibodies bound to the protein products of each of three nonoverlapping regions of the open reading frame [3].
  • We found that the loss of titin's kinase domain and binding sites for myomesin and MURF-1 causes structural changes in the sarcomere that proceed from the M-line to the Z-disc and ultimately result in disassembly of the sarcomere [4].
  • CAT expression assays using promoter deletion constructs identified three regions that seem to be important for the muscle-specific transcriptional activation of the myomesin gene [5].
 

Anatomical context of Myom1

 

Associations of Myom1 with chemical compounds

  • The amino acid residues in the isolated clones encompassed C2 motifs 4 and 5 of skelemin [2].
 

Other interactions of Myom1

 

Analytical, diagnostic and therapeutic context of Myom1

References

  1. Dynamic modulation of cytoskeletal proteins linking integrins to signaling complexes in spreading cells. Role of skelemin in initial integrin-induced spreading. Reddy, K.B., Bialkowska, K., Fox, J.E. J. Biol. Chem. (2001) [Pubmed]
  2. Identification of an interaction between the m-band protein skelemin and beta-integrin subunits. Colocalization of a skelemin-like protein with beta1- and beta3-integrins in non-muscle cells. Reddy, K.B., Gascard, P., Price, M.G., Negrescu, E.V., Fox, J.E. J. Biol. Chem. (1998) [Pubmed]
  3. Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of adhesion/recognition and intermediate filament proteins. Price, M.G., Gomer, R.H. J. Biol. Chem. (1993) [Pubmed]
  4. Muscle atrophy in Titin M-line deficient mice. Peng, J., Raddatz, K., Labeit, S., Granzier, H., Gotthardt, M. J. Muscle Res. Cell. Motil. (2005) [Pubmed]
  5. M band proteins myomesin and skelemin are encoded by the same gene: analysis of its organization and expression. Steiner, F., Weber, K., Fürst, D.O. Genomics (1999) [Pubmed]
  6. Stimulation and inhibition of myoblast differentiation by hormones. Florini, J.R., Ewton, D.Z., Evinger-Hodges, M.J., Falen, S.L., Lau, R.L., Regan, J.F., Vertel, B.M. In vitro. (1984) [Pubmed]
 
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