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Gene Review

dgn-1  -  Protein DGN-1

Caenorhabditis elegans

 
 
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High impact information on dgn-1

  • Basement membrane assembly is a cooperative process in which laminins polymerize through their LN domains and anchor to the cell surface through their G domains; this leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin [1].
  • Unlike vertebrate DG, DGN-1 is not expressed in muscle or required for muscle function. dgn-1 null mutants are viable but sterile owing to severe disorganization of the somatic gonad epithelium, and show defects in vulval and excretory cell epithelia and in motoneuron axon guidance [2].
  • Dystroglycan is a novel laminin receptor that links the extracellular matrix and sarcolemma in skeletal muscle [3].
  • The specific dystroglycan-Grb2 interaction may play an important role in extracellular matrix-mediated signal transduction and/or cytoskeleton organization in skeletal muscle that may be essential for muscle cell viability [3].
  • The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors [4].

References

  1. Assembly and tissue functions of early embryonic laminins and netrins. Yurchenco, P.D., Wadsworth, W.G. Curr. Opin. Cell Biol. (2004) [Pubmed]
  2. C. elegans dystroglycan DGN-1 functions in epithelia and neurons, but not muscle, and independently of dystrophin. Johnson, R.P., Kang, S.H., Kramer, J.M. Development (2006) [Pubmed]
  3. SH3 domain-mediated interaction of dystroglycan and Grb2. Yang, B., Jung, D., Motto, D., Meyer, J., Koretzky, G., Campbell, K.P. J. Biol. Chem. (1995) [Pubmed]
  4. Form and function: the laminin family of heterotrimers. Colognato, H., Yurchenco, P.D. Dev. Dyn. (2000) [Pubmed]
 
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