The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Dys  -  Dystrophin

Drosophila melanogaster

Synonyms: CG17750, CG31175, CG34157, CG7240, CG7243, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Dys

 

High impact information on Dys

 

Chemical compound and disease context of Dys

 

Biological context of Dys

  • The Drosophila homologue of the dystrophin gene - introns containing promoters are the major contributors to the large size of the gene [7].
  • Our results indicate that the postsynaptically localized scaffolding protein Dystrophin is required for appropriate control of neuromuscular synaptic homeostasis [1].
  • Members of this superfamily have been discovered in a relatively serendipitous way; we set out to compile a comprehensive description of dystrophin- and dystrobrevin-related sequences from available metazoan genome sequences, validated in representative organisms by RT-PCR, or acquired de novo from key species [8].
  • A Drosophila dystrophin-related protein, MSP-300, is required for embryonic muscle morphogenesis [9].
 

Anatomical context of Dys

  • As an integral component of the Dystrophin-associated glycoprotein complex, Dg plays a central role in linking the ECM and the cytoskeleton [10].
  • In expression and rescue studies, we show that lack of the large dystrophin isoforms in the postsynaptic muscle cell leads to elevated evoked neurotransmitter release from the presynaptic apparatus [1].
  • Dystrophin is required for appropriate retrograde control of neurotransmitter release at the Drosophila neuromuscular junction [1].
  • Despite significant progress over the past decade, many fundamental questions about the roles played by dystrophin and the other DGC proteins in the muscle and peripheral and central nervous systems remain to be answered [2].
  • Dystrophin is a 427-kDa cytoskeletal protein, which occurs in scant amounts in vertebrate muscle and nerve cells [11].
 

Other interactions of Dys

  • A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin [12].
  • kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin [13].
  • Spectrin and the related proteins dystrophin and alpha-actinin consist largely of repeated motifs of 100-120 residues [14].
 

Analytical, diagnostic and therapeutic context of Dys

References

  1. Dystrophin is required for appropriate retrograde control of neurotransmitter release at the Drosophila neuromuscular junction. van der Plas, M.C., Pilgram, G.S., Plomp, J.J., de Jong, A., Fradkin, L.G., Noordermeer, J.N. J. Neurosci. (2006) [Pubmed]
  2. Embryonic expression patterns of the Drosophila dystrophin-associated glycoprotein complex orthologs. Dekkers, L.C., van der Plas, M.C., van Loenen, P.B., den Dunnen, J.T., van Ommen, G.J., Fradkin, L.G., Noordermeer, J.N. Gene Expr. Patterns (2004) [Pubmed]
  3. Dissecting muscle and neuronal disorders in a Drosophila model of muscular dystrophy. Shcherbata, H.R., Yatsenko, A.S., Patterson, L., Sood, V.D., Nudel, U., Yaffe, D., Baker, D., Ruohola-Baker, H. EMBO J. (2007) [Pubmed]
  4. Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, vein, at the muscle-tendon junction site. Strumpf, D., Volk, T. J. Cell Biol. (1998) [Pubmed]
  5. Isolation and characterization of a Drosophila gene essential for early embryonic development and formation of cortical cleavage furrows. Zhang, C.X., Lee, M.P., Chen, A.D., Brown, S.D., Hsieh, T. J. Cell Biol. (1996) [Pubmed]
  6. Dystroglycan is required for polarizing the epithelial cells and the oocyte in Drosophila. Deng, W.M., Schneider, M., Frock, R., Castillejo-Lopez, C., Gaman, E.A., Baumgartner, S., Ruohola-Baker, H. Development (2003) [Pubmed]
  7. The Drosophila homologue of the dystrophin gene - introns containing promoters are the major contributors to the large size of the gene. Neuman, S., Kovalio, M., Yaffe, D., Nudel, U. FEBS Lett. (2005) [Pubmed]
  8. The dystrotelin, dystrophin and dystrobrevin superfamily: new paralogues and old isoforms. Jin, H., Tan, S., Hermanowski, J., Böhm, S., Pacheco, S., McCauley, J.M., Greener, M.J., Hinits, Y., Hughes, S.M., Sharpe, P.T., Roberts, R.G. BMC Genomics (2007) [Pubmed]
  9. A Drosophila dystrophin-related protein, MSP-300, is required for embryonic muscle morphogenesis. Rosenberg-Hasson, Y., Renert-Pasca, M., Volk, T. Mech. Dev. (1996) [Pubmed]
  10. Perlecan and Dystroglycan act at the basal side of the Drosophila follicular epithelium to maintain epithelial organization. Schneider, M., Khalil, A.A., Poulton, J., Castillejo-Lopez, C., Egger-Adam, D., Wodarz, A., Deng, W.M., Baumgartner, S. Development (2006) [Pubmed]
  11. Presence of invertebrate dystrophin-like products in obliquely striated muscle of the leech, Pontobdella muricata (Annelida, Hirudinea). Royuela, M., Paniagua, R., Rivier, F., Hugon, G., Robert, A., Mornet, D. Histochem. J. (1999) [Pubmed]
  12. A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin. Dubreuil, R.R., Byers, T.J., Stewart, C.T., Kiehart, D.P. J. Cell Biol. (1990) [Pubmed]
  13. kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin. Gregory, S.L., Brown, N.H. J. Cell Biol. (1998) [Pubmed]
  14. Phasing the conformational unit of spectrin. Winograd, E., Hume, D., Branton, D. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
 
WikiGenes - Universities