Dystroglycan: Difference between revisions
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* [http://www.sdbonline.org/fly/sturtevant/dystrog1.htm Overview at sdbonline.org] |
* [http://www.sdbonline.org/fly/sturtevant/dystrog1.htm Overview at sdbonline.org] |
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* http://www.neuro.wustl.edu/neuromuscular/musdist/dag2.htm#ad |
* http://www.neuro.wustl.edu/neuromuscular/musdist/dag2.htm#ad |
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* [http://www.immunoportal.com/modules.php?name=gallery2&g2_view=keyalbum.KeywordAlbum&g2_keyword=Dystroglycan Immunohistochemistry Image Gallery: Dystroglycan] |
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Revision as of 11:00, 28 January 2010
Template:PBB
Dystroglycan is a protein that in humans is encoded by the DAG1 gene.[1][2][3]
Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in Homo sapiens by chromosome 3.[4] There are two exons that are separated by a large intron. The spliced exons codes for a protein product is finally cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal).
Function
In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin [alpha]-2 laminin in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan.
Expression
Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in Mus musculus brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear
Interactions
Dystroglycan has been shown to interact with FYN,[5] C-src tyrosine kinase,[5] Src,[5] NCK1,[5] Grb2,[6] Caveolin 3[7] and SHC1.[5]
See also
References
- ^ Skynner MJ, Gangadharan U, Coulton GR, Mason RM, Nikitopoulou A, Brown SD, Blanco G (1995). "Genetic mapping of the mouse neuromuscular mutation kyphoscoliosis". Genomics. 25 (1): 207–13. PMID 7774920.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, Campbell KP (1992). "Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix". Nature. 355 (6362): 696–702. doi:10.1038/355696a0. PMID 1741056.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ "Entrez Gene: DAG1 dystroglycan 1 (dystrophin-associated glycoprotein 1)".
- ^ Spence HJ, Dhillon AS, James M, Winder SJ (2004). "Dystroglycan, a scaffold for the ERK-MAP kinase cascade". EMBO Rep. 5 (5): 484–9. doi:10.1038/sj.embor.7400140. PMID 15071496.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ a b c d e Sotgia, F (2001). "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins". Biochemistry. 40 (48). United States: 14585–92. ISSN 0006-2960. PMID 11724572.
{{cite journal}}: Check date values in:|year=(help); Cite has empty unknown parameters:|laydate=,|laysource=, and|laysummary=(help); Unknown parameter|coauthors=ignored (|author=suggested) (help); Unknown parameter|month=ignored (help); Unknown parameter|quotes=ignored (help)CS1 maint: year (link) - ^ Yang, B (1995). "SH3 domain-mediated interaction of dystroglycan and Grb2". J. Biol. Chem. 270 (20). UNITED STATES: 11711–4. ISSN 0021-9258. PMID 7744812.
{{cite journal}}: Check date values in:|year=(help); Cite has empty unknown parameters:|laydate=,|laysource=, and|laysummary=(help); Unknown parameter|coauthors=ignored (|author=suggested) (help); Unknown parameter|month=ignored (help); Unknown parameter|quotes=ignored (help)CS1 maint: year (link) - ^ Sotgia, F (2000). "Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members". J. Biol. Chem. 275 (48). UNITED STATES: 38048–58. doi:10.1074/jbc.M005321200. ISSN 0021-9258. PMID 10988290.
{{cite journal}}: Check date values in:|year=(help); Cite has empty unknown parameters:|laydate=,|laysource=, and|laysummary=(help); Unknown parameter|coauthors=ignored (|author=suggested) (help); Unknown parameter|month=ignored (help); Unknown parameter|quotes=ignored (help)CS1 maint: unflagged free DOI (link) CS1 maint: year (link)
Further reading
PDB gallery | |
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External links
- Dystroglycans at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Overview at sdbonline.org
- http://www.neuro.wustl.edu/neuromuscular/musdist/dag2.htm#ad
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