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The evolution of the dystroglycan complex, a major mediator of muscle integrity.

Adams JC, Brancaccio A - Biol Open (2015)

Bottom Line: This comprises the non-covalently-associated extracellular α-DG, that interacts with laminin in the BM, and the transmembrane β-DG, that interacts principally with dystrophin to connect to the actin cytoskeleton.Phylogenetic analysis based on the C-terminal IG2_MAT_NU region identified three distinct clades corresponding to deuterostomes, arthropods, and mollusks/early-diverging metazoans.Whereas the glycosyltransferases that modify α-DG are also present in choanoflagellates, the DG-binding proteins dystrophin and laminin originated at the base of the metazoa, and DG-associated sarcoglycan is restricted to cnidarians and bilaterians.

View Article: PubMed Central - PubMed

Affiliation: School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.

No MeSH data available.


Related in: MedlinePlus

. Multiple sequence alignments of functionally important regions from β-dystroglycan. Key as in Fig. 1. (A) Schematic of β-DG and the regions presented in the alignments. (B) The Gly-Ser α/β maturation site (**). (C) Region of the NU domain encompassing the two conserved Cys residues (*). (D) The dystrophin-binding site. The shade coding is as in Fig. 2. Codes for species names are as in Table 2. Tyr892 (*) is a phosphorylation site.
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BIO012468F4: . Multiple sequence alignments of functionally important regions from β-dystroglycan. Key as in Fig. 1. (A) Schematic of β-DG and the regions presented in the alignments. (B) The Gly-Ser α/β maturation site (**). (C) Region of the NU domain encompassing the two conserved Cys residues (*). (D) The dystrophin-binding site. The shade coding is as in Fig. 2. Codes for species names are as in Table 2. Tyr892 (*) is a phosphorylation site.

Mentions: β-DG is liberated upon proteolysis at the α/β cleavage site. It represents the transmembrane subunit of the DG complex and includes the natively unfolded region (Boffi et al., 2001) in its extracellular region and a cytoplasmic domain of about 120 aa that contains the dystrophin-binding site (DBS) at its C-terminus (Fig. 4A).Fig. 4


The evolution of the dystroglycan complex, a major mediator of muscle integrity.

Adams JC, Brancaccio A - Biol Open (2015)

. Multiple sequence alignments of functionally important regions from β-dystroglycan. Key as in Fig. 1. (A) Schematic of β-DG and the regions presented in the alignments. (B) The Gly-Ser α/β maturation site (**). (C) Region of the NU domain encompassing the two conserved Cys residues (*). (D) The dystrophin-binding site. The shade coding is as in Fig. 2. Codes for species names are as in Table 2. Tyr892 (*) is a phosphorylation site.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4582122&req=5

BIO012468F4: . Multiple sequence alignments of functionally important regions from β-dystroglycan. Key as in Fig. 1. (A) Schematic of β-DG and the regions presented in the alignments. (B) The Gly-Ser α/β maturation site (**). (C) Region of the NU domain encompassing the two conserved Cys residues (*). (D) The dystrophin-binding site. The shade coding is as in Fig. 2. Codes for species names are as in Table 2. Tyr892 (*) is a phosphorylation site.
Mentions: β-DG is liberated upon proteolysis at the α/β cleavage site. It represents the transmembrane subunit of the DG complex and includes the natively unfolded region (Boffi et al., 2001) in its extracellular region and a cytoplasmic domain of about 120 aa that contains the dystrophin-binding site (DBS) at its C-terminus (Fig. 4A).Fig. 4

Bottom Line: This comprises the non-covalently-associated extracellular α-DG, that interacts with laminin in the BM, and the transmembrane β-DG, that interacts principally with dystrophin to connect to the actin cytoskeleton.Phylogenetic analysis based on the C-terminal IG2_MAT_NU region identified three distinct clades corresponding to deuterostomes, arthropods, and mollusks/early-diverging metazoans.Whereas the glycosyltransferases that modify α-DG are also present in choanoflagellates, the DG-binding proteins dystrophin and laminin originated at the base of the metazoa, and DG-associated sarcoglycan is restricted to cnidarians and bilaterians.

View Article: PubMed Central - PubMed

Affiliation: School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.

No MeSH data available.


Related in: MedlinePlus