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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 α-dystroglycan. The dataset includes representative species from the phyla in which DG was identified. (A) Schematic of α-DG and the regions presented in the alignments. Key as in Fig. 1. (B) Thr192 (*) and the surrounding secondary structure at the beginning of the S6 domain. (C) The furin cleavage site and the Thr-Pro-Thr motif (* *) at the beginning of the mucin-like region. (D) The last two β-strands (dashed line) of the IG2 domain, followed by a spacer region that precedes MAT. The conserved Gly563, Pro565 and Ile593 are also pinpointed by asterisks. Alignments were prepared as in Fig. 2. Codes for species names are as in Table 2.
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BIO012468F3: Multiple sequence alignments of functionally important regions from α-dystroglycan. The dataset includes representative species from the phyla in which DG was identified. (A) Schematic of α-DG and the regions presented in the alignments. Key as in Fig. 1. (B) Thr192 (*) and the surrounding secondary structure at the beginning of the S6 domain. (C) The furin cleavage site and the Thr-Pro-Thr motif (* *) at the beginning of the mucin-like region. (D) The last two β-strands (dashed line) of the IG2 domain, followed by a spacer region that precedes MAT. The conserved Gly563, Pro565 and Ile593 are also pinpointed by asterisks. Alignments were prepared as in Fig. 2. Codes for species names are as in Table 2.

Mentions: As introduced above, the domain architecture of αDG includes the N-terminal IG1 and S6 domains, followed by the central mucin-like region and the IG2 domain; the latter anticipates the α/β maturation interface (Fig. 3A). A number of key functional motifs are recognized within mammalian α-DG. We examined the conservation of these motifs by multiple sequence alignments of DGs from species representative of the phyla identified in our phylogenetic survey.Fig. 3.


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 α-dystroglycan. The dataset includes representative species from the phyla in which DG was identified. (A) Schematic of α-DG and the regions presented in the alignments. Key as in Fig. 1. (B) Thr192 (*) and the surrounding secondary structure at the beginning of the S6 domain. (C) The furin cleavage site and the Thr-Pro-Thr motif (* *) at the beginning of the mucin-like region. (D) The last two β-strands (dashed line) of the IG2 domain, followed by a spacer region that precedes MAT. The conserved Gly563, Pro565 and Ile593 are also pinpointed by asterisks. Alignments were prepared as in Fig. 2. Codes for species names are as in Table 2.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

BIO012468F3: Multiple sequence alignments of functionally important regions from α-dystroglycan. The dataset includes representative species from the phyla in which DG was identified. (A) Schematic of α-DG and the regions presented in the alignments. Key as in Fig. 1. (B) Thr192 (*) and the surrounding secondary structure at the beginning of the S6 domain. (C) The furin cleavage site and the Thr-Pro-Thr motif (* *) at the beginning of the mucin-like region. (D) The last two β-strands (dashed line) of the IG2 domain, followed by a spacer region that precedes MAT. The conserved Gly563, Pro565 and Ile593 are also pinpointed by asterisks. Alignments were prepared as in Fig. 2. Codes for species names are as in Table 2.
Mentions: As introduced above, the domain architecture of αDG includes the N-terminal IG1 and S6 domains, followed by the central mucin-like region and the IG2 domain; the latter anticipates the α/β maturation interface (Fig. 3A). A number of key functional motifs are recognized within mammalian α-DG. We examined the conservation of these motifs by multiple sequence alignments of DGs from species representative of the phyla identified in our phylogenetic survey.Fig. 3.

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