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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.


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A model for the evolution of dystroglycan and the DGC. See text for details.
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BIO012468F7: A model for the evolution of dystroglycan and the DGC. See text for details.

Mentions: We propose that the ancestral DG included a signal peptide, the IG2-MAT-NU region, transmembrane and a cytoplasmic domain with a dystrophin-binding motif. This protein might have included a serine/threonine-rich region proximal to the N-terminus; alternatively, this region may have become incorporated subsequently by domain shuffling. We speculate that this protein had weak laminin-binding activity (Fig. 7A). Rapid evolution of the N-terminal region resulting from domain duplication and shuffling of the IG domain then gave rise to the IG1 domain, in conjunction with incorporation of the S6 domain by domain shuffling from another genomic locus, and evolution of the Ser/Thr-rich region to a mucin-like nature with increased laminin-binding activity (Fig. 7B). We propose that these events set the scene for assembly of the DGC complex, by incorporation of cis-acting, transmembrane partners of DG and subsequent lineage-specific divergence of DGs in certain phyla (Fig. 7C).Fig. 7.


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

Adams JC, Brancaccio A - Biol Open (2015)

A model for the evolution of dystroglycan and the DGC. See text for details.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

BIO012468F7: A model for the evolution of dystroglycan and the DGC. See text for details.
Mentions: We propose that the ancestral DG included a signal peptide, the IG2-MAT-NU region, transmembrane and a cytoplasmic domain with a dystrophin-binding motif. This protein might have included a serine/threonine-rich region proximal to the N-terminus; alternatively, this region may have become incorporated subsequently by domain shuffling. We speculate that this protein had weak laminin-binding activity (Fig. 7A). Rapid evolution of the N-terminal region resulting from domain duplication and shuffling of the IG domain then gave rise to the IG1 domain, in conjunction with incorporation of the S6 domain by domain shuffling from another genomic locus, and evolution of the Ser/Thr-rich region to a mucin-like nature with increased laminin-binding activity (Fig. 7B). We propose that these events set the scene for assembly of the DGC complex, by incorporation of cis-acting, transmembrane partners of DG and subsequent lineage-specific divergence of DGs in certain phyla (Fig. 7C).Fig. 7.

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