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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

Evolution of dystroglycan-binding proteins. (A) Schematic of the interactions of dystroglycan with other members of the DGC and the modifying enzymes that act on DG. In the Golgi complex, α-dystroglycan is post-translationally modified at multiple Thr/Ser residues in its mucin-like region during its trafficking to the cell surface. CR, cysteine-rich domain; SG: sarcoglycan; SS: sarcospan. (B) The phylogenetic distributions of DG, dystroglycan-binding proteins of the DGC and DG-modifying enzymes in early-diverging metazoans and their closest unicellular relatives. Species are representative of the indicated phyla. Key: Grey squares, predicted protein identified, BLASTP e-value<1e−10; black circles, BLASTP e-value>1e−10 and <0.05; white squares, no homologue identified. See supplementary material Table S1 for accession numbers.
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BIO012468F6: Evolution of dystroglycan-binding proteins. (A) Schematic of the interactions of dystroglycan with other members of the DGC and the modifying enzymes that act on DG. In the Golgi complex, α-dystroglycan is post-translationally modified at multiple Thr/Ser residues in its mucin-like region during its trafficking to the cell surface. CR, cysteine-rich domain; SG: sarcoglycan; SS: sarcospan. (B) The phylogenetic distributions of DG, dystroglycan-binding proteins of the DGC and DG-modifying enzymes in early-diverging metazoans and their closest unicellular relatives. Species are representative of the indicated phyla. Key: Grey squares, predicted protein identified, BLASTP e-value<1e−10; black circles, BLASTP e-value>1e−10 and <0.05; white squares, no homologue identified. See supplementary material Table S1 for accession numbers.

Mentions: As described in the Introduction, DG is the central member of the major non-integrin, laminin-binding, cell-ECM adhesion complex of mammals, the dystrophin-glycoprotein complex. Given the importance of extracellular, membrane-associated and intracellular binding partners of DG for the functionality of the DGC and post-translational processing of DG for its function and binding activities at the plasma membrane (Fig. 6A), we next investigated the phylogenetic distribution of these proteins in comparison to DG itself. Initial studies showed that all these proteins are present in bilaterians, therefore we focused our study on the early-diverging metazoa and certain unicellular eukaryotes, choanoflagellates and the filasterian C. owczarzaki, that are the closest outgroups to the metazoa. It was important to consider these outgroups because other cell adhesion receptors, integrins and cadherins, evolved before the emergence of metazoans (Abedin and King, 2008; Sebé-Pedrós et al., 2010).Fig. 6.


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

Adams JC, Brancaccio A - Biol Open (2015)

Evolution of dystroglycan-binding proteins. (A) Schematic of the interactions of dystroglycan with other members of the DGC and the modifying enzymes that act on DG. In the Golgi complex, α-dystroglycan is post-translationally modified at multiple Thr/Ser residues in its mucin-like region during its trafficking to the cell surface. CR, cysteine-rich domain; SG: sarcoglycan; SS: sarcospan. (B) The phylogenetic distributions of DG, dystroglycan-binding proteins of the DGC and DG-modifying enzymes in early-diverging metazoans and their closest unicellular relatives. Species are representative of the indicated phyla. Key: Grey squares, predicted protein identified, BLASTP e-value<1e−10; black circles, BLASTP e-value>1e−10 and <0.05; white squares, no homologue identified. See supplementary material Table S1 for accession numbers.
© Copyright Policy - open-access
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4582122&req=5

BIO012468F6: Evolution of dystroglycan-binding proteins. (A) Schematic of the interactions of dystroglycan with other members of the DGC and the modifying enzymes that act on DG. In the Golgi complex, α-dystroglycan is post-translationally modified at multiple Thr/Ser residues in its mucin-like region during its trafficking to the cell surface. CR, cysteine-rich domain; SG: sarcoglycan; SS: sarcospan. (B) The phylogenetic distributions of DG, dystroglycan-binding proteins of the DGC and DG-modifying enzymes in early-diverging metazoans and their closest unicellular relatives. Species are representative of the indicated phyla. Key: Grey squares, predicted protein identified, BLASTP e-value<1e−10; black circles, BLASTP e-value>1e−10 and <0.05; white squares, no homologue identified. See supplementary material Table S1 for accession numbers.
Mentions: As described in the Introduction, DG is the central member of the major non-integrin, laminin-binding, cell-ECM adhesion complex of mammals, the dystrophin-glycoprotein complex. Given the importance of extracellular, membrane-associated and intracellular binding partners of DG for the functionality of the DGC and post-translational processing of DG for its function and binding activities at the plasma membrane (Fig. 6A), we next investigated the phylogenetic distribution of these proteins in comparison to DG itself. Initial studies showed that all these proteins are present in bilaterians, therefore we focused our study on the early-diverging metazoa and certain unicellular eukaryotes, choanoflagellates and the filasterian C. owczarzaki, that are the closest outgroups to the metazoa. It was important to consider these outgroups because other cell adhesion receptors, integrins and cadherins, evolved before the emergence of metazoans (Abedin and King, 2008; Sebé-Pedrós et al., 2010).Fig. 6.

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