Limits...
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

. Analysis of the multiple repetitions of the IG2_MAT_NU region in N. vectensis DG. (A) Multiple sequence alignment of the six IG2_MAT_NU modules of N. vectensis DG compared with this region of human DG. Alignments were prepared in MUSCLE 3.8 and are presented in Boxshade. Asterisks indicate the GS proteolysis site in human DG. At each position, black background includes identical residues; grey background indicates conservative substitutions, and white background indicates non-conserved residues. (B) Phylogenetic analysis of the six IG2_MAT_NU modules of N. vectensis DG (alignment of 153 positions) compared with the same region of human DG. The tree was prepared in PhyML with 200 cycles of boot-strapping. Numbers indicate bootstrap support values, with 1 as maximum. Scale=substitutions/site.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4582122&req=5

BIO012468F2: . Analysis of the multiple repetitions of the IG2_MAT_NU region in N. vectensis DG. (A) Multiple sequence alignment of the six IG2_MAT_NU modules of N. vectensis DG compared with this region of human DG. Alignments were prepared in MUSCLE 3.8 and are presented in Boxshade. Asterisks indicate the GS proteolysis site in human DG. At each position, black background includes identical residues; grey background indicates conservative substitutions, and white background indicates non-conserved residues. (B) Phylogenetic analysis of the six IG2_MAT_NU modules of N. vectensis DG (alignment of 153 positions) compared with the same region of human DG. The tree was prepared in PhyML with 200 cycles of boot-strapping. Numbers indicate bootstrap support values, with 1 as maximum. Scale=substitutions/site.

Mentions: Predicted DG proteins were identified in cnidarian species (Tables 1 and 2). The DGs of Hydra magnipapillata (Fig. 1G) and Nematostella vectensis (Fig. 1H) have unusually short mucin-like regions and the α/β maturation site is not conserved in the latter. N. vectensis DG is characterized by extensive duplication of the IG2_MAT_NU region, leading to an unusual domain architecture in which six such modules are present in tandem (Fig. 1H). Each of these modules has a distinct sequence (Fig. 2A, supplementary material Fig. S2). Phylogenetic analysis revealed that the sixth, most C-terminal module is distinct in being the most closely related to human IG2_MAT_NU, whereas each of the other modules are more closely related to each other than to the sixth repeated region (Fig. 2B). N. vectensis DG is also characterized by an inserted sequence in the cytoplasmic domain (Fig. 1H).Fig. 2


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

Adams JC, Brancaccio A - Biol Open (2015)

. Analysis of the multiple repetitions of the IG2_MAT_NU region in N. vectensis DG. (A) Multiple sequence alignment of the six IG2_MAT_NU modules of N. vectensis DG compared with this region of human DG. Alignments were prepared in MUSCLE 3.8 and are presented in Boxshade. Asterisks indicate the GS proteolysis site in human DG. At each position, black background includes identical residues; grey background indicates conservative substitutions, and white background indicates non-conserved residues. (B) Phylogenetic analysis of the six IG2_MAT_NU modules of N. vectensis DG (alignment of 153 positions) compared with the same region of human DG. The tree was prepared in PhyML with 200 cycles of boot-strapping. Numbers indicate bootstrap support values, with 1 as maximum. Scale=substitutions/site.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

BIO012468F2: . Analysis of the multiple repetitions of the IG2_MAT_NU region in N. vectensis DG. (A) Multiple sequence alignment of the six IG2_MAT_NU modules of N. vectensis DG compared with this region of human DG. Alignments were prepared in MUSCLE 3.8 and are presented in Boxshade. Asterisks indicate the GS proteolysis site in human DG. At each position, black background includes identical residues; grey background indicates conservative substitutions, and white background indicates non-conserved residues. (B) Phylogenetic analysis of the six IG2_MAT_NU modules of N. vectensis DG (alignment of 153 positions) compared with the same region of human DG. The tree was prepared in PhyML with 200 cycles of boot-strapping. Numbers indicate bootstrap support values, with 1 as maximum. Scale=substitutions/site.
Mentions: Predicted DG proteins were identified in cnidarian species (Tables 1 and 2). The DGs of Hydra magnipapillata (Fig. 1G) and Nematostella vectensis (Fig. 1H) have unusually short mucin-like regions and the α/β maturation site is not conserved in the latter. N. vectensis DG is characterized by extensive duplication of the IG2_MAT_NU region, leading to an unusual domain architecture in which six such modules are present in tandem (Fig. 1H). Each of these modules has a distinct sequence (Fig. 2A, supplementary material Fig. S2). Phylogenetic analysis revealed that the sixth, most C-terminal module is distinct in being the most closely related to human IG2_MAT_NU, whereas each of the other modules are more closely related to each other than to the sixth repeated region (Fig. 2B). N. vectensis DG is also characterized by an inserted sequence in the cytoplasmic domain (Fig. 1H).Fig. 2

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