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

Biology Open
Josephine C Adams, Andrea Brancaccio

Abstract

Basement membrane (BM) extracellular matrices are crucial for the coordination of different tissue layers. A matrix adhesion receptor that is important for BM function and stability in many mammalian tissues is the dystroglycan (DG) complex. 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. Mutations in dystrophin, DG, or several enzymes that glycosylate α-DG underlie severe forms of human muscular dystrophy. Nonwithstanding the pathophysiological importance of the DG complex and its fundamental interest as a non-integrin system of cell-ECM adhesion, the evolution of DG and its interacting proteins is not understood. We analysed the phylogenetic distribution of DG, its proximal binding partners and key processing enzymes in extant metazoan and relevant outgroups. We identify that DG originated after the divergence of ctenophores from porifera and eumetazoa. The C-terminal half of the DG core protein is highly-conserved, yet the N-terminal region, that includes the laminin-binding region, has undergone major lineage-specific divergences. Phylogenetic analysis based on ...Continue Reading

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Citations

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Methods Mentioned

BETA
glycosylation
gene knockout

Software Mentioned

Phylemon
MUSCLE
PhyML
COMPAGEN
TBLASTX
BLASTP
PROTPARS PHYLIP ( Phylogeny Inference Package )
PROTPARS
PRANK
LARGE

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