Recombinant Rabbit Dystroglycan (DAG1), partial

Function

Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity (By similarity)

Subcellular Location

Cell membrane (Single-pass type I membrane protein); Cytoplasm, cytoskeleton; Nucleus, nucleoplasm; Cell membrane, sarcolemma; Synapse; Postsynaptic cell membrane

Tissue Specificity

Detected in brain, cardiac muscle and skeletal muscle (at protein level) (PubMed:16709410). Expressed in lung, brain, liver, kidney, diaphragm and stomach (PubMed:1741056)

Subunit

Monomer. Heterodimer of alpha- and beta-dystroglycan subunits which are the central components of the dystrophin-glycoprotein complex. This complex then can form a dystrophin-associated glycoprotein complex (DGC) which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex. Interacts (via the N-terminal of alpha-dystroglycan) with LARGE1; the interaction enhances laminin binding (PubMed:15210115). Interacts with SGCD. Interacts with AGR2 and AGR3. Interacts (beta-dystroglycan) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (beta-dystroglycan, via its PPXY motif) with UTRN (via its WWW and ZZ domains); the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (beta-dystroglycan, via its phosphorylated PPXY motif) with the SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts (beta-dystroglycan) with CAV3 (via a central WW-like domain); the interaction disrupts the binding of DMD. beta-dystroglycan directly interacts with ANK3, but not with ANK2; this interaction does not interfere with DMD-binding and is required for retention at costameres (By similarity). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity). Interacts with POMGNT1 (By similarity). beta-dystroglycan interacts with CD93 (By similarity). Alpha-dystroglycan interacts with HSPG2; the interaction is required for acetylcholinesterase (AChE) localization at the neuromuscular junctions (NMJ) (By similarity). Alpha-dystroglycan interacts with AGRN; the interaction is required for up-regulation of SOX9 and cartilage formation (By similarity). Alpha-dystroglycan interacts with pikachurin (EGFLAM); the interaction is required for photoreceptor ribbon synapse formation (By similarity)

• Ibraghimov-Beskrovnaya O. et al. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. — Nature (1992)
• Sasaki T. et al. Detection of O-mannosyl glycans in rabbit skeletal muscle alpha-dystroglycan. — Biochim. Biophys. Acta (1998)
• Oak S.A. et al. Skeletal muscle signaling pathway through the dystrophin glycoprotein complex and Rac1. — J. Biol. Chem. (2003)
• Kanagawa M. et al. Molecular recognition by LARGE is essential for expression of functional dystroglycan. — Cell (2004)
• Zhou Y.W. et al. Binding of laminin alpha1-chain LG4-5 domain to alpha-dystroglycan causes tyrosine phosphorylation of syntrophin to initiate Rac1 signaling. — Biochemistry (2006)
• McDearmon E.L. et al. Brain alpha-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11. — FEBS Lett. (2006)
• Zhou Y. et al. Laminin-induced activation of Rac1 and JNKp46 is initiated by Src family kinases and mimics the effects of skeletal muscle contraction. — Biochemistry (2007)