Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor

@article{Gee1994DystroglycanAD,
  title={Dystroglycan-$\alpha$, a dystrophin-associated glycoprotein, is a functional agrin receptor},
  author={Stephen H. Gee and Federica Alice Maria Montanaro and Michael H. Lindenbaum and Salvatore Carbonetto},
  journal={Cell},
  year={1994},
  volume={77},
  pages={675-686}
}

Dystroglycan Is a Dual Receptor for Agrin and Laminin-2 in Schwann Cell Membrane*

TLDR
Results indicate that α-dystroglycan is a dual receptor for agrin and laminin-2 in the Schwann cell membrane.

AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha‐dystroglycan.

TLDR
It is concluded that agrin‐induced AChR phosphorylation and aggregation are triggered by an agrin receptor that is distinct from alpha‐dystroglycan.

α-Dystroglycan Is a Laminin Receptor Involved in Extracellular Matrix Assembly on Myotubes and Muscle Cell Viability

TLDR
It is suggested that α-DG is a functional LN receptor in situ which is required for deposition of LN on the cell and, further, implicate α- DG in the maintenance of myotube viability.

Dystroglycan overexpression in vivo alters acetylcholine receptor aggregation at the neuromuscular junction.

TLDR
Overexpressed dystroglycan altered AChR aggregation in a rostral-caudal gradient, consistent with the sequential development of neuromuscular synapses along the embryo, and supports the hypothesis that dystoglycan is not the myotube-associated specificity component, (MASC) a putative coreceptor needed for agrin to activate muscle-specific kinase (MuSK) and signal ACh R aggregation.

Alternative RNA splicing that determines agrin activity regulates binding to heparin and alpha-dystroglycan.

TLDR
A model in which multiple distinct domains of agrin interact with both protein and sugar moieties of alpha-dystroglycan is proposed, which is consistent with a functional role for this interaction during synaptogenesis.

Agrin Is a High-affinity Binding Protein of Dystroglycan in Non-muscle Tissue*

TLDR
Tissue distribution and binding affinities show that the agrin isoform expressed in non-muscle tissue is a high-affinity binding partner of dystroglycan and suggest that this interaction, like that between laminin and dystoglycan, may be important for the mechanical integrity of the tissue.

A Role of Dystroglycan in Schwannoma Cell Adhesion to Laminin*

TLDR
A role for dystroglycan as a major cell adhesion molecule in the surface membrane of RT4 cells is characterized and shown to be a major laminin-binding protein complex.

The Dystroglycan Complex Is Necessary for Stabilization of Acetylcholine Receptor Clusters at Neuromuscular Junctions and Formation of the Synaptic Basement Membrane

TLDR
It is shown that myotubes differentiated from dystroglycan−/− embryonic stem cells are responsive to agrin, but produce acetylcholine receptor (AChR) clusters which are two to three times larger in area, about half as dense, and significantly less stable than those on dystoglycan+/+ myot tubes.

An Extracellular Pathway for Dystroglycan Function in Acetylcholine Receptor Aggregation and Laminin Deposition in Skeletal Myotubes*

TLDR
It is discussed how DG may regulate synapses through extracellular signaling functions of its α subunit, which modulate the size and the microcluster density of agrin-induced acetylcholine receptor aggregates and are responsible for targeting laminin to these clusters.
...

References

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TLDR
The results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin- based cytoskeleton with the extracellular matrix and suggest that dystophin and dystroglycan may play substantially different functional roles in nonmuscle tissues.

Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle

TLDR
The results could provide a basis for the upregulation of DRP as a potential therapeutic approach in Duchenne muscular dystrophy and mdx muscle.

Localization of dystrophin relative to acetylcholine receptor domains in electric tissue and adult and cultured skeletal muscle

TLDR
Results suggest that dystrophin may have a role in organization of AChR in electric tissue and, at the neuromuscular junction, its roles may be more related to organization of the junctional folds.

Different distributions of dystrophin and related proteins at nerve-muscle junctions.

TLDR
DRP is more closely associated with AChRs than are dystrophin or beta-spectrin, according to immunofluorescence techniques used at rat nerve-muscle junctions.

Agrin induces phosphorylation of the nicotinic acetylcholine receptor

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TLDR
It is shown that AChRs present on the fibroblast cell surface prior to transfection of 43k are recruited into 43k-rich membrane domains, and cytoskeletal component, dystrophin related protein (DRP) contributed to the development of AChR clusters.

Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle.

TLDR
It is demonstrated that DAPs, dystrophin, and laminin colocalize to the sarcolemma in rabbit and sheep papillary myofibers as they do in skeletal my ofibers, implying that the protein composition and thus possibly some functions of T tubules in cardiac muscle are distinct from those of skeletal muscle.
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