Relation Results

Summary

Name DGC
Primary ID SIGNOR-C217
Type complex
Formed by DAG1, SGCG, LAMA2, SNTB2, SNTG2, DTNB, DMD, SNTG1, DTNA, CAV3, SGCB, SNTB1, SGCA, SGCD, SNTA1, NOS1
Relations 37

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Type: Score: Layout: SPV 
0.3110.20.3510.5220.4540.4520.4620.5040.6820.3680.4970.2580.4930.3050.20.2840.4110.20.3050.4960.4740.5730.20.20.20.5210.2840.4420.20.20.20.4230.20.3510.20.539DGCAQP4GABA-A (a2-b1-g2) receptorNRXN1SNTG2DTNASGCGSNTG1SGCDDMDNOS1SNTB1MAGI2SGCBNRXN3GABA-A (a1-b1-g2) receptorNRXN2POMT GABA-A (a6-b3-d) receptorNRXN3CAV3SNTB2DAG1GABA-AGABA-A (a3-b1-g2) receptorGABA-A (a4-b3-d) receptorSNTA1NRXN2DTNBGABA-A (a4-b2-d) receptorGABA-A (a6-b1-g2) receptorGABA-A (a4-b1-g2) receptorLAMA2GABA-A (a6-b2-d) receptorNRXN1GABA-A (a5-b1-g2) receptorSGCA

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Relations
Regulator
Mechanism
target
score ℹ
+ DGCup-regulates quantity img/direct-activation.png binding AQP4 0.311
Identifier Residue Sequence Organism Cell Line
SIGNOR-265443 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a2-b1-g2) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265433 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates activity img/direct-activation.png binding NRXN1 0.351
Identifier Residue Sequence Organism Cell Line
SIGNOR-265447 Homo sapiens
pmid sentence
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ SNTG2form complex img/form-complex.png binding DGC 0.522
Identifier Residue Sequence Organism Cell Line
SIGNOR-255995 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DTNAform complex img/form-complex.png binding DGC 0.454
Identifier Residue Sequence Organism Cell Line
SIGNOR-255989 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ SGCGform complex img/form-complex.png binding DGC 0.452
Identifier Residue Sequence Organism Cell Line
SIGNOR-255987 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ SNTG1form complex img/form-complex.png binding DGC 0.462
Identifier Residue Sequence Organism Cell Line
SIGNOR-255994 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ SGCDform complex img/form-complex.png binding DGC 0.504
Identifier Residue Sequence Organism Cell Line
SIGNOR-255988 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DMDform complex img/form-complex.png binding DGC 0.682
Identifier Residue Sequence Organism Cell Line
SIGNOR-255998 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ NOS1form complex img/form-complex.png binding DGC 0.368
Identifier Residue Sequence Organism Cell Line
SIGNOR-255996 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ SNTB1form complex img/form-complex.png binding DGC 0.497
Identifier Residue Sequence Organism Cell Line
SIGNOR-255979
pmid sentence
Basal localization of the p38γ/p-Carm1 complex in muscle stem cells occurs via binding to the dystrophin-glycoprotein complex (DGC) through β1-syntrophin. In dystrophin-deficient muscle stem cells undergoing asymmetric division, p38γ/β1-syntrophin interactions are abrogated
Identifier Residue Sequence Organism Cell Line
SIGNOR-255992 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 2 Organism: , Homo Sapiens
Tissue: Skeletal Muscle
+ MAGI2up-regulates activity img/direct-activation.png binding DGC 0.258
Identifier Residue Sequence Organism Cell Line
SIGNOR-265445 Homo sapiens
pmid sentence
S-SCAM is a member of the membrane-associated guanylate kinase (MAGUK) family of PDZ-domain-containing proteins that include the synaptic organising molecule PSD-95. The PDZ domain of S-SCAM binds to the C-terminal tail of NL2, forming a ternary complex at the cell membrane (Figure 2b). The DGC is potentially recruited to the postsynaptic membrane though a direct neurexin–dystroglycan interaction and an indirect interaction with NL2 via the synaptic scaffolding protein S-SCAM.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ SGCBform complex img/form-complex.png binding DGC 0.493
Identifier Residue Sequence Organism Cell Line
SIGNOR-255986 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates activity img/direct-activation.png binding NRXN3 0.305
Identifier Residue Sequence Organism Cell Line
SIGNOR-265450 Homo sapiens
pmid sentence
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a1-b1-g2) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265432 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates activity img/direct-activation.png binding NRXN2 0.284
Identifier Residue Sequence Organism Cell Line
SIGNOR-265448 Homo sapiens
pmid sentence
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ POMT up-regulates activity img/direct-activation.png glycosylation DGC 0.411
Identifier Residue Sequence Organism Cell Line
SIGNOR-265431 Homo sapiens HEK-293 Cell
pmid sentence
we showed that coexpression of both POMT1 and POMT2 (another gene homologous to yeast protein O-mannosyltransferases) was necessary for the enzyme activity, but expression of either POMT1 or POMT2 alone was insufficient. The requirement of an active enzyme complex of POMT1 and POMT2 suggests that the regulation of protein O-mannosylation is complex. Further, protein O-mannosylation appears to be required for normal structure and function of α-dystroglycan in muscle and brain.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a6-b3-d) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265441 Homo sapiens
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates activity img/direct-activation.png binding NRXN3 0.305
Identifier Residue Sequence Organism Cell Line
SIGNOR-265451 Homo sapiens
pmid sentence
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ CAV3form complex img/form-complex.png binding DGC 0.496
Identifier Residue Sequence Organism Cell Line
SIGNOR-255997 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ SNTB2form complex img/form-complex.png binding DGC 0.474
Identifier Residue Sequence Organism Cell Line
SIGNOR-255993 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DAG1form complex img/form-complex.png binding DGC 0.573
Identifier Residue Sequence Organism Cell Line
SIGNOR-255983 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265442 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a3-b1-g2) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265434 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a4-b3-d) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265437 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ SNTA1form complex img/form-complex.png binding DGC 0.521
Identifier Residue Sequence Organism Cell Line
SIGNOR-255991 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates activity img/direct-activation.png binding NRXN2 0.284
Identifier Residue Sequence Organism Cell Line
SIGNOR-265449 Homo sapiens
pmid sentence
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ DTNBform complex img/form-complex.png binding DGC 0.442
Identifier Residue Sequence Organism Cell Line
SIGNOR-255990 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a4-b2-d) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265436 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a6-b1-g2) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265439 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a4-b1-g2) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265435 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ LAMA2form complex img/form-complex.png binding DGC 0.423
Identifier Residue Sequence Organism Cell Line
SIGNOR-255984 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a6-b2-d) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265440 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ DGCup-regulates activity img/direct-activation.png binding NRXN1 0.351
Identifier Residue Sequence Organism Cell Line
SIGNOR-265446 Homo sapiens
pmid sentence
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ DGCup-regulates quantity img/direct-activation.png binding GABA-A (a5-b1-g2) receptor 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265438 Homo sapiens Neuron, Glial Cell
pmid sentence
 In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses.
Publications: 1 Organism: Homo Sapiens
+ SGCAform complex img/form-complex.png binding DGC 0.539
Identifier Residue Sequence Organism Cell Line
SIGNOR-255985 Homo sapiens
pmid sentence
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink).
Publications: 1 Organism: Homo Sapiens
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