+ |
MUSK | up-regulates activity
phosphorylation
|
DOK7 |
0.746 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273845 |
Tyr395 |
CLPGTVEyQVPTSLR |
Mus musculus |
|
pmid |
sentence |
20603078 |
Here, we demonstrate that Dok-7 also functions downstream from MuSK, and we identify the proteins that are recruited to the C-terminal domain of Dok-7. We show that Agrin stimulates phosphorylation of two tyrosine residues in the C-terminal domain of Dok-7, which leads to recruitment of two adapter proteins: Crk and Crk-L. Y396 and Y406 are the major tyrosine phosphorylation sites in Dok-7 expressed in C2 myotubes. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273845 |
Tyr395 |
CLPGTVEyQVPTSLR |
Mus musculus |
C2C12 Cell |
pmid |
sentence |
20603078 |
Here, we demonstrate that Dok-7 also functions downstream from MuSK, and we identify the proteins that are recruited to the C-terminal domain of Dok-7. We show that Agrin stimulates phosphorylation of two tyrosine residues in the C-terminal domain of Dok-7, which leads to recruitment of two adapter proteins: Crk and Crk-L. Y396 and Y406 are the major tyrosine phosphorylation sites in Dok-7 expressed in C2 myotubes. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273846 |
Tyr405 |
PTSLRAHyDTPRSLC |
Mus musculus |
|
pmid |
sentence |
20603078 |
Here, we demonstrate that Dok-7 also functions downstream from MuSK, and we identify the proteins that are recruited to the C-terminal domain of Dok-7. We show that Agrin stimulates phosphorylation of two tyrosine residues in the C-terminal domain of Dok-7, which leads to recruitment of two adapter proteins: Crk and Crk-L. Y396 and Y406 are the major tyrosine phosphorylation sites in Dok-7 expressed in C2 myotubes. |
|
Publications: |
3 |
Organism: |
Mus Musculus |
+ |
WNT9A | up-regulates
binding
|
MUSK |
0.409 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195975 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
22309736 |
we provide evidence that wnt9a and wnt11 bind directly to the extracellular domain of musk, to induce musk dimerization and subsequent tyrosine phosphorylation of the kinase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
DOK7 | up-regulates
binding
|
MUSK |
0.746 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-192264 |
|
|
Homo sapiens |
|
pmid |
sentence |
23467009 |
In addition, dok7, a cytoplasmic adaptor protein, is also required for musk activation in vivo. This review focuses on the physical interplay between these proteins and musk for activation and downstream signaling, which culminates in nmj formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MUSK | up-regulates activity
phosphorylation
|
MUSK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273851 |
|
|
Homo sapiens |
|
pmid |
sentence |
23458718 |
AGRN is released by the nerve and binds to LRP4, which then binds to MuSK. This interaction leads to MuSK autophosphorylation and activation of its kinase function, leading to anterograde signalling by subsequent phosphorylation of DOK7 (not shown), which binds MuSK as a dimer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
WNT11 | up-regulates
binding
|
MUSK |
0.47 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195966 |
|
|
Homo sapiens |
|
pmid |
sentence |
22309736 |
We provide evidence that wnt9a and wnt11 bind directly to the extracellular domain of musk, to induce musk dimerization and subsequent tyrosine phosphorylation of the kinase |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199641 |
|
|
Homo sapiens |
|
pmid |
sentence |
23151663 |
Musk has an extracellular region with homology to the frizzled crd,binding of which by wnt11 stimulates a pcp-like pathway during neuromuscolar development. Here, we show that in vivo, wnt11r and wnt4a initiate musk translocation from muscle membranes to recycling endosomes we provide evidence that wnt9a and wnt11 bind directly to the extracellular domain of musk, to induce musk dimerization and subsequent tyrosine phosphorylation of the kinase |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
LRP4 | up-regulates activity
binding
|
MUSK |
0.72 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273850 |
|
|
Homo sapiens |
|
pmid |
sentence |
23458718 |
AGRN is released by the nerve and binds to LRP4, which then binds to MuSK. This interaction leads to MuSK autophosphorylation and activation of its kinase function, leading to anterograde signalling by subsequent phosphorylation of DOK7 (not shown), which binds MuSK as a dimer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
MUSK | up-regulates
binding
|
WNT11 |
0.47 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199518 |
|
|
Homo sapiens |
|
pmid |
sentence |
23151663 |
Like ror, musk has an extracellular region with homolgogy to the frizzled crd, binding of which by wnt11 stimulates a pcp-like pathway during neuromuscular development |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PDZRN3 | down-regulates quantity
ubiquitination
|
MUSK |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271664 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
17576800 |
We have identified a PDZ domain containing RING finger 3 (PDZRN3) as a synapse-associated E3 ubiquitin ligase and have demonstrated that it regulates the surface expression of muscle-specific receptor tyrosine kinase (MuSK), the key organizer of postsynaptic development at the mammalian neuromuscular junction. PDZRN3 binds to MuSK and promotes its ubiquitination. Together, these data demonstrate that PDZRN3 is a catalytically active RING-type E3 ubiquitin ligase |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |