| + |
GCGR | up-regulates activity 
binding
|
GNAS |
0.49 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267715 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12626323 |
Glucagon signals through its receptor on the cell surface (Fig.1). The binding of glucagon to the extracellular loops of the glucagon receptor results in conformational changes of the latter, leading to subsequent activation of the coupled G proteins. At least two classes of G proteins are known to be associated with and involved in the signal transduction of the glucagon receptor, namely Gsα and Gq. The activation of Gsα leads to activation of adenylate cyclase, increase in intracellular cAMP levels, and subsequent activation of protein kinase A (PKA). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GCG | up-regulates
binding
|
GCGR |
0.769 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198504 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22863277 |
In contrast, stimulation of gs-coupled receptors by glucagon or epinephrine activates lats1/2 kinase activity, thereby inhibiting yap function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97338 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12529935 |
Mutation of a highly conserved d64 residue in the n-terminal portion of the rat glucagon receptor completely eliminates glucagon binding. This residue corresponds to a mutated asp residue at amino acid 60 in the growth hormone releasing hormone receptor that gives rise to the little mouse phenotype (lin et al.1993). Antisera directed against amino acid sequences 126_137 of the n-terminal region, and agai residues 206_219 of the first extracellular loop block [125i]-glucagon binding and interfere with glucagon-induced adenylyl cyclase generation in rat liver membranes. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
GCGR
- 
- 