+ |
AKT2 | down-regulates activity
phosphorylation
|
STXBP4 |
0.433 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262635 |
Ser99 |
GAKLRLEsAWEIAFI |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15753124 |
Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles. These data demonstrate that insulin activation of Akt2 specifically regulates the docking/fusion step of GLUT4-containing vesicles at the plasma membrane through the regulation of Synip phosphorylation and Synip-Syntaxin4 interaction.Thus, our data demonstrate that insulin-stimulated Akt2-dependent phosphorylation of Synip on serine residue 99 results in reduced binding interactions between Synip and Syntaxin4. |
|
Publications: |
1 |
Organism: |
Cricetulus Griseus |
+ |
STXBP4 | down-regulates activity
binding
|
YAP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260013 |
|
|
in vitro |
|
pmid |
sentence |
31782549 |
WW domain‐containing protein STXBP4 inhibits YAP activity via LATS1‐mediated phosphorylation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
STXBP4 | up-regulates activity
binding
|
STX4 |
0.793 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262634 |
|
|
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15753124 |
Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles. These data demonstrate that insulin activation of Akt2 specifically regulates the docking/fusion step of GLUT4-containing vesicles at the plasma membrane through the regulation of Synip phosphorylation and Synip-Syntaxin4 interaction.Thus, our data demonstrate that insulin-stimulated Akt2-dependent phosphorylation of Synip on serine residue 99 results in reduced binding interactions between Synip and Syntaxin4. |
|
Publications: |
1 |
Organism: |
Cricetulus Griseus |