+ |
SRC | down-regulates
phosphorylation
|
SH3GL1 |
0.625 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139150 |
Tyr315 |
QPSCKALyDFEPEND |
Homo sapiens |
|
pmid |
sentence |
16054026 |
Further, we identified an interaction between fak's second pro-rich motif and endophilin a2's sh3 domain. This interaction served as an autophosphorylation-dependent scaffold to allow src phosphorylation of endophilin a2 at tyr315. Tyr315 phosphorylation inhibited endophilin/dynamin interactions, and blockade of tyr315 phosphorylation promoted endocytosis of mt1-mmp. Together, these results suggest a regulatory mechanism of cell invasion whereby fak promotes cell-surface presentation of mt1-mmp by inhibiting endophilin a2-dependent endocytosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTK2 |
phosphorylation
|
SH3GL1 |
0.41 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139146 |
Tyr315 |
QPSCKALyDFEPEND |
Homo sapiens |
|
pmid |
sentence |
16054026 |
These results identified y315 of endophilin a2 as a major phosphorylation site by fak/src complex. tyr315 phosphorylation inhibited endophilin/dynamin interactions, and blockade of tyr315 phosphorylation promoted endocytosis of mt1-mmp. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC |
phosphorylation
|
SH3GL1 |
0.625 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139154 |
Tyr315 |
QPSCKALyDFEPEND |
Homo sapiens |
|
pmid |
sentence |
16054026 |
These results identified y315 of endophilin a2 as a major phosphorylation site by fak/src complex. tyr315 phosphorylation inhibited endophilin/dynamin interactions, and blockade of tyr315 phosphorylation promoted endocytosis of mt1-mmp. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SH3GL1 | up-regulates
|
Endocytosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263885 |
|
|
Homo sapiens |
|
pmid |
sentence |
25517094 |
Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRRK2 | down-regulates
phosphorylation
|
SH3GL1 |
0.479 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-192068 |
|
|
Homo sapiens |
|
pmid |
sentence |
22998870 |
We show that lrrk2 affects synaptic endocytosis by phosphorylating endoa at s75, a residue in the bar domain / our work uncovers a regulatory mechanism that indicates that reduced lrrk2 kinase activity facilitates endoa membrane association, while increased kinase activity inhibits membrane association. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |