+ |
SRC | up-regulates activity
phosphorylation
|
PANX1 |
0.386 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277803 |
Tyr199 |
KYPIVEQyLKTKKNS |
Homo sapiens |
Vascular Smooth Muscle Cell |
pmid |
sentence |
30814251 |
We recently identified amino acids 198-200 (YLK) on the PANX1 intracellular loop that are critical for α1-AR-mediated vasoconstriction and PANX1 channel function. We report herein that the YLK motif is contained within an SRC homology 2 domain and is directly phosphorylated by SRC proto-oncogene, nonreceptor tyrosine kinase (SRC) at Tyr198 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273806 |
Tyr199 |
KYPIVEQyLKTKKNS |
Homo sapiens |
Coronary Artery Smooth Muscle Cell |
pmid |
sentence |
30814251 |
We report herein that the YLK motif is contained within an SRC homology 2 domain and is directly phosphorylated by SRC proto-oncogene, nonreceptor tyrosine kinase (SRC) at Tyr198. Using a PANX1 Tyr198-specific antibody, SFK inhibitors, SRC knockdown, temperature-dependent SRC cells, and kinase assays, we found that PANX1-mediated ATP release and vasoconstriction involves constitutive phosphorylation of PANX1 Tyr198 by SRC. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277817 |
Tyr199 |
KYPIVEQyLKTKKNS |
Homo sapiens |
Vascular Smooth Muscle Cell |
pmid |
sentence |
30814251 |
We recently identified amino acids 198-200 (YLK) on the PANX1 intracellular loop that are critical for α1-AR-mediated vasoconstriction and PANX1 channel function. We report herein that the YLK motif is contained within an SRC homology 2 domain and is directly phosphorylated by SRC proto-oncogene, nonreceptor tyrosine kinase (SRC) at Tyr198 |
|
Publications: |
3 |
Organism: |
Homo Sapiens |