| + |
PRKACA | up-regulates activity
phosphorylation
|
RYR2 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250079 |
Ser2808 |
YNRTRRIsQTSQVSV |
in vitro |
|
| pmid |
sentence |
| 14532276 |
PKA-mediated hyperphosphorylation of a conserved serine, Ser-2843 in skeletal RyR and Ser-2809 in cardiac RyR, results in an aberrant SR function during heart failure. hyperphosphorylated RyRs are leaky and therefore lead to a reduced SR Ca2+ load and impaired contractile function in heart failure |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SPEG | down-regulates activity
phosphorylation
|
RYR2 |
0.249 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279114 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32683896 |
Conclusions : Unlike other kinases (PKA, CaMKII) that increase RyR2 activity, SPEG phosphorylation reduces RyR2 mediated SR Ca 2+ -release.|Further, we show that SPEG phosphorylates RyR2 at a previously uncharacterized serine (S2367) located in the central domain of the channel. xref Importantly, in contrast to previously studied phosphorylation sites that activate RyR2 (e.g. S2808, S2814), we show that SPEG mediated RyR2-S2367 phosphorylation suppresses pathogenic diastolic SR Ca 2+ -leak. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |