| + |
FAM20C | up-regulates activity 
phosphorylation
|
HRC |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273639 |
Ser96 |
EKEDEDVsKEYGHLL |
Rattus norvegicus |
H9c2 Cell |
| pmid |
sentence |
| 28784772 |
Here, we demonstrate that family with sequence similarity 20C (Fam20C), a recently characterized protein kinase in the secretory pathway, phosphorylates HRC on Ser96. HRC Ser96 phosphorylation was confirmed in cells and human hearts.The pSer96-HRC binds tighter to triadin than S96A-HRC, which cannot be phosphorylated. Conversely, S96A-HRC or unphosphorylated Ser96-HRC binds tighter to SERCA2a. This suggests that Ser96-HRC phosphorylation (P) regulates HRC’s interactions with the major SR Ca-cycling proteins. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
HRC | down-regulates activity 
binding
|
ATP2A2 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273662 |
|
|
Rattus norvegicus |
H9c2 Cell |
| pmid |
sentence |
| 28784772 |
Furthermore, a Ser96Asp HRC variant, which mimics constitutive phosphorylation of Ser96, diminished delayed aftercontractions in HRC null cardiac myocytes. This HRC phosphomimetic variant was also able to rescue the aftercontractions elicited by the Ser96Ala variant, demonstrating that phosphorylation of Ser96 is critical for the cardioprotective function of HRC. Phosphorylation of HRC on Ser96 regulated the interactions of HRC with both triadin and SERCA2a, suggesting a unique mechanism for regulation of SR Ca homeostasis. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
HRC
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