| + |
AMPK | down-regulates quantity by destabilization 
phosphorylation
|
PPP1R3C |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273739 |
Ser33 |
MRLCLAHsPPVKSFL |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 19171932 |
AMPK induces the phosphorylation of residues Ser-8 and Ser-268 in R5/PTG. We now demonstrate that phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. Thus, our results define a novel role of AMPK in glycogen homeostasis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276237 |
Ser33 |
MRLCLAHsPPVKSFL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19171932 |
We have recently described that the activity of R5/PTG is down-regulated by the laforin-malin complex, composed of a dual specificity phosphatase (laforin) and an E3-ubiquitin ligase (malin). We now demonstrate that phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. |
|
| Publications: |
2 |
Organism: |
Cricetulus Griseus, Homo Sapiens |
| + |
NHLRC1 | down-regulates quantity by destabilization
ubiquitination
|
PPP1R3C |
0.731 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276238 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19171932 |
We have recently described that the activity of R5/PTG is down-regulated by the laforin-malin complex, composed of a dual specificity phosphatase (laforin) and an E3-ubiquitin ligase (malin). We now demonstrate that phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271727 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18029386 |
Here, we show that the laforin-malin complex downregulates PTG-induced glycogen synthesis in FTO2B hepatoma cells through a mechanism involving ubiquitination and degradation of PTG. We show here that laforin and malin play a crucial role in the regulation of glycogen biosynthesis in FTO2B hepatoma cells. In these cells, the laforin–malin complex counteracts the glycogenic effect of PTG because it promotes its ubiquitination and degradation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP1R3C | up-regulates 
binding
|
GYS1 |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271733 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
| + |
EPM2A | up-regulates quantity by stabilization
dephosphorylation
|
PPP1R3C |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276239 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19171932 |
We have recently described that the activity of R5/PTG is down-regulated by the laforin-malin complex, composed of a dual specificity phosphatase (laforin) and an E3-ubiquitin ligase (malin). We now demonstrate that phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1R3C | up-regulates
binding
|
GYS2 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271731 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
| + |
PPP1R3C | up-regulates
binding
|
PP1 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271735 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
3.0
PPP1R3C
- 
- 