+ |
NHLRC1 | down-regulates quantity by destabilization
ubiquitination
|
PPP1R3B |
0.409 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271728 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |
+ |
NHLRC1 | down-regulates quantity by destabilization
polyubiquitination
|
EPM2A |
0.78 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271547 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15930137 |
Here, we demonstrate that malin is a single subunit E3 ubiquitin (Ub) ligase and that its RING domain is necessary and sufficient to mediate ubiquitination. Additionally, malin interacts with and polyubiquitinates laforin, leading to its degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
NHLRC1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271135 |
|
|
Homo sapiens |
|
pmid |
sentence |
34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NHLRC1 | down-regulates quantity by destabilization
ubiquitination
|
PPP1R3C |
0.731 |
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. |
|
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. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NHLRC1 | down-regulates quantity by destabilization
polyubiquitination
|
DVL2 |
0.474 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272005 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22223637 |
We have also found that malin enhances K48- and K63-linked ubiquitination of dishevelled2 that could lead to its degradation through both proteasome and autophagy. Altogether, our results indicate that malin regulates Wnt signaling pathway through the degradation of dishevelled2 and suggest possible deregulation of Wnt signaling in Lafora disease. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NHLRC1 | down-regulates quantity by destabilization
ubiquitination
|
AGL |
0.578 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271669 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
17908927 |
The E3 ubiquitin ligase Malin interacts with and promotes the ubiquitination of AGL. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
EPM2A | up-regulates activity
binding
|
NHLRC1 |
0.78 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271729 |
|
|
Rattus norvegicus |
FTO-2B Cell |
pmid |
sentence |
18029386 |
Here, we provide evidence indicating that the formation of the laforin–malin complex is positively regulated by AMPK. We show that laforin, but not malin, can interact physically with the catalytic subunit of AMPK and that purified AMPK phosphorylates GST::laforin in vitro. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |