+ |
AMPK | up-regulates activity
phosphorylation
|
EPM2A |
0.357 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276338 |
Ser25 |
PELLVVGsRPELGRW |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21728993 |
In the present study, we demonstrate that laforin is a phosphoprotein, as indicated by two-dimensional electrophoresis, and we identify Ser(25) as the residue involved in this modification. We also show that Ser(25) is phosphorylated both in vitro and in vivo by AMPK. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271730 |
|
|
in vitro |
|
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: |
2 |
Organism: |
Homo Sapiens, In Vitro |
+ |
EPM2A |
dephosphorylation
|
GSK3B |
0.474 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248345 |
Ser9 |
SGRPRTTsFAESCKP |
Mus musculus |
|
pmid |
sentence |
16959610 |
Epm2a-encoded laforin is a phosphatase for GSK-3beta and an important repressor in the Wnt signaling pathway| only GSK-3β phosphorylation on Ser9 was affected by overexpression of laforin|Although GSK-3β is inactivated by phosphorylation at the Ser9 position, it is unclear if the inactivated enzyme can be reactivated by dephosphorylation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
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 |
+ |
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 |
+ |
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 |