+ |
VRK2 | down-regulates activity
phosphorylation
|
USP25 |
0.298 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273579 |
Ser745 |
PEYLEQPsRSDFSKH |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273580 |
Thr680 |
QPLVGIEtLPPDLRD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273578 |
Thr727 |
QKLRESEtSVTTAQA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
SYK | down-regulates quantity
phosphorylation
|
USP25 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278458 |
Tyr740 |
QAAGDPEyLEQPSRS |
Homo sapiens |
|
pmid |
sentence |
19909739 |
Altogether, these data strengthen our results that SYK specifically phosphorylates USP25 and suggest that Y740 is the most probable phosphorylated tyrosine on USP25.We also assessed whether the SYK mediated phosphorylation of USP25 alters its protease activity.|Preliminary data indicate that proteasome inhibition by MG132 treatment did not modify the SYK dependent decrease of USP25 levels in contrary to accumulation of USP25 protein by MG132 treatment in the absence of SYK overexpression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
USP25 | up-regulates quantity by stabilization
deubiquitination
|
TRiC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273583 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |