
IndraLab
Statements
sparser
"AMPKα AMPKα increases its activity by mediating phosphorylation of Ser76 at the USP10 N-terminus.
[15]
ATM ATM mediates phosphorylation of USP10 at Thr42 and Ser337 and causes USP10's migration into the nucleus.
[27]
TRAF4 TRAF4 and p53 competitively bind to USP10 and inhibit usP10-mediated p53 deubiquitination. [73] AKT Co-stimulation by BCR and TLR1/2 initiates Akt-dependent phosphorylation of T674 in the USP10 NLS domain.
[72]
USP13/beclin-1
When USP10 and USP13 interact with beclin-1, the deubiquitination activity of USP10 can be increased.
[53]
MiR-138
MiR-138 binds to a conserved region of USP10's 3 -UTR and inhibits the accumulation of USP10 mRNA and protein expression level.
[31]
MicroRNA-191
MicroRNA-191 binds to the 3 -untranslated region of USP10 mRNA, reducing USP10 protein levels.
[28]
MiR-34a-5p MiR-34a-5p binds to the 3 -untranslated region of USP10 and reduces the expression of USP10. [79] G3BP Direct binding of G3BP to USP10 inhibits its ability to decompose ubiquitin chains. [56] HTLV-1 Tax
The central region of Tax interacts with amino acids 727-798 in USP10, inhibiting the activity of USP10.
[78]
Daam1 negatively regulates USP10's DUB activity. [80] Estrogen Estrogen induces p53 degradation by regulating USP10 activity.
[81]
Overexpressed FOXO4 inhibits USP10 transcription and protein expression by binding to the bases 1771-1776 in the promoter region TSS of USP10. [82] Zhang et al. indicated that miR-34a-5p acted as a negative regulator of USP10, but the underlying mechanism of the microRNA's action remains largely unclear [79] ."
sparser
"Indeed, following various genotoxic stresses (IR, UV or etoposide treatment), USP10 became phosphorylated at SQ/TQ motifs ( xref and xref , USP10 protein levels were equalized to specifically examine USP10 phosphorylation in experiments of xref , xref ), which are consensus phosphorylation sites for PI3-kinase like kinases (PIKKs), such as ATM, ATR, and DNA-PK ( xref )."
sparser
"In particular, the phosphorylation of USP10 in its NLS domain by BCR-TLR1/2-PI3K-Akt integrates the dual signals from the interaction between TLR and its ligand, or BCR and antigen on the cell surface, facilitating its translocation into the nucleus and transmitting signals into the nucleus to regulate the abundance of AID."
sparser
"Both USP7 and USP10 are subjected to phosphorylation-dependent regulation. xref , xref Particularly, phosphorylation of USP7 by the protein kinase CK2 is shown to stabilize USP7. xref Although USP7 or USP10 expression was not altered by acute FSK treatment, any effect on USP7 and USP10 phosphorylation remains to be determined."