IndraLab

"To further clarify that anti-μ antibody and Pam 3 Csk 4 co-treatment promoted T674 phosphorylation of USP10, we first generated an antibody that specifically recognizes the phosphorylation site of USP10 by ."

"In addition, Luo et al. reported that co-stimulation by BCR and TLR1/2 initiated the AKT-dependent phosphorylation of T674 of USP10; subsequently, USP10 entered the nucleus and stabilized the AID protein (also see Figure 4 and Table 2 ) [72] ."

"BCR and TLR1/2 activation synergistically inhibited AID degradation in the nucleus through Akt-mediated USP10 T674 phosphorylation and the nuclear translocation USP10 is a cytoplasmic protein characterized by a nucleus-cytoplasm shuttle."

"To further clarify that anti-μ antibody and Pam 3 Csk 4 co-treatment promoted T674 phosphorylation of USP10, we first generated an antibody that specifically recognizes the phosphorylation site of USP10 by immunizing rabbits with the phosphorylated and sequence-homologous polypeptides (Supplementary Fig. xref )."

"Interestingly, the BCR-PI3K-Akt signaling pathway activates AKT and phosphorylates the T674 site of USP10 and the TLR1/2 signal, which significantly enhances signal transduction."

"Luo et al. Fig. 6 BCR and TLR2 activation synergistically inhibited AID degradation in the nucleus through Akt-mediated USP10 T674 phosphorylation and nuclear translocation."

"Collectively, these results indicated that BCR and TLR2 synergistically enhance Akt activity and promote USP10 T674 phosphorylation located within the NLS domain and, therefore, the nuclear import of USP10, consequently inhibiting the AID degradation in the nucleus."

"BCR and TLR1/2 activation synergistically inhibited AID degradation in the nucleus through Akt-mediated USP10 T674 phosphorylation and the nuclear translocation."

"I, j Western blot indicated TLR1/2 and BCR co-stimulation promoted USP10 T674 phosphorylation, but not when AKT inhibitor treatment."

"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] ."