IndraLab

Statements


5 | 11

sparser
"These findings suggest that CAPZA1 acts as a scaffold to mediate the interaction between USP48 and SIRT6, thus decreasing the ubiquitination-mediated degradation of SIRT6."

sparser
"Conversely, overexpression of CAPZA1 promoted the interaction of SIRT6 with USP48 and reduced the ubiquitination of SIRT6, whereas knockdown of USP48 increased the ubiquitination of SIRT6 (Fig. xref )."

sparser
"Du et al. described that after being stabilized by methyltransferase-like 14 (Mettl14), USP48 binds and stabilizes SIRT6 by K48-linked deubiquitination of this SIRT (K33/K128)."

sparser
"USP48 physically bound and stabilized SIRT6 by K48-linked deubiquitination at the K33 and K128 sites of SIRT6, which impeded metabolic reprogramming to hamper HCC tumorigenesis."

sparser
"CAPZA1 promotes SIRT6 stabilization by mediating the interaction of USP48 with SIRT6."

sparser
"Knockdown of CAPZA1 largely reduced the interaction between USP48 and SIRT6 (Fig. xref )."

sparser
"This dysregulation consequently affects glycolysis through the USP48-SIRT6 axis and contributes to the deterioration of HCC ( xref )."

sparser
"METTL14 also regulates the glycolytic pathway and inhibits tumor proliferation through the USP48-SIRT6 pathway xref ."

No evidence text available

sparser
"However, knockdown of CAPZA1 reduced SIRT6 binding to USP48 and thus increased SIRT6 ubiquitination (Fig. xref )."

No evidence text available

sparser
"USP48 physically binds and stabilizes SIRT6 by K48-linked deubiquitination to impede glucose metabolic reprogramming and hamper HCC tumorigenesis."

No evidence text available

No evidence text available

sparser
"These findings indicate that specifically targeting hepatocyte USP48 or the USP48-SIRT6 axis may be a potential therapeutic strategy for future HCC treatment."

No evidence text available