USP1-dependent RPS16 protein stability drives growth and metastasis of human hepatocellular carcinoma cells.

ABSTRACT:

Background

Hepatocellular carcinoma (HCC) remains a medical challenge due to its high proliferation and metastasis. Although deubiquitinating enzymes (DUBs) play a key role in regulating protein degradation, their pathological roles in HCC have not been fully elucidated.

Methods

By using biomass spectrometry, co-immunoprecipitation, western blotting and immunofluorescence assays, we identify ribosomal protein S16 (RPS16) as a key substrate of ubiquitin-specific peptidase 1 (USP1). The role of USP1-RPS16 axis in the progression of HCC was evaluated in cell cultures, in xenograft mouse models, and in clinical observations.

Results

We show that USP1 interacts with RPS16. The depletion of USP1 increases the level of K48-linked ubiquitinated-RPS16, leading to proteasome-de

SUBMITTER: Liao Y 

PROVIDER: S-EPMC8215741 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature