ArticleCell death discovery2026
OTUB1 inhibits autophagy-dependent ferroptosis in hepatocellular carcinoma by stabilizing p62 via non-canonical deubiquitination.
Article in Cell death discovery, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitination plays a critical role in hepatocellular carcinoma (HCC) pathogenesis and is closely linked to ferroptosis. This study investigates the function of OTUB1, a deubiquitinase overexpressed in HCC, in regulating autophagy-dependent ferroptosis. Using integrated bioinformatics, biochemical assays, and xenograft models, we demonstrated that OTUB1 is upregulated in HCC and correlates with poor prognosis. Functionally, OTUB1 knockdown suppressed proliferation and induced ferroptosis, whereas its overexpression promoted malignancy. Mechanistically, OTUB1 competitively binds to p62/SQSTM1, thereby suppressing autophagic flux. Crucially, we identified that OTUB1 stabilizes p62 via non-canonical, D88-dependent deubiquitination by specifically removing K48-linked polyubiquitin chains. This stabilization hinders the initiation of autophagy-dependent ferroptosis. Pharmacological inhibition of autophagy abrogated the ferroptosis induced by OTUB1 knockdown. Furthermore, inhibiting OTUB1 sensitized HCC tumors to Lenvatinib, resulting in synergistic anti-tumor efficacy in vivo. Collectively, these findings reveal that OTUB1 drives HCC progression by stabilizing p62 to block autophagy-dependent ferroptosis. Targeting the OTUB1-p62 axis represents a novel therapeutic strategy to overcome drug resistance and improve outcomes in advanced HCC.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.