ArticleiScience2026
PCMTD1-127aa suppresses osteosarcoma progression by competitively binding to USP10 to promote
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
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Who cites it
1 citing paper in PubMed.
- Regulatory roles of five key USP family deubiquitinases in cancer: from mechanisms to targeted therapy advances.Frontiers in pharmacology · 2026Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Osteosarcoma (OS) is a highly malignant tumor prone to distant metastasis and is associated with a poor prognosis. To date, therapeutic outcomes for this disease remain unsatisfactory. In this study, we found that circPCMTD1 encodes a 127-amino acid protein, termed PCMTD1-127aa in OS. The expression of PCMTD1-127aa was significantly lower in OS tissues than in normal paratumoral tissues. Clinical data analysis revealed that low expression of PCMTD1-127aa was associated with poor OS prognosis. Functionally, overexpression of PCMTD1-127aa not only inhibited the proliferation and invasion of osteosarcoma cells but also suppressed glycolysis in these cells. Mechanistically, PCMTD1-127aa competitively bound to the F1 (1-100) domain of USP10, thereby counteracting the USP10-mediated deubiquitination of c-MYC and subsequently promoting c-MYC degradation. We further identified that amino acid 148 of c-MYC plays a critical role in ubiquitination-mediated degradation. Our findings reveal the PCMTD1-127aa/USP10/c-MYC axis may be a promising therapeutic target for OS.
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Registered trials
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