ArticleMolecular oncology2025
The subcellular distribution of phosphorylated Y-box-binding protein-1 at S102 in colorectal cancer patients, stratified by KRAS mutational status and clinicopathological features.
Article in Molecular oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Y-box binding protein-1 at the crossroads of DNA damage response and tumor immune evasion.JNCI cancer spectrum · 2026Review
- Inhibition of YB-1 phosphorylation enhances cisplatin activity and disrupts cell division in pleural mesothelioma.British journal of cancer · 2025Article
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Authors and funding
10 authors.
Funding
Abstract
Oncoprotein Y-box-binding protein-1 (YB-1) is involved in all cancer hallmarks. One of the most studied post-translational modifications of YB-1 is phosphorylation on Serine 102 (S102), which is involved in cancer progression. KRAS mutations are frequent, have been associated with poor prognosis and therapy resistance, and they are considered a major stimulator of S102 YB-1 in vitro. In this study, a relationship between S102 YB-1 phosphorylation in subcellular fractions and KRAS mutation was investigated in CRC tissues, and its association with clinicopathological parameters was analyzed. Immunohistochemistry on 36 patient samples and 5 normal tissue samples highlighted nuclear S102 YB-1 was specific to cancer tissues. Nuclear S102 YB-1 was expressed in 47.2% of tumor tissues, which was positively correlated with KRAS mutation (P = 0.017). There was no significant association between cytoplasmic S102 YB-1 with KRAS mutation status (P = 0.391). Further studies in larger cohorts are needed to validate the observed results. The significant association between S102 YB-1 in the nucleus and KRAS mutation may suggest YB-1 as an effective target to improve survival of CRC patients with KRAS-mutated tumors.
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