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The subcellular distribution of phosphorylated Y‐box‐binding protein‐1 at S102 in colorectal cancer patients, stratified by KRAS mutational status and clinicopathological features
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The subcellular distribution of phosphorylated Y‐box‐binding protein‐1 at S102 in colorectal cancer patients, stratified by KRAS mutational status and clinicopathological features
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The subcellular distribution of phosphorylated Y‐box‐binding protein‐1 at S102 in colorectal cancer patients, stratified by KRAS mutational status and clinicopathological features
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Journal Article
The subcellular distribution of phosphorylated Y‐box‐binding protein‐1 at S102 in colorectal cancer patients, stratified by KRAS mutational status and clinicopathological features
2025
Overview
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. This study identifies nuclear YB‐1 S102 phosphorylation as a marker associated with KRAS and FBXW7 mutations in colorectal cancer. Mutated KRAS correlates specifically with nuclear, not cytoplasmic, S102 YB‐1. These findings provide the first ex vivo evidence of this link in CRC and suggest future studies should assess the prognostic and therapeutic relevance of its subcellular localization.
Publisher
John Wiley & Sons, Inc,Wiley
Subject
/ Aged
/ Cancer
/ Colorectal Neoplasms - genetics
/ Colorectal Neoplasms - metabolism
/ Colorectal Neoplasms - pathology
/ Ethylenediaminetetraacetic acid
/ Female
/ Humans
/ Kinases
/ Male
/ Mutation
/ Post-translational modification
/ Proto-Oncogene Proteins p21(ras) - genetics
/ Subcellular Fractions - metabolism
/ Vascular endothelial growth factor
