ArticleCancer genomics & proteomics
Regulation of β-Catenin Phosphorylation by PR55β in Adenoid Cystic Carcinoma.
Article in Cancer genomics & proteomics. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- RSF-1/hSNF2H Promotes the Proliferation and Migration of Adenoid Cystic Cancer Cells.Bulletin of experimental biology and medicine · 2026Article
- Current Insights on Salivary Gland Adenoid Cystic Carcinoma: Related Genes and Molecular Pathways.Genes · 2025Review
- Unique Cohorts of Salivary Gland Cancer Cells as anJournal of maxillofacial and oral surgery · 2024Article
- Integrated analysis reveals the alterations that LMNA interacts with euchromatin in LMNA mutation-associated dilated cardiomyopathy.Clinical epigenetics · 2021Article
- Clinicopathologic implications of Myb and Beta-catenin expression in adenoid cystic carcinoma.Journal of otolaryngology - head & neck surgery = Le Journal d'oto-rhino-laryngologie et de chirurgie cervico-faciale · 2020Article
- Benzene-induced mouse hematotoxicity is regulated by a protein phosphatase 2A complex that stimulates transcription ofThe Journal of biological chemistry · 2019Article
- Regulation of NF-kB Signalling Through the PR55β-RelA Interaction in Osteoblasts.In vivo (Athens, Greece)Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND/
aimAdenoid cystic carcinoma (AdCC) is a rare cancer of the salivary gland with high risk of recurrence and metastasis. Wnt signalling is critical for determining tumor grade in AdCC, as it regulates invasion and migration. β-catenin dephosphorylation plays an important role in the Wnt pathway, but its underlying molecular mechanism remains unclear. MATERIALS AND
methodsBecause the regulatory subunits of protein phosphatase 2A (PP2A) drive Wnt signalling via target molecules, including β-catenin, we used qRT-PCR and immunoblot analysis to investigate the expression of these subunits in an AdCC cell line (ACCS) and a more aggressive subline (ACCS-M).
resultsPR55β was highly expressed in ACCS-M, suggesting its functional importance. In addition, PR55β expression was associated with tumor grade, with ACCS-M exhibiting higher PR55β levels. More importantly, knockdown of PR55β in ACCS-M cells significantly reduced invasiveness and metastatic ability. Furthermore, dephosphorylation and total levels of β-catenin were dependent on PR55β in ACCS-M. Finally, we confirmed a correlation between PR55β staining intensity and histopathological type in human AdCC tissues.
conclusionOur study provides new insight into the interaction between PR55β and β-catenin and suggests that PR55β may be a target for the clinical treatment of AdCC.
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