# Ribosome-binding protein 1: A multidimensional regulator of cancer progression and a novel target for precision therapy (Review)

**Authors:** Ho Huang, Jia Ouyang

PMC · DOI: 10.3892/ol.2025.15358 · Oncology Letters · 2025-10-23

## TL;DR

This review explores how ribosome-binding protein 1 (RRBP1) influences cancer progression and could be a target for precision therapy.

## Contribution

The paper identifies RRBP1 as a multidimensional regulator in cancer and a potential target for precision therapies.

## Key findings

- RRBP1 regulates cancer cell adaptation to stress and chemotherapy by stabilizing glucose-regulated protein 78.
- RRBP1 fusion genes exacerbate malignant progression through kinase and deubiquitination pathways.
- RRBP1 has environment-dependent roles in neurodegeneration, cardiovascular homeostasis, and bone metabolism.

## Abstract

Ribosome-binding protein 1 (RRBP1), a core regulator of endoplasmic reticulum-ribosome interactions, serves key roles in the development and progression of various cancer types by coordinating protein synthesis and organelle dynamic interactions. RRBP1 regulates the unfolded protein response by stabilizing glucose-regulated protein 78 and it enhances cancer cell adaptation to endoplasmic reticulum stress and chemotherapy. The stability of RRBP1 is regulated by N6-methyladenosine modification by methyltransferase-like 3 and deubiquitination by ubiquitin-specific processing protease 35. Furthermore, RRBP1 drives cellular anti-apoptosis mechanisms by activating pro-survival pathways such as TGF-β1/SMAD, PI3K/AKT and Notch or binding cyclic RNAs. By contrast, aberrant activation of kinase function and deubiquitination pathways by RRBP1 fusion genes [RRBP1-anaplastic lymphoma kinase, RRBP1-Raf1 proto-oncogene, serine/threonine kinase and RRBP1-ubiquitin specific peptidase 6] exacerbates malignant progression. Furthermore, the pleiotropic regulation of RRBP1 in neurodegeneration, cardiovascular homeostasis and bone metabolism highlights its environment-dependent functions. The present review identified the multidimensional regulatory network of RRBP1 in cancer and non-cancer systems to enhance the understanding of its molecular mechanism, demonstrated its broad regulatory value and potentially provided a key entry point to analyze the disease and develop precision therapies.

## Linked entities

- **Genes:** RRBP1 (ribosome binding protein 1) [NCBI Gene 6238], TGFB1 (transforming growth factor beta 1) [NCBI Gene 7040], PIK3CA (phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha) [NCBI Gene 5290], AKT1 (AKT serine/threonine kinase 1) [NCBI Gene 207], Notch (neurogenic locus notch homolog) [NCBI Gene 100616083]
- **Diseases:** cancer (MONDO:0004992)

## Full-text entities

- **Genes:** AKT1 (AKT serine/threonine kinase 1) [NCBI Gene 207] {aka AKT, PKB, PKB-ALPHA, PRKBA, RAC, RAC-ALPHA}, PIK3CB (phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta) [NCBI Gene 5291] {aka P110BETA, PI3K, PI3KBETA, PIK3C1}, TGFB1 (transforming growth factor beta 1) [NCBI Gene 7040] {aka CAEND1, CED, DPD1, IBDIMDE, LAP, TGF-beta1}, METTL3 (methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit) [NCBI Gene 56339] {aka IME4, M6A, MT-A70, Spo8, hMETTL3}, RAF1 (Raf-1 proto-oncogene, serine/threonine kinase) [NCBI Gene 5894] {aka CMD1NN, CRAF, NS5, Raf-1, c-Raf}, USP35 (ubiquitin specific peptidase 35) [NCBI Gene 57558], RRBP1 (ribosome binding protein 1) [NCBI Gene 6238] {aka ES/130, ES130, RRp, hES, p180}, USP6 (ubiquitin specific peptidase 6) [NCBI Gene 9098] {aka HRP1, TRE17, TRE2, TRESMCR, Tre-2, USP6-short}
- **Diseases:** cancer (MESH:D009369), neurodegeneration (MESH:D019636)
- **Chemicals:** N6-methyladenosine (MESH:C010223)

## Full text

_Full body text omitted from this summary view._ Fetch the complete paper as Markdown: https://tomesphere.com/paper/PMC12587471/full.md

## Figures

6 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12587471/full.md

## References

87 references — full list in the complete paper: https://tomesphere.com/paper/PMC12587471/full.md

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Source: https://tomesphere.com/paper/PMC12587471