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Review
. 2024 Aug 12:12:e17768.
doi: 10.7717/peerj.17768. eCollection 2024.

The role of protein post-translational modifications in prostate cancer

Affiliations
Review

The role of protein post-translational modifications in prostate cancer

Yinghui Hao et al. PeerJ. .

Abstract

Involving addition of chemical groups or protein units to specific residues of the target protein, post-translational modifications (PTMs) alter the charge, hydrophobicity, and conformation of a protein, which in turn influences protein function, protein-protein interaction, and protein aggregation. These alterations, which include phosphorylation, glycosylation, ubiquitination, methylation, acetylation, lipidation, and lactylation, are significant biological events in the development of cancer, and play vital roles in numerous biological processes. The processes behind essential functions, the screening of clinical illness signs, and the identification of therapeutic targets all depend heavily on further research into the PTMs. This review outlines the influence of several PTM types on prostate cancer (PCa) diagnosis, therapy, and prognosis in an effort to shed fresh light on the molecular causes and progression of the disease.

Keywords: Diagnosis; Prognosis; Prostate cancer; Protein post-translational modification; Treatment.

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Conflict of interest statement

The authors declare there are no competing interests.

Figures

Figure 1
Figure 1. Schematic diagram of PI3K/Akt/mTOR signaling pathway.
PTEN, phosphatidylinositol 3-kinase (PI3K) mediates the production of phosphatidylinositol 4, 5-diphosphate (PIP2) from phosphatidylinositol triphosphate (PIP3). PIP3 recruits PDK1, a protein with PH domain, phosphorylates and disrupts tuberculosis complex 1/2 (TSC1-TSC2) through Akt, and phosphorylates mTOR through RHEB. The two complexes that mTOR proteins are involved in are mTOR protein complex 1 (mTORC1) and mTOR protein complex 2 (mTORC2). mTORC1 increases protein translation by phosphorylation of its two direct targets and P70S6K. The arrows represent promotion, and the others represent inhibition.
Figure 2
Figure 2. Some types and structures of glycosylation.

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Grants and funding

This work was supported by the Guangdong Provincial Medical Science and Technology Research Fund Projects (Nos. A2023216; A2022524; A2020304), Basic and Applied Basic Research Foundation of Guangdong Province (No. 2022A1515220217), Science and Technology Program of Guangzhou (Nos. 202201010840; 202201010810; 202102080532; 202002030032; 202002020023; 20211A011116). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

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