The impact of RNA binding proteins and the associated long non-coding RNAs in the TCA cycle on cancer pathogenesis

Tao Shen; Haiyang Wang; Bin Tang; Guoping Zhu; Xiangting Wang

doi:10.1080/15476286.2023.2216562

The impact of RNA binding proteins and the associated long non-coding RNAs in the TCA cycle on cancer pathogenesis

RNA Biol. 2023 Jan;20(1):223-234. doi: 10.1080/15476286.2023.2216562.

Authors

Tao Shen^{1

2}, Haiyang Wang¹, Bin Tang³, Guoping Zhu¹, Xiangting Wang^{4

5}

Affiliations

¹ Anhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, Anhui Provincial Engineering Research Centre for Molecular Detection and Diagnostics, College of Life Sciences, Anhui Normal University, Wuhu, China.
² Hefei National Research Center for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, China.
³ Department of Gynecology, East China Normal University Wuhu Affiliated Hospital (The Second People's Hospital of Wuhu City), Wuhu, China.
⁴ Department of Geriatrics, Gerontology Institute of Anhui Province, The First Affiliated Hospital, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
⁵ The Key Laboratory of Tumor Immunotherapy and Nutrition Therapy, Hefei, China.

Abstract

The tricarboxylic acid (TCA) cycle is a central route for generating cellular energy and precursors for biosynthetic pathways. Emerging evidences have shown that the aberrations of metabolic enzymes which affect the integrity of TCA cycle are implicated in various tumour pathological processes. Interestingly, several TCA enzymes exhibit the characteristics of RNA binding properties, and their long non-coding RNA (lncRNA) partners play critical regulatory roles in regulating the function of TCA cycle and tumour progression. In this review, we will discuss the functional roles of RNA binding proteins and their lncRNA partners in TCA cycle, with emphasis placed on the cancer progression. A further understanding of RNA binding proteins and their lncRNA partners in TCA cycle, as well as their molecular mechanisms in oncogenesis, will aid in developing novel layers of metabolic targets for cancer therapy in the near future.Abbreviations: CS: citrate synthase. AH: aconitase, including ACO1, and ACO2. IDH: isocitrate dehydrogenase, including IDH1, IDH2, and IDH3. KGDHC: α-ketoglutarate dehydrogenase complex, including OGDH, DLD, and DLST. SCS: succinyl-CoA synthase, including SUCLG1, SUCLG2, and SUCLA2. SDH: succinate dehydrogenase, including SDHA, SDHB, SDHC, and SDHD. FH: fumarate hydratase. MDH: malate dehydrogenase, including MDH1 and MDH2. PC: pyruvate carboxylase. ACLY: ATP Citrate Lyase. NIT: nitrilase. GAD: glutamate decarboxylase. ABAT: 4-aminobutyrate aminotransferase. ALDH5A1: aldehyde dehydrogenase 5 family member A1. ASS: argininosuccinate synthase. ASL: adenylosuccinate synthase. DDO: D-aspartate oxidase. GOT: glutamic-oxaloacetic transaminase. GLUD: glutamate dehydrogenase. HK: hexokinase. PK: pyruvate kinase. LDH: lactate dehydrogenase. PDK: pyruvate dehydrogenase kinase. PDH: pyruvate dehydrogenase complex. PHD: prolyl hydroxylase domain protein.

Keywords: RNA binding protein; TCA cycle; TCA cycle enzymes; long non-coding RNA; tumour progression.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Aconitate Hydratase
Carcinogenesis
Humans
Neoplasms*
RNA, Long Noncoding*
RNA-Binding Proteins

Substances

RNA, Long Noncoding
Aconitate Hydratase
RNA-Binding Proteins

Grants and funding

This work is supported by the National Natural Science Foundation of China (31970598 to X.W. and 32071270 to G.Z.), the Major Science and Technology Projects in Anhui Province (202003a06020009 to G.Z.), the University Natural Science Research Project of Anhui Province (2022AH050211 to T.S.) and the start-up funds from Anhui Normal University (762189 to T.S.).