98%
921
2 minutes
20
Lysine succinylation is an emerging post-translational modification of proteins. It involves the addition of the succinyl group to lysine residues of target proteins through both enzymatic and non-enzymatic pathways. This modification can alter the structure of the target protein, which, in turn, impacts protein activity and function and is involved in a wide range of diseases. In the field of cancer biology, lysine succinylation has been shown to exert a substantial influence on metabolic reprogramming of tumor cells, regulation of gene expression, and activation of oncogenic signaling pathways. Furthermore, lysine succinylation modulates the activity of immune cells, thereby affecting the immune evasion of tumor cells. Notably, researchers are currently developing inhibitors and activators of lysine succinylation which can inhibit tumor cell proliferation, migration, and metastasis, with potential usefulness in future clinical practice. This article provides an overview of the biological functions of lysine succinylation in cancer and its potential applications in cancer treatment, offering a novel perspective for future cancer management.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11705062 | PMC |
http://dx.doi.org/10.7150/jca.105849 | DOI Listing |
Arch Biochem Biophys
September 2025
Department of Chemistry and Biochemistry, Howard College of Arts and Sciences, Samford University, 800 Lakeshore Drive, Birmingham, AL, USA, 35229. Electronic address:
Tetrahydrodipicolinate N-succinyltransferase (DapD) catalyzes the reaction of tetrahydrodipicolinate (THDP) and succinyl-CoA to form (S)-2-(3-carboxypropanamido)-6-oxoheptanedioic acid and coenzyme A. The enzyme is in the diaminopimelate-lysine biosynthesis pathway which produces two metabolites necessary for the survival and growth of pathogenic bacteria. Since lysine is an essential amino acid to humans, DapD is a potentially safe target for antibiotic therapies.
View Article and Find Full Text PDFBioinform Adv
August 2025
Department of CSE, BUET, Dhaka 1000, Bangladesh.
Motivation: Lysine (K) succinylation is a crucial post-translational modification involved in cellular homeostasis and metabolism, and has been linked to several diseases in recent research. Despite its emerging importance, current computational methods are limited in performance for predicting succinylation sites.
Results: We propose ResLysEmbed, a novel ResNet-based architecture that combines traditional word embeddings with per-residue embeddings from protein language models for succinylation site prediction.
Cancers (Basel)
August 2025
Institute of Biochemistry, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.
Lysine succinylation is a recently discovered post-translational protein modification, the process of which requires the participation of various enzymes. The close association between cancer and protein post-translational modifications (PTMs), such as acetylation and phosphorylation, has been extensively investigated and well-established. In recent years, growing attention has been directed toward the role of succinylation in cancer progression.
View Article and Find Full Text PDFInt J Surg
August 2025
Department of Urology, The First Affiliated Hospital of Dalian Medical University, Dalian, China.
Lysine succinylation is the covalent modification of succinyl groups (-CO-CH ₂ -CH ₂ -COOH) to lysine residues of target proteins, which causes conformational changes and regulates their functional states. In this figure, mitochondria are used as the metabolic hub to summarize the production and consumption of succinyl-CoA in the TCA cycle and mediate the succinylation of key enzymes and transcription factors such as PDH, SDH, GLUD1, HMGCS2, and FEN1. The central region showed the negative regulation of SIRT5/SIRT7 and the positive regulation of KAT2A, alpha-KGDH, CPT1A, HAT1, and other acyltransferases.
View Article and Find Full Text PDFMol Oral Microbiol
August 2025
State Key Laboratory of Oral Diseases & National Center for Stomatology & National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, China.
Lysine succinylation (Ksuc) is a novel post-translational modification (PTM), which regulates biological functions in bacteria. Streptococcus mutans has been identified as a predominant cariogenic pathogen responsible for the initiation and progression of dental caries. However, lysine succinylation in S.
View Article and Find Full Text PDF