In light of the increasing incidence of renal cell carcinoma (RCC), its molecular mechanisms have been comprehensively explored in numerous recent studies. However, few studies focus on the influence of multi-factor interactions during the occurrence and development of RCC. This study aims to investigate the quantitative global proteome and the changes in lysine succinylation in related proteins, seeking to facilitate a better understanding of the molecular mechanisms underlying RCC. LC-MS/MS combined with bioinformatics analysis are used to quantitatively detect the perspectives at the global protein level. IP and WB analysis were conducted to further verify the alternations of related proteins and lysine succinylation. A total of 3,217 proteins and 1,238 lysine succinylation sites are quantified in RCC tissues, and 668 differentially expressed proteins and 161 differentially expressed lysine succinylation sites are identified. Besides, expressions of PGK1 and PKM2 at protein and lysine, succinylation levels are significantly altered in RCC tissues. Bioinformatics analysis indicates that the glycolysis pathway is a potential mechanism of RCC progression and lysine succinylation may plays a potential role in energy metabolism. These results can provide a new direction for exploring the molecular mechanism of RCC tumorigenesis.
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http://dx.doi.org/10.1002/pmic.201800001 | DOI Listing |
Lett Appl Microbiol
January 2025
Clinical Laboratory, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Fifth School of Clinical Medicine of Zhejiang Chinese Medical University, Huzhou 313000, China.
Methicillin-resistant Staphylococcus aureus's (MRSA) resistance poses a global health challenge. This study investigates lysine succinylation in MRSA using proteomics and bioinformatics approaches to uncover metabolic and virulence mechanisms, with the goal of identifying novel therapeutic targets. Mass spectrometry and bioinformatics analyses mapped the MRSA succinylome, identifying 8048 succinylation sites on 1210 proteins.
View Article and Find Full Text PDFComput Biol Med
January 2025
Thai Nguyen University of Information and Communication Technology, Thai Nguyen City, Viet Nam. Electronic address:
Protein succinylation, a post-translational modification wherein a succinyl group (-CO-CH₂-CH₂-CO-) attaches to lysine residues, plays a critical regulatory role in cellular processes. Dysregulated succinylation has been implicated in the onset and progression of various diseases, including liver, cardiac, pulmonary, and neurological disorders. However, identifying succinylation sites through experimental methods is often labor-intensive, costly, and technically challenging.
View Article and Find Full Text PDFJ Cancer
January 2025
Key Laboratory of Translational Cancer Stem Cell Research, Department of Pathophysiology, School of Basic Medical Sciences, Hunan Normal University, Changsha, Hunan 410013, China.
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.
View Article and Find Full Text PDFAppl Biochem Biotechnol
January 2025
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
As a novel protein post-translational modification, lysine succinylation is widely involved in metabolism regulation. To describe succinylated lysine's physiological functions and distribution patterns in Saccharopolyspora erythraea, a large and global protein succinylome was identified in a hypersuccinylated strain E3ΔsucC, using high-resolution 4D label-free mass spectrometry. Bioinformatic analysis was conducted to examine the succinylated proteins further in this study.
View Article and Find Full Text PDFBiomolecules
November 2024
Department of Pediatrics, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15224, USA.
Lysine succinylation, and its reversal by sirtuin-5 (SIRT5), is known to modulate mitochondrial fatty acid β-oxidation (FAO). We recently showed that feeding mice dodecanedioic acid, a 12-carbon dicarboxylic acid (DC) that can be chain-shortened four rounds to succinyl-CoA, drives high-level protein hypersuccinylation in the peroxisome, particularly on peroxisomal FAO enzymes. However, the ability of SIRT5 to reverse DC-induced peroxisomal succinylation, or to regulate peroxisomal FAO in this context, remained unexplored.
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