
Deciphering functional roles of protein succinylation and …
Mar 26, 2024 · Post-translational modifications (PTMs) dynamically regulate cellular processes. Lysine undergoes a range of acylations, including malonylation, succinylation (SucK) and glutarylation (GluK).
Protein succinylation: regulating metabolism and beyond - PMC
Succinylation of proteins contributes to many cellular processes such as proliferation, growth, differentiation, metabolism and even tumorigenesis. Mechanically, Succinylation leads to conformation alteration of chromatin or remodeling. As a result, transcription/expression of target genes is changed accordingly.
A review of the mechanism of succinylation in cancer - PMC
Lysine succinylation is a novel, broad-spectrum, dynamic, non-enzymatic protein post-translational modification (PTM). Succinylation is essential for the regulation of protein function and control of various signaling and regulatory pathways. It is ...
The dawn of succinylation: a posttranslational modification
Studies of acetylation have led research to focus on other acyl modifications of lysine residues, such as succinylation, malonylation, and glutarylation. This paper will explore and explain the relatively new, and compelling, modification called succinylation.
SUCLA2 mutations cause global protein succinylation ... - Nature
Nov 23, 2020 · Here, we show that succinyl-CoA accumulates in cells derived from patients with recessive mutations in the tricarboxylic acid cycle (TCA) gene succinyl-CoA ligase subunit-β (SUCLA2), causing global...
Identification of lysine succinylation as a new post ... - Nature
Dec 12, 2010 · Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation. The succinyllysine residue was initially...
Succinylation - an overview | ScienceDirect Topics
Succinylation is a post-translational modification, in which a succinyl moiety is attached on a lysine residue through an amide bond. This modification masks the positive charge on lysine, thereby resulting in a likely significant conformational change.
Protein succinylation mechanisms and potential targeted …
Succinylation is a relatively common post-translational modification. It occurs in the cytoplasm, mitochondria, and the nucleus, where its essential precursor, succinyl-CoA, is present, allowing for the modification of non-histone and histone proteins.
Succinylation Links Metabolism to Protein Functions
Mar 22, 2019 · Succinylation causes a protein charge flip from positive to negative and a relatively large increase in mass compared to other PTMs. Hundreds of protein succinylation sites are present in proteins of multiple tissues and species, and the significance is …
The growing landscape of succinylation links metabolism and …
Feb 19, 2021 · Succinylation is a newly discovered post-translational modification with the hallmark of a significant chemical and structural change. Succinylation has many similarities with other modifications, but succinylation may lead to more functional changes.
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