Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation.
By B. Weinert, Christian Schölz, Sebastian A. Wagner, V. Iesmantavicius, D. Su, J. A. Daniel, Chunaram Choudhary. Cell Reports, 2013
697 citations recorded by the source corpus.
Recent studies have shown that lysines can be posttranslationally modified by various types of acylations. However, except for acetylation, very little is known about their scope and cellular distribution. We mapped thousands of succinylation sites in bacteria (E. coli), yeast (S. cerevisiae), human (HeLa) cells, and mouse liver tissue, demonstrating widespread succinylation in diverse organisms. A majority of succinylation sites in bacteria, yeast, and mouse liver were acetylated at the same position. Quantitative analysis of succinylation in yeast showed that succinylation was globally altered by growth conditions and mutations that affected succinyl-coenzyme A (succinyl-CoA) metabolism in the tricarboxylic acid cycle, indicating that succinylation levels are globally affected by succinyl-CoA concentration. We preferentially detected succinylation on abundant proteins, suggesting that succinylation occurs at a low level and that many succinylation sites remain unidentified. These data provide a systems-wide view of succinylation and its dynamic regulation and show its extensive overlap with acetylation.
Subfields: Geriatrics and Gerontology, Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/a72e5312c74d3e3c5896de54239cbf896382595b
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Geriatrics and Gerontology
In Molecular Biology
In Oncology
Citations in the corpus
- Lysine Glutarylation Is a Protein Post-Translational Modification Regulated by SIRT5 (2014, background): “In addition, lysine succinylation is an abundant protein PTM in diverse model organisms (Weinert et al., 2013).”
- Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “…between H3K9 acetylation and methylation (Nicolas et al., 2003), dynamic competition of H4 K5K8 acetylation and butyrylation (Goudarzi et al., 2016), and the overlap of succinylation sites and acetylation sites in diverse organisms including bacteria, yeast, and human cells (Weinert et al., 2013).”