GO:0036055 protein-succinyllysine desuccinylase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0036055 describes the enzymatic removal of a succinyl group from a succinylated lysine residue on a protein, using NAD+ as a cofactor.
• SIRT5 is the best-characterized enzyme with protein-succinyllysine desuccinylase activity, and it also removes malonyl and glutaryl groups.
• Desuccinylation by SIRT5 regulates mitochondrial metabolism, fatty acid oxidation, oxidative stress, and inflammation [1,3,5,6,8].
• Dysregulated desuccinylation is linked to acute liver injury, diabetic cardiomyopathy, cancer, sepsis, and intervertebral disc degeneration [1,3,4,5,6,7].
• Studying GO:0036055 requires tools such as succinylome proteomics, site-specific antibodies, and CRISPR-engineered cell and animal models [2,8].
• EDITGENE provides knockout, point-mutation, knock-in, overexpression, and library screening services to dissect desuccinylase biology.
Description
Protein-succinyllysine desuccinylase activity (GO:0036055) is a molecular function that catalyzes the removal of a succinyl group from N(6)-succinyl-L-lysine residues on target proteins, consuming NAD+ and producing 2''-O-succinyl-ADP-D-ribose, nicotinamide, and the unmodified lysine. This reaction is a key component of the mitochondrial sirtuin pathway and is primarily mediated by SIRT5, which was initially identified as a NAD-dependent protein lysine demalonylase and desuccinylase. The discovery that SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks has placed this enzymatic activity at the center of mitochondrial physiology and disease research. Researchers study GO:0036055 because it directly controls the succinylation status of metabolic enzymes and signaling proteins. For example, SIRT5-mediated desuccinylation of ALDH2 alleviates mitochondrial oxidative stress in acetaminophen-induced acute liver injury, while desuccinylation of CPT2 improves fatty acid metabolism in diabetic cardiomyopathy. In cancer, SIRT5-mediated desuccinylation of ME2 promotes tumor growth by enhancing mitochondrial respiration. These findings demonstrate that protein-succinyllysine desuccinylase activity is not a housekeeping function but a regulatory node with broad physiological and pathological impact. The importance of GO:0036055 extends to inflammation, sepsis, and tissue degeneration. SIRT5 desuccinylates TBK1 to regulate macrophage inflammatory responses in sepsis, and desuccinylation of AIFM1 protects against compression-induced intervertebral disc degeneration by maintaining mitochondrial homeostasis. Additionally, SIRT5-related lysine demalonylation of GSTP1 contributes to cardiomyocyte pyroptosis suppression in diabetic cardiomyopathy. Together, these studies highlight the need for precise experimental models to dissect the substrates, regulators, and therapeutic potential of this enzymatic activity.
protein-succinyllysine desuccinylase activity At A Glance
| GO ID | GO:0036055 |
|---|---|
| GO term | protein-succinyllysine desuccinylase activity |
| Ontology | molecular_function |
| Synonym | peptidyl-succinyllysine desuccinylase activity; succinyl lysine desuccinylase activity; succinyllysine desuccinylase activity |
| Major function | Removal of succinyl groups from succinylated lysine residues on proteins, using NAD+ as a cofactor |
| Reaction | N(6)-succinyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-succinyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein] |
| Primary enzyme | SIRT5 (sirtuin 5), a mitochondrial NAD-dependent desuccinylase [2,8] |
| Related activities | Protein lysine demalonylase and deglutarylase activities, also catalyzed by SIRT5 |
| Biological context | Mitochondrial metabolism, fatty acid oxidation, oxidative stress response, and inflammation [1,3,5,6,8] |
What Is GO:0036055?
Protein-succinyllysine desuccinylase activity (GO:0036055) is defined as the catalysis of the reaction: N(6)-succinyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-succinyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]. In simpler terms, it is an enzymatic activity that removes a succinyl chemical tag from a lysine residue on a protein, using NAD+ as a co-substrate and releasing nicotinamide and 2''-O-succinyl-ADP-D-ribose as byproducts. This activity belongs to the molecular_function ontology and is also known as peptidyl-succinyllysine desuccinylase activity, succinyl lysine desuccinylase activity, or succinyllysine desuccinylase activity.
Why Is protein-succinyllysine desuccinylase activity Important in Cell Biology?
Protein-succinyllysine desuccinylase activity is critically important because it reverses protein succinylation, a post-translational modification that alters enzyme activity, protein stability, and protein-protein interactions. SIRT5 is the principal enzyme carrying this activity, and its loss or dysregulation leads to hyper-succinylation of mitochondrial proteins, metabolic inflexibility, and increased susceptibility to oxidative stress [2,8]. Studies in acute liver injury, diabetic cardiomyopathy, cancer, sepsis, and intervertebral disc degeneration have shown that modulating this activity can protect or harm tissues depending on context [1,3,4,5,6,7]. Therefore, understanding GO:0036055 provides mechanistic insight into mitochondrial quality control and offers potential therapeutic targets for metabolic and inflammatory diseases.
• Regulates mitochondrial energy metabolism by controlling succinylation of metabolic enzymes such as CPT2 and ME2 [3,5].
• Protects against oxidative stress in acute liver injury through desuccinylation of ALDH2.
• Modulates inflammatory responses in sepsis via desuccinylation of TBK1 in macrophages.
• Suppresses cardiomyocyte pyroptosis in diabetic cardiomyopathy through SIRT5-related demalonylation of GSTP1.
• Maintains mitochondrial homeostasis and protects against intervertebral disc degeneration via AIFM1 desuccinylation.
• Serves as a key regulator of the mitochondrial lysine succinylome and metabolic networks.
• Provides a mechanism for crosstalk between NAD+ availability and protein acylation status.
• Represents a druggable target for metabolic diseases, cancer, and inflammation [1,3,5,6].
• Enables researchers to study the functional consequences of site-specific lysine succinylation [2,8].
• Underpins the development of CRISPR models to test causality of desuccinylase-substrate axes [1,3,5,6,7].
Molecular Mechanism of protein-succinyllysine desuccinylase activity
Substrate recognition and binding
In simple terms: The enzyme first finds and grabs onto a protein that has a succinyl tag on one of its lysine residues.
The desuccinylase enzyme, primarily SIRT5, recognizes N(6)-succinyl-L-lysine on target proteins. This recognition is mediated by the sirtuin catalytic core, which accommodates the succinyl group within a hydrophobic tunnel. SIRT5 was shown to preferentially bind succinylated peptides and to remove succinyl groups from mitochondrial proteins. The substrate specificity is determined by both the succinyl-lysine mark and the surrounding amino acid sequence, as demonstrated by succinylome analyses.
NAD+ binding and cofactor role
In simple terms: The enzyme uses NAD+ as a helper molecule to perform the chemical reaction.
The desuccinylation reaction requires NAD+ as a co-substrate. SIRT5 is an NAD-dependent enzyme, and its activity is coupled to the cleavage of NAD+ into nicotinamide and 2''-O-succinyl-ADP-D-ribose. This dependence links desuccinylase activity to cellular NAD+ levels and metabolic status [2,8].
Catalytic cleavage of the succinyl-lysine bond
In simple terms: The enzyme cuts the bond between the succinyl group and the lysine, releasing the succinyl group as part of a larger byproduct.
Following NAD+ binding, the enzyme catalyzes the removal of the succinyl group from the lysine residue. The reaction yields 2''-O-succinyl-ADP-D-ribose, nicotinamide, and the unmodified lysine on the target protein. This catalytic step is conserved among sirtuins but SIRT5 has evolved to efficiently process negatively charged acyl groups such as succinyl, malonyl, and glutaryl.
Product release and restoration of lysine
In simple terms: After the succinyl group is removed, the protein is left with a normal lysine, and the byproducts are released.
The desuccinylation reaction restores the target lysine to its unmodified state, which can alter the protein's function, stability, or interactions. For example, desuccinylation of ALDH2 restores its enzymatic activity and reduces oxidative stress, while desuccinylation of CPT2 enhances fatty acid oxidation. The byproducts 2''-O-succinyl-ADP-D-ribose and nicotinamide are released into the cellular environment.
Regulation by NAD+ availability and metabolic state
In simple terms: The enzyme works faster or slower depending on how much NAD+ is available in the cell.
Because SIRT5 requires NAD+, its desuccinylase activity is sensitive to cellular NAD+ levels, which fluctuate with metabolic state. SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks, and its activity is linked to mitochondrial respiration and fatty acid oxidation. In diabetic cardiomyopathy, SIRT5-mediated desuccinylation of CPT2 improves fatty acid metabolism, indicating that metabolic stress can modulate this activity.
Key Genes Involved in GO:0036055 protein-succinyllysine desuccinylase activity
The following genes and proteins are central to protein-succinyllysine desuccinylase activity, either as the enzyme itself or as validated substrates whose desuccinylation has been experimentally demonstrated.
| Gene | Major Role | Research Relevance |
|---|---|---|
| SIRT5 | Primary NAD-dependent desuccinylase enzyme | Central to GO:0036055; regulates mitochondrial succinylome and metabolism [2,8] |
| ALDH2 | Substrate; mitochondrial aldehyde dehydrogenase | Desuccinylation by SIRT5 alleviates oxidative stress in acute liver injury |
| CPT2 | Substrate; carnitine palmitoyltransferase 2 | Desuccinylation improves fatty acid metabolism in diabetic cardiomyopathy |
| GSTP1 | Substrate; glutathione S-transferase pi 1 | SIRT5-related demalonylation suppresses cardiomyocyte pyroptosis |
| ME2 | Substrate; malic enzyme 2 | Desuccinylation promotes cancer growth via mitochondrial respiration |
| TBK1 | Substrate; TANK-binding kinase 1 | Desuccinylation regulates macrophage inflammatory response in sepsis |
| AIFM1 | Substrate; apoptosis-inducing factor 1 | Desuccinylation protects against intervertebral disc degeneration |
| SDHA | Substrate; succinate dehydrogenase complex flavoprotein subunit A | Succinylation target regulated by SIRT5 in mitochondrial networks |
| IDH2 | Substrate; isocitrate dehydrogenase 2 | Succinylation target in mitochondrial metabolism |
| PDHA1 | Substrate; pyruvate dehydrogenase E1 subunit alpha 1 | Succinylation target linked to metabolic regulation |
| ACAT1 | Substrate; acetyl-CoA acetyltransferase 1 | Succinylation target in mitochondrial fatty acid oxidation |
| HADHA | Substrate; hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha | Succinylation target in fatty acid oxidation |
| GAPDH | Substrate; glyceraldehyde-3-phosphate dehydrogenase | Succinylation target with potential metabolic impact |
| ATP5A1 | Substrate; ATP synthase F1 subunit alpha | Succinylation target in oxidative phosphorylation |
| MDH2 | Substrate; malate dehydrogenase 2 | Succinylation target in TCA cycle |
| CS | Substrate; citrate synthase | Succinylation target in mitochondrial metabolism |
| OGDH | Substrate; oxoglutarate dehydrogenase | Succinylation target in TCA cycle |
How Is protein-succinyllysine desuccinylase activity Regulated?
Protein-succinyllysine desuccinylase activity is primarily regulated by the availability of NAD+ and the expression level of SIRT5. SIRT5 is an NAD-dependent enzyme, so its activity fluctuates with cellular energy status and NAD+ biosynthesis. In addition, SIRT5 expression and activity can be modulated by metabolic stress, as seen in diabetic cardiomyopathy where SIRT5-mediated desuccinylation of CPT2 improves fatty acid metabolism. The activity is also influenced by substrate availability and the presence of other acyl modifications that compete for the same lysine residues. Furthermore, SIRT5-related desuccinylation of specific substrates such as TBK1 in sepsis indicates that inflammatory signaling can regulate or be regulated by this activity.
protein-succinyllysine desuccinylase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| SIRT5 | Acute liver injury, diabetic cardiomyopathy, cancer, sepsis, intervertebral disc degeneration | Sirt5 knockout mice, CRISPR knockout cell lines, overexpression models [1,3,4,5,6,7] |
| ALDH2 | Acetaminophen-induced acute liver injury | ALDH2 point-mutation knock-in mice, hepatocyte-specific knockout |
| CPT2 | Diabetic cardiomyopathy, cardiac lipotoxicity | Cpt2 knockout or desuccinylation-site mutant knock-in cardiomyocytes |
| ME2 | Cancer growth and mitochondrial respiration | ME2 knockout cancer cell lines, xenograft models |
| TBK1 | Sepsis and macrophage inflammation | TBK1 desuccinylation-site mutant knock-in macrophages, Sirt5 knockout mice |
| AIFM1 | Intervertebral disc degeneration | AIFM1 mutant knock-in nucleus pulposus cells, Sirt5 knockout mice |
Acute liver injury and oxidative stress
SIRT5-mediated desuccinylation of ALDH2 alleviates mitochondrial oxidative stress following acetaminophen-induced acute liver injury. This study demonstrates that loss of desuccinylase activity leads to hyper-succinylation and inactivation of ALDH2, exacerbating liver damage. The findings suggest that enhancing GO:0036055 activity could be protective in acute liver injury.
Diabetic cardiomyopathy and cardiac lipotoxicity
SIRT5 improves cardiomyocyte fatty acid metabolism and ameliorates cardiac lipotoxicity in diabetic cardiomyopathy via CPT2 de-succinylation. Additionally, SIRT5-related lysine demalonylation of GSTP1 contributes to cardiomyocyte pyroptosis suppression in diabetic cardiomyopathy. These studies link desuccinylase activity to cardiac protection under metabolic stress [3,4].
Cancer metabolism and tumor growth
SIRT5-mediated ME2 desuccinylation promotes cancer growth by enhancing mitochondrial respiration. This indicates that in certain cancers, high desuccinylase activity supports tumor metabolism. Targeting GO:0036055 may therefore be a therapeutic strategy in cancers dependent on mitochondrial respiration.
Sepsis and inflammatory responses
Desuccinylation of TBK1 by SIRT5 regulates inflammatory responses of macrophages in sepsis. This study shows that SIRT5-mediated desuccinylation of TBK1 is required for proper macrophage activation and that dysregulation contributes to sepsis pathology. Modulating this activity could influence inflammatory outcomes.
Intervertebral disc degeneration
SIRT5-related desuccinylation modification of AIFM1 protects against compression-induced intervertebral disc degeneration by regulating mitochondrial homeostasis. This finding expands the role of GO:0036055 beyond metabolic tissues to musculoskeletal degeneration.
From protein-succinyllysine desuccinylase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of SIRT5 desuccinylase activity alter mitochondrial metabolism? | SIRT5 knockout cell lines and mice [2,8] |
| Is a specific lysine succinylation site on ALDH2 functionally important? | ALDH2 point-mutation knock-in (K-to-R or K-to-Q) cell and mouse models |
| Does desuccinylation of CPT2 improve fatty acid oxidation? | CPT2 desuccinylation-site mutant knock-in cardiomyocytes |
| Can overexpression of SIRT5 protect against oxidative stress? | SIRT5 overexpression in hepatocytes or cardiomyocytes [1,3] |
| What is the role of SIRT5 in cancer growth? | SIRT5 knockout or overexpression in cancer cell lines and xenografts |
| Does TBK1 desuccinylation regulate macrophage inflammation? | TBK1 knock-in mutants in macrophages, Sirt5 knockout mice |
How to Study the protein-succinyllysine desuccinylase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Succinylome proteomics | Global lysine succinylation sites and stoichiometry | Mapping SIRT5 substrates and pathways [2,8] |
| Site-specific Western blot | Succinylation level of a specific protein | Validating desuccinylation of ALDH2, CPT2, TBK1 [1,3,6] |
| In vitro desuccinylase assay | Enzymatic removal of succinyl groups from substrates | Testing SIRT5 activity and inhibitor effects |
| NAD+ quantification | Cellular NAD+ levels | Linking metabolic state to desuccinylase activity [2,8] |
| CRISPR knockout | Loss-of-function effects on succinylation and phenotype | Testing causality of SIRT5 in disease models [1,3,5,6,7] |
| CRISPR knock-in | Site-specific lysine mutations (K-to-R, K-to-Q) | Dissecting the function of individual succinylation sites [1,3,6] |
| Overexpression | Gain-of-function effects on desuccinylation | Testing protective or oncogenic roles of SIRT5 [1,5] |
| Co-immunoprecipitation | Protein-protein interactions between SIRT5 and substrates | Identifying novel desuccinylation targets [2,8] |
Succinylome proteomics
Succinylome proteomics uses mass spectrometry to identify and quantify lysine succinylation sites across the proteome. This method is essential for mapping the substrates of GO:0036055 and for determining how loss of SIRT5 alters global succinylation patterns [2,8]. Researchers can compare wild-type and SIRT5 knockout cells or tissues to identify hyper-succinylated proteins.
Site-specific antibodies and Western blotting
Site-specific antibodies against succinylated lysine residues on target proteins such as ALDH2, CPT2, or TBK1 allow researchers to monitor desuccinylation events by Western blotting. This approach is used to confirm that SIRT5 directly removes succinyl groups from specific substrates [1,3,6].
Enzymatic activity assays
In vitro desuccinylase activity assays use recombinant SIRT5 and succinylated peptide or protein substrates in the presence of NAD+. The reaction can be monitored by detecting the release of nicotinamide or 2''-O-succinyl-ADP-D-ribose, or by measuring the decrease in succinylated substrate using mass spectrometry or antibodies.
CRISPR-based functional genomics
CRISPR knockout, point-mutation knock-in, and overexpression models enable causal testing of desuccinylase-substrate axes. For example, knocking out SIRT5 or mutating specific lysine residues on substrates can reveal their roles in metabolism, inflammation, and disease [1,3,5,6,7].
How CRISPR Can Be Used to Study GO:0036055 protein-succinyllysine desuccinylase activity
Knockout
CRISPR knockout of SIRT5 or its substrates is used to abolish protein-succinyllysine desuccinylase activity or the modification site, respectively. SIRT5 knockout cells and mice exhibit hyper-succinylation of mitochondrial proteins and metabolic defects, making them valuable for studying GO:0036055 in liver injury, cardiomyopathy, cancer, and sepsis [1,3,5,6,7,8].
Point Mutation
Point mutations can be introduced into the catalytic domain of SIRT5 to abrogate enzymatic activity without deleting the protein, or into specific lysine residues of substrates (e.g., K-to-R to mimic desuccinylation, K-to-Q to mimic succinylation). These models help distinguish catalytic activity from scaffolding functions and test the importance of individual succinylation sites [1,3,6].
Knock-in
Knock-in models can introduce epitope tags (e.g., FLAG, HA) into endogenous SIRT5 or substrates for tracking and purification, or can express mutant versions of substrates that cannot be desuccinylated. These models are useful for studying endogenous protein interactions and for validating antibody specificity [1,3,6].
Overexpression
Overexpression of SIRT5 or its substrates can enhance or suppress desuccinylation flux. For example, SIRT5 overexpression protects against oxidative stress in hepatocytes and improves fatty acid metabolism in cardiomyocytes, while ME2 overexpression promotes cancer growth [1,3,5]. Overexpression models are valuable for gain-of-function studies and for testing therapeutic hypotheses.
How EDITGENE Supports protein-succinyllysine desuccinylase activity Research
Researchers studying protein-succinyllysine desuccinylase activity-related genes often need to determine whether a candidate gene is causally involved in a specific metabolic or disease phenotype. This requires precise genetic models that can knockout, mutate, tag, or overexpress the gene of interest in relevant cell types. EDITGENE provides a comprehensive suite of CRISPR-based services to accelerate such investigations.
Contact EDITGENE today to design your custom CRISPR model for protein-succinyllysine desuccinylase activity research.
Frequently Asked Questions About protein-succinyllysine desuccinylase activity
What is protein-succinyllysine desuccinylase activity?
It is an enzymatic activity (GO:0036055) that removes a succinyl group from a succinylated lysine residue on a protein, using NAD+ as a cofactor and producing 2''-O-succinyl-ADP-D-ribose, nicotinamide, and the unmodified lysine.
What genes are involved in protein-succinyllysine desuccinylase activity?
The primary gene is SIRT5, which encodes a mitochondrial NAD-dependent desuccinylase. Substrates include ALDH2, CPT2, GSTP1, ME2, TBK1, and AIFM1 [1,2,3,4,5,6,7].
What is the role of SIRT5 in desuccinylation?
SIRT5 is the main enzyme that catalyzes protein-succinyllysine desuccinylase activity. It removes succinyl groups from mitochondrial proteins and regulates metabolic networks, oxidative stress, and inflammation [2,8].
How is protein-succinyllysine desuccinylase activity measured?
It can be measured using in vitro enzymatic assays with recombinant SIRT5 and succinylated substrates, by monitoring NAD+ consumption or byproduct formation, or by Western blotting with site-specific antibodies against succinylated proteins [2,1,3].
What diseases are associated with protein-succinyllysine desuccinylase activity?
Dysregulation is linked to acute liver injury, diabetic cardiomyopathy, cancer, sepsis, and intervertebral disc degeneration [1,3,4,5,6,7].
What is the difference between desuccinylation and demalonylation?
Both are enzymatic activities of SIRT5 that remove negatively charged acyl groups from lysine residues. Desuccinylation removes a succinyl group, while demalonylation removes a malonyl group. SIRT5 can catalyze both reactions [2,4].
Can CRISPR be used to study protein-succinyllysine desuccinylase activity?
Yes. CRISPR knockout of SIRT5 or its substrates, point mutations at catalytic or succinylation sites, knock-in of tags, and overexpression models are widely used to study this activity [1,3,5,6,7].
What are the substrates of SIRT5 desuccinylase activity?
Validated substrates include ALDH2, CPT2, GSTP1, ME2, TBK1, and AIFM1, as well as many mitochondrial metabolic enzymes identified by succinylome proteomics [1,3,4,5,6,7,8].
How does NAD+ affect protein-succinyllysine desuccinylase activity?
SIRT5 requires NAD+ as a co-substrate. Therefore, cellular NAD+ levels directly influence the rate of desuccinylation, linking this activity to metabolic state [2,8].
What model systems are best for studying protein-succinyllysine desuccinylase activity?
SIRT5 knockout mice and cell lines, substrate point-mutation knock-in models, and overexpression systems in relevant cell types (hepatocytes, cardiomyocytes, cancer cells, macrophages) are commonly used [1,3,5,6,7].
Conclusion
Protein-succinyllysine desuccinylase activity (GO:0036055) is a fundamental enzymatic function that reverses protein succinylation and regulates mitochondrial metabolism, oxidative stress, and inflammation. SIRT5 is the principal enzyme responsible for this activity, and its substrates include key metabolic and signaling proteins such as ALDH2, CPT2, ME2, TBK1, and AIFM1 [1,2,3,5,6,7]. Dysregulation of this activity contributes to acute liver injury, diabetic cardiomyopathy, cancer, sepsis, and intervertebral disc degeneration [1,3,4,5,6,7]. Researchers can leverage CRISPR-based knockout, point-mutation, knock-in, and overexpression models, combined with succinylome proteomics and enzymatic assays, to dissect the mechanisms and therapeutic potential of GO:0036055. EDITGENE provides end-to-end services to accelerate these studies.
References
- 1. Yu Q et al.. 2024. Sirtuin 5-Mediated Desuccinylation of ALDH2 Alleviates Mitochondrial Oxidative Stress Following Acetaminophen-Induced Acute Liver Injury.. Adv Sci (Weinh) 11(39):e2402710 PMID: 39159058
- 2. Du J et al.. 2011. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.. Science 334(6057):806-9 PMID: 22076378
- 3. Wu M et al.. 2024. Sirt5 improves cardiomyocytes fatty acid metabolism and ameliorates cardiac lipotoxicity in diabetic cardiomyopathy via CPT2 de-succinylation.. Redox Biol 73:103184 PMID: 38718533
- 4. Wei C et al.. 2024. SIRT5-related lysine demalonylation of GSTP1 contributes to cardiomyocyte pyroptosis suppression in diabetic cardiomyopathy.. Int J Biol Sci 20(2):585-605 PMID: 38169591
- 5. Teng P et al.. 2024. SIRT5-mediated ME2 desuccinylation promotes cancer growth by enhancing mitochondrial respiration.. Cell Death Differ 31(1):65-77 PMID: 38007551
- 6. Zhang X et al.. 2024. Desuccinylation of TBK1 by SIRT5 regulates inflammatory response of macrophages in sepsis.. Cell Rep 43(12):115060 PMID: 39673708
- 7. Mao J et al.. 2023. SIRT5-related desuccinylation modification of AIFM1 protects against compression-induced intervertebral disc degeneration by regulating mitochondrial homeostasis.. Exp Mol Med 55(1):253-268 PMID: 36653443
- 8. Rardin MJ et al.. 2013. SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks.. Cell Metab 18(6):920-33 PMID: 24315375
