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Sirtuin 5

SIRT5, Sirtuin 5, NAD-dependent deacetylase sirtuin 5
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: SIRT3, Sir2, SIRT4, SIRT6, CAN
Papers on SIRT5
Deposition of 5-Methylcytosine on Enhancer RNAs Enables the Coactivator Function of PGC-1α.
Walsh et al., New York City, United States. In Cell Rep, Feb 2016
Consistently, loss of Set7/9 and NSun7 in liver cell model systems resulted in depletion of the PGC-1α target genes Pfkl, Sirt5, Idh3b, and Hmox2, which was accompanied by a decrease in the eRNAs levels associated with these loci.
Identification of sirtuin 5 inhibitors by ultrafast microchip electrophoresis using nanoliter volume samples.
Kennedy et al., Ann Arbor, United States. In Anal Bioanal Chem, Jan 2016
Sirtuin 5 (SIRT5) is a member of the sirtuin family of protein deacylases that catalyzes removal of post-translational modifications, such as succinyl and malonyl moieties, on lysine residues.
Assessing sirtuin expression in endometrial carcinoma and non-neoplastic endometrium.
Jerónimo et al., Porto, Portugal. In Oncotarget, Jan 2016
Compared to NNE, ECs showed SIRT7 (p < 0.001) mRNA overexpression, whereas SIRT1 (p < 0.001), SIRT2 (p < 0.001), SIRT4 (p < 0.001) and SIRT5 (p < 0.001) were underexpressed.
The expression levels of the sirtuins in patients with BCC.
Göğebakan et al., Antioch, Turkey. In Tumour Biol, Jan 2016
Sirt2, Sirt3, Sirt4, Sirt5, Sirt6, and Sirt7) were examined by real-time PCR.
The orphan estrogen-related receptor alpha and metabolic regulation: new frontiers.
Ranhotra, Shillong, India. In J Recept Signal Transduct Res, Dec 2015
Data show that ERRα exerts its metabolic control by regulating the expression of SIRT5 that influences oxygen consumption and ATP generation.
The role of sirtuins in cardiac disease.
Sadoshima et al., Newark, United States. In Am J Physiol Heart Circ Physiol, Nov 2015
On the other hand, the roles of Sirt4 and Sirt5 in the heart remain largely uncharacterized.
Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation.
Zhao et al., Chicago, United States. In Mol Cell Proteomics, Sep 2015
The deacylase sirtuin 5 (SIRT5) catalyzes the removal of these modifications from a wide range of proteins in different subcellular compartments.
Mitochondrial sirtuins and their relationships with metabolic disease and cancer.
Lombard et al., Ann Arbor, United States. In Antioxid Redox Signal, May 2015
Mitochondrial sirtuins (SIRT3, SIRT4, and SIRT5) play pivotal roles in promoting this homeostasis by regulating numerous aspects of mitochondrial metabolism in response to environmental stressors.
Mitochondrial sirtuins: emerging roles in metabolic regulations, energy homeostasis and diseases.
Parihar et al., Ujjain, India. In Exp Gerontol, 2015
Mitochondria inhabit three main types of sirtuins classified as Sirt3, Sirt4 and Sirt5.
Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity.
Cristea et al., Princeton, United States. In Cell, 2015
Despite conserved deacetylase domains, mitochondrial SIRT4 and SIRT5 have little to no deacetylase activity, and a robust catalytic activity for SIRT4 has been elusive.
SUN2 exerts tumor suppressor functions by suppressing the Warburg effect in lung cancer.
Sang et al., Nanchang, China. In Sci Rep, 2014
Finally, our results provided evidence that SIRT5 acts, at least partly, as a negative regulator of SUN2.Taken together, our findings indicate that SUN2 is a key component in lung cancer progression by inhibiting the Warburg effect and that the novel SIRT5/SUN2 axis may prove to be useful for the development of new strategies for treating the patients with lung cancer.
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5.
Zhao et al., Shanghai, China. In Cell Metab, 2014
We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase.
SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks.
Verdin et al., Novato, United States. In Cell Metab, 2014
Here, we use a label-free quantitative proteomic approach to characterize the lysine succinylome in liver mitochondria and its regulation by the desuccinylase SIRT5.
The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5).
Hao et al., Ithaca, United States. In J Biol Chem, 2012
The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5).
Resveratrol stimulates cortisol biosynthesis by activating SIRT-dependent deacetylation of P450scc.
Sewer et al., San Diego, United States. In Endocrinology, 2012
NAD(+)-dependent SIRT deacetylase has a role in regulating the expression of mitochondrial steroidogenic P450
Old enzymes, new tricks: sirtuins are NAD(+)-dependent de-acylases.
Hirschey, Durham, United States. In Cell Metab, 2012
Two new studies by Du et al. (2011) and Peng et al. (2011) identify a new enzymatic activity for SIRT5, expanding the cellular repertoire of posttranslational modifications targeted by the sirtuins.
SIRT1 and SIRT5 activity expression and behavioral responses to calorie restriction.
Fu et al., Shantou, China. In J Cell Biochem, 2011
Caloric restriction (CR) retarded declines in cognitive ability and enhanced the expression of both SIRT1 and SIRT5 proteins in the cerebral tissue of CR rats compared with AL rats
The first identification of lysine malonylation substrates and its regulatory enzyme.
Zhao et al., Chicago, United States. In Mol Cell Proteomics, 2011
we demonstrate that Sirt5, a member of the class III lysine deacetylases, can catalyze lysine demalonylation and lysine desuccinylation reactions both in vitro and in vivo
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.
Lin et al., Ithaca, United States. In Science, 2011
study found that Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro; protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo
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