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Sirtuin 4

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 IV of the sirtuin family. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Sir2, SIRT3, SIRT5, CAN, ACID
Papers on SIRT4
SIRT4 regulates cancer cell survival and growth after stress.
Seong et al., South Korea. In Biochem Biophys Res Commun, Feb 2016
Although mitochondrial SIRT4 has been shown to be involved in cellular stress response and tumor suppression, its roles in survival and drug resistance of cancer cells are not well determined.
Gestational diabetes induces alterations of sirtuins in fetal endothelial cells.
von Versen Höynck et al., Hannover, Germany. In Pediatr Res, Jan 2016
NAD+ concentration, SIRT1 and SIRT3 activity, transcription levels of SIRT1, SIRT3 and SIRT4 as well as protein levels of SIRT1, SIRT3 and SIRT4 were determined in vitro with or without sirtuin activators resveratrol and paeonol.
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.
A SIRT4-like auto ADP-ribosyltransferase is essential for the environmental growth of Mycobacterium smegmatis.
Yao et al., Shanghai, China. In Acta Biochim Biophys Sin (shanghai), Jan 2016
Here, a SIRT4 homologue MSMEG_4620 was identified and characterized in Mycobacterium smegmatis.
Loss of Mitochondrial Tumor Suppressor Genes Expression Is Associated with Unfavorable Clinical Outcome in Head and Neck Squamous Cell Carcinoma: Data from Retrospective Study.
Kayani et al., Islamabad, Pakistan. In Plos One, Dec 2015
A family of orthologues of yeast silent information regulator 3 (SIRT3), 4 (SIRT4) and mitochondrial tumor suppressor 1 (MTUS1) are important mitochondrial tumor suppressor genes which play an important role in the progression of multiple cancers.
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.
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.
SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis.
Gius et al., Chicago, United States. In Cancer Metab, 2013
In addition, these new results demonstrate that the mitochondrial anti-aging or fidelity/sensing proteins, SIRT3 and SIRT4, respond to changes in cellular nutrient status to alter the enzymatic activity of specific downstream targets to maintain energy production that matches energy availability and ATP consumption.
Oncogenes and tumor suppressors regulate glutamine metabolism in cancer cells.
Kim et al., Seoul, South Korea. In J Cancer Prev, 2013
The tumor suppressor SIRT4 inhibits glutamate dehydrogenase, which converts glutamic acid to α-ketoglutarate, an intermediate in the TCA cycle.
The mTORC1 pathway stimulates glutamine metabolism and cell proliferation by repressing SIRT4.
Blenis et al., Boston, United States. In Cell, 2013
This regulation requires transcriptional repression of SIRT4, the mitochondrial-localized sirtuin that inhibits GDH.
Sirt4: the glutamine gatekeeper.
Serrano et al., Madrid, Spain. In Cancer Cell, 2013
In this issue of Cancer Cell, Jeong and colleagues report that an important component of the DNA damage response is the SIRT4-mediated blockade of glutamine catabolism.
SIRT4 has tumor-suppressive activity and regulates the cellular metabolic response to DNA damage by inhibiting mitochondrial glutamine metabolism.
Haigis et al., Boston, United States. In Cancer Cell, 2013
This block requires the mitochondrial SIRT4, which is induced by numerous genotoxic agents and represses the metabolism of glutamine into tricarboxylic acid cycle.
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.
Lin et al., Ithaca, United States. In Science, 2011
Four of them (Sirt4 to Sirt7) have no detectable or very weak deacetylase activity.
The expression of Sirtuins 1 and 4 in peripheral blood leukocytes from patients with type 2 diabetes.
Fu et al., Shantou, China. In Eur J Histochem, 2010
there is a negative correlation between SIRTs 1 and 4 and fasting plasma glucose, a positive correlation between SIRT4 mRNA levels and triglyceride/lipoprotein a levels, and a negative correlation between SIRT4 mRNA levels and HDL
SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells.
Bordone et al., Cambridge, United States. In J Biol Chem, 2010
Data demonstrate that SIRT4 inhibition increases fat oxidative capacity in liver and mitochondrial function in muscle.
Fluorescence in situ hybridization and chromosomal organization of the sirtuin 4 gene (Sirt4) in the mouse.
Voelter-Mahlknecht et al., Homburg, Germany. In Biochem Biophys Res Commun, 2009
Fluorescence in situ hybridization analysis identified a single genomic locus for murine Sirt4 gene on chromosome 5F and is neighbored by the PLA2G1B and PXN genes.
Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD.
Lin et al., Ithaca, United States. In Biochemistry, 2009
NAD analogues and 32P-NAD were used to study the ADP-ribosyltransferase activity of several different sirtuins, including yeast Sir2, human SirT1, mouse SirT4, and mouse SirT6.
Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase.
Verdin et al., San Francisco, United States. In J Biol Chem, 2007
mitochondrial SIRT4 has a role in the regulation of insulin secretion
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