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structural model of a complex of human Sirt4 and GDH (show GLUD1 Proteins) in order to elucidate the molecular mechanism underlying the ADP-ribosylation of GDH (show GLUD1 Proteins) by Sirt4
we propose that the SIRT4-OPA1 (show OPA1 Proteins) axis is causally linked to mitochondrial dysfunction and altered mitochondrial dynamics that translates into aging-associated decreased mitophagy based on an unbalanced mitochondrial fusion/fission cycle.
SIRT4 protein levels in endometrioid adenocarcinoma were markedly lower than its non-neoplastic tissue counterpart (P< 0.001).
The function of the three mitochondrial sirtuins (SIRT3 (show SIRT3 Proteins), SIRT4, SIRT5 (show SIRT5 Proteins)) and their role in disease are reviewed.
Protein levels of SIRT 4 were significantly higher in HUVECs from HELLP pregnancies compared to control after 60 and 120 minutes of hypoxia.
we found that knock-out of mitochondrial sirtuin (show SIRT1 Proteins) sir-2.3, homologous to mammalian SIRT4, is protective in both chemical ischemia and hyperactive channel induced necrosis. This work suggests a deleterious role of SIRT4 during ischemic processes in mammals that must be further investigated
This is the first study to identify an association between SIRT4 expression and decreased mitochondrial fission, which was driven by Drp1. SIRT4 inhibited Drp1 phosphorylation and weakened Drp1 recruitment to the mitochondrial membrane via an interaction with Fis-1.
miR (show MLXIP Proteins)-15b is a negative regulator of stress-induced SIRT4 expression, thereby counteracting senescence associated mitochondrial dysfunction and regulating the SASP (show ASPRV1 Proteins) and possibly organ aging, such as photoaging of human skin.
SIRT4 overexpression inhibits the proliferation of colorectal cancer cells in vitro and in vivo.
Data indicate that compared to non-neoplastic endometria (NNE), endometrial cancer (EC) showed SIRT7 (show SIRT7 Proteins) mRNA overexpression, whereas SIRT1 (show SIRT1 Proteins), SIRT2 (show SIRT2 Proteins), SIRT4 and SIRT5 (show SIRT5 Proteins) were underexpressed, and no significant differences were observed for SIRT3 (show SIRT3 Proteins) and SIRT6 (show SIRT6 Proteins).
Data suggest that high-fat diet (HFD) alters regulation of expression of sirtuins (Sirt4 and Sirt7 (show SIRT7 Proteins)) and enzymes in NAD biosynthetic pathway (Tdo2 (show TDO2 Proteins) and Nnmt (show NNMT Proteins)); these alterations are more prominent in liver as compared to white adipose tissue or skeletal muscle; Tdo2 (show TDO2 Proteins) and Nnmt (show NNMT Proteins) may serve as markers of HFD consumption. (Tdo2 (show TDO2 Proteins) = tryptophan 2,3-dioxygenase (show TDO2 Proteins); Nnmt (show NNMT Proteins) = nicotinamide N-methyltransferase (show NNMT Proteins))
These findings identify a robust enzymatic activity for SIRT4, uncover a mechanism controlling branched-chain amino acid flux, and position SIRT4 as a crucial player maintaining insulin (show INS Proteins) secretion and glucose homeostasis during aging.
miR (show MLXIP Proteins)-497 modulates cardiac hypertrophy by targeting Sirt4 and may serve as a potential therapeutic substance in the course.
Until now, a mammalian cellular lipoamidase has not been characterized; this study discovered that SIRT4 can function with this enzymatic capacity in the mitochondria, and that PDH (show PDP Proteins) is a biological substrate; compared to its catalytic efficiency for deacetylation, SIRT4 exhibits far superior enzymatic activity for lipoyl- and biotinyl-lysine modifications.
The results of this study indicated a critical and novel stress response role for SIRT4 in promoting proper glutamate (show GRIN1 Proteins) transport capacity and protecting against excitotoxicity
regulates ATP levels via ANT2 (show SLC25A5 Proteins) and a feedback loop involving AMPK (show PRKAA1 Proteins)
these results highlight the tumor-suppressive role of SIRT4 in Myc-induced B cell lymphoma and suggest that SIRT4 may be a potential target against Myc-induced and/or glutamine-dependent cancers.
The enhanced fatty acid oxidation observed in SIRT4 knockout hepatocytes requires functional SIRT1 (show SIRT1 Proteins), demonstrating a clear cross talk between mitochondrial and nuclear sirtuins.
Data uncover SIRT4 as an important component of the DNA damage response pathway that orchestrates a metabolic block in glutamine metabolism, cell cycle arrest, and tumor suppression.
SIRT4 represses fatty acid oxidation and stimulates lipogenesis. SIRT4 deacetylates and represses malonyl CoA decarboxylase, regulating malonyl coA levels.
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.
sirtuin (silent mating type information regulation 2 homolog) 4 (S. cerevisiae)
, sirtuin 4
, NAD-dependent ADP-ribosyltransferase sirtuin-4
, NAD-dependent protein deacetylase sirtuin-4
, SIR2-like protein 4
, regulatory protein SIR2 homolog 4
, sir2-like 4
, sirtuin type 4
, NAD-dependent deacetylase sirtuin-4