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Nicotinamide nucleotide adenylyltransferase 2

This gene product belongs to the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze an essential step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; this enzyme is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Nicotinamide-Nucleotide Adenylyltransferase, Nmnat3, CAN, SARM, visfatin
Papers on NMNAT2
Decreased SMG7 expression associates with lupus-risk variants and elevated antinuclear antibody production.
Tsao et al., Los Angeles, United States. In Ann Rheum Dis, Feb 2016
OBJECTIVES: Following up the systemic lupus erythematosus (SLE) genome-wide association studies (GWAS) identification of NMNAT2 at rs2022013, we fine-mapped its 150 kb flanking regions containing NMNAT2 and SMG7 in a 15 292 case-control multi-ancestry population and tested functions of identified variants.
Obesity Is Associated With Low NAD(+)/SIRT Pathway Expression in Adipose Tissue of BMI-Discordant Monozygotic Twins.
Pietiläinen et al., Düsseldorf, Germany. In J Clin Endocrinol Metab, Jan 2016
RESULTS: SIRT1, SIRT3, SIRT5, NAMPT, NMNAT2, NMNAT3, and NRK1 expressions were significantly down-regulated and the activity of main cellular NAD(+) consumers, PARPs, trended to be higher in the SAT of heavier co-twins of body mass index-discordant pairs.
Wallerian Degeneration Is Executed by an NMN-SARM1-Dependent Late Ca(2+) Influx but Only Modestly Influenced by Mitochondria.
Conforti et al., Nottingham, United Kingdom. In Cell Rep, Jan 2016
Axon injury leads to rapid depletion of NAD-biosynthetic enzyme NMNAT2 and high levels of its substrate, NMN.
A rise in NAD precursor nicotinamide mononucleotide (NMN) after injury promotes axon degeneration.
Conforti et al., Ancona, Italy. In Cell Death Differ, May 2015
Axons depend on the activity of the central enzyme in NAD biosynthesis, nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2), for their maintenance and degenerate rapidly when this activity is lost.
Absence of SARM1 rescues development and survival of NMNAT2-deficient axons.
Coleman et al., Ancona, Italy. In Cell Rep, May 2015
SARM1 function and nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) loss both promote axon degeneration, but their relative relationship in the process is unknown.
Identification of palmitoyltransferase and thioesterase enzymes that control the subcellular localization of axon survival factor nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2).
Coleman et al., Cambridge, United Kingdom. In J Biol Chem, 2014
The NAD-synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is a critical survival factor for axons and its constant supply from neuronal cell bodies into axons is required for axon survival in primary culture neurites and axon extension in vivo.
Wallerian degeneration: an emerging axon death pathway linking injury and disease.
Coleman et al., Nottingham, United Kingdom. In Nat Rev Neurosci, 2014
Nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is essential for axon growth and survival.
The NAD+ synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT-2) is a p53 downstream target.
Lee et al., Halifax, Canada. In Cell Cycle, 2013
Our search resulted in the identification of nicotinamide mononucleotide adenylyltransferase 2 (NMNAT-2), a NAD(+) synthetase, as a novel downstream target gene of p53.
SIRT3 regulates cell proliferation and apoptosis related to energy metabolism in non-small cell lung cancer cells through deacetylation of NMNAT2.
Xia et al., Beijing, China. In Int J Oncol, 2013
One of the positive clones encoded the full-length cDNA of the nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) gene and the interaction between SIRT3 and NMNAT2 was identified.
Axonal trafficking of NMNAT2 and its roles in axon growth and survival in vivo.
Coleman et al., Cambridge, United Kingdom. In Bioarchitecture, 2013
The NAD-synthesizing enzyme NMNAT2 is critical for axon survival in primary culture and its depletion may contribute to axon degeneration in a variety of neurodegenerative disorders.
Rescue of peripheral and CNS axon defects in mice lacking NMNAT2.
Coleman et al., Cambridge, United Kingdom. In J Neurosci, 2013
NMNAT2 is an NAD(+)-synthesizing enzyme with an essential axon maintenance role in primary culture neurons.
Nicotinamide mononucleotide adenylyltransferase2 overexpression enhances colorectal cancer cell-kill by Tiazofurin.
Jayaram et al., Indianapolis, United States. In Cancer Gene Ther, 2013
Colorectal cancer cells exhibit limited cytotoxicity towards Tiazofurin, a pro-drug metabolized by cytosolic nicotinamide mononucleotide adenylyltransferase2 (NMNAT2) to thiazole-4-carboxamide adenine dinucleotide, a potent inhibitor of inosine 5'-monophosphate dehydrogenase required for cellular guanylate synthesis.
The Phr1 ubiquitin ligase promotes injury-induced axon self-destruction.
DiAntonio et al., Saint Louis, United States. In Cell Rep, 2013
Phr1 depletion increases the axonal level of the axon survival molecule nicotinamide mononucleotide adenyltransferase 2 (NMNAT2), and NMNAT2 is necessary for Phr1-dependent axon stability.
MEK inhibitor U0126 reverses protection of axons from Wallerian degeneration independently of MEK-ERK signaling.
Gilley et al., Cambridge, United Kingdom. In Plos One, 2012
Proteasome inhibition also delays Wallerian degeneration, although much less robustly, with stabilization of NMNAT2 likely to play a key role in this mechanism.
CREB-activity and nmnat2 transcription are down-regulated prior to neurodegeneration, while NMNAT2 over-expression is neuroprotective, in a mouse model of human tauopathy.
Lu et al., Houston, United States. In Hum Mol Genet, 2012
Decreased endogenous NMNAT2 function caused by reduced CREB signaling during pathological insults may be one of underlying mechanisms for neuronal death in tauopathies
Expression, localization, and biochemical characterization of nicotinamide mononucleotide adenylyltransferase 2.
Yu et al., Dallas, United States. In J Biol Chem, 2011
Nmnat2 is a neuronal protein peripherally attached to membranes via palmitoylation and suggest that Nmnat2 is transported to synaptic terminals via an endosomal pathway.
NMNAT expression and its relation to NAD metabolism.
Yalowitz et al., Indianapolis, United States. In Curr Med Chem, 2010
Based on their localization, three different NMNAT's have been recognized, NMNAT-1 (homohexamer) in the nucleus (chromosome 1 p32-35), NMNAT-2 (homodimer) in the cytoplasm (chromosome 1q25) and NMNAT-3 (homotetramer) in the mitochondria.
Overexpression of Wld(S) or Nmnat2 in mauthner cells by single-cell electroporation delays axon degeneration in live zebrafish.
Zhai et al., Shanghai, China. In J Neurosci Res, 2010
that overexpression of Nmnat2 in M-cells significantly delayed axon degeneration in vivo
Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases.
Ziegler et al., Bergen, Norway. In J Biol Chem, 2010
analysis of isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases
Nmnat2 delays axon degeneration in superior cervical ganglia dependent on its NAD synthesis activity.
Zhai et al., Shanghai, China. In Neurochem Int, 2010
The brain-specific Nmnat2 delays injury-induced axon degeneration dependent on its NAD synthesis activity. These findings provide new clues to further study the molecular mechanisms of axon degeneration and the related neurodegenerative diseases.
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