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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 2

AIMP2, JTV-1
Top mentioned proteins: p38, V1a, CAN, Ubiquitin, Msc
Papers on AIMP2
Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.
New
Kim et al., Taegu, South Korea. In J Biol Chem, Jan 2016
Here we show the heterotetrameric complex structure of the glutathione transferase (GST) domains shared among the four MSC components, methionyl-tRNA synthetase (MRS), glutaminyl-prolyl-tRNA synthetase (EPRS), AIMP2 and AIMP3.
Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to SUMOylation of M1 in influenza A virus-infected cells.
Huang et al., Beijing, China. In J Virol, 2015
In this study, we searched for novel binding partners of the influenza A virus NS2 protein, the nuclear export protein responsible for overcoming host range restriction, by a yeast two-hybrid screening assay and glutathione S-transferase-pulldown and coimmunoprecipitation assays and identified AIMP2, a potent tumor suppressor that usually functions to regulate protein stability, as one of the major NS2-binding candidates.
Evaluation of Multi-tRNA Synthetase Complex by Multiple Reaction Monitoring Mass Spectrometry Coupled with Size Exclusion Chromatography.
Lee et al., Seoul, South Korea. In Plos One, 2014
TARSL2 and AIMP2-DX2, despite their low abundance, were co-purified with KARS and detected in the SEC fractions, where MSC appeared.
Case of 7p22.1 Microduplication Detected by Whole Genome Microarray (REVEAL) in Workup of Child Diagnosed with Autism.
Stratton et al., Corpus Christi, United States. In Case Rep Genet, 2014
This interval included 14 OMIM annotated genes (FBXL18, ACTB, FSCN1, RNF216, OCM, EIF2AK1, AIMP2, PMS2, CYTH3, RAC1, DAGLB, KDELR2, GRID2IP, and ZNF12).
Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.
Cho et al., South Korea. In Proc Natl Acad Sci U S A, 2014
This ternary complex was further anchored to AIMP2/p38 through interaction with AIMP1.
Parkin plays a role in sporadic Parkinson's disease.
Review
Dawson et al., Baltimore, United States. In Neurodegener Dis, 2013
RESULTS: Parkin is inactivated in sporadic PD via S-nitrosylation, oxidative and dopaminergic stress, and phosphorylation by the stress-activated kinase c-Abl, leading to the accumulation of AIMP2 and PARIS (ZNF746).
Architecture and metamorphosis.
Review
Yang et al., Jupiter, United States. In Top Curr Chem, 2013
The human MSC consists of nine aaRSs (LysRS, ArgRS, GlnRS, AspRS, MetRS, IleRS, LeuRS, GluProRS, and bifunctional aaRs) and three scaffold proteins (AIMP1/p43, AIMP2/p38, and AIMP3/p18), and has a molecular weight of 1.5 million Dalton.
Protein-protein interactions and multi-component complexes of aminoacyl-tRNA synthetases.
Review
Kim et al., Seoul, South Korea. In Top Curr Chem, 2013
The mammalian multi-tRNA synthetase complex (MSC) consists of eight different enzymes: EPRS, IRS, LRS, QRS, MRS, KRS, RRS, and DRS, and three auxiliary proteins: AIMP1/p43, AIMP2/p38, and AIMP/p18.
The c-Abl inhibitor, nilotinib, protects dopaminergic neurons in a preclinical animal model of Parkinson's disease.
Ko et al., Baltimore, United States. In Sci Rep, 2013
On the other hand, we observe no reduction in the tyrosine phosphorylation of parkin and the parkin substrate, AIMP2 suggesting that the protective effect of nilotinib may, in part, be parkin-independent or to the pharmacodynamics properties of nilotinib.
Parthanatos mediates AIMP2-activated age-dependent dopaminergic neuronal loss.
Dawson et al., Baltimore, United States. In Nat Neurosci, 2013
We found that transgenic overexpression of a parkin substrate, aminoacyl-tRNA synthetase complex interacting multifunctional protein-2 (AIMP2), led to a selective, age-dependent, progressive loss of dopaminergic neurons via activation of poly(ADP-ribose) polymerase-1 (PARP1).
Chemical suppression of an oncogenic splicing variant of AIMP2 induces tumour regression.
Kim et al., Seoul, South Korea. In Biochem J, 2013
AIMP2 (aminoacyl-tRNA synthetase-interacting multifunctional protein 2) is a potent tumour suppressor that induces apoptosis in response to various oncogenic signals.
Far upstream element binding protein 1: a commander of transcription, translation and beyond.
Review
Chen et al., Tucson, United States. In Oncogene, 2013
The interaction of FBP1 with p38/JTV-1 results in FBP1 ubiquitination and degradation by the proteasomes.
Neuroprotective efficacy of a new brain-penetrating C-Abl inhibitor in a murine Parkinson's disease model.
Ali et al., United States. In Plos One, 2012
This treatment regimen also abrogated activation of c-Abl, tyrosine phosphorylation of the Abl substrate and E3-ubiquitin ligase parkin, and accumulation of the toxic parkin substrate AIMP2.
Reinvestigation of aminoacyl-tRNA synthetase core complex by affinity purification-mass spectrometry reveals TARSL2 as a potential member of the complex.
Lee et al., Seoul, South Korea. In Plos One, 2012
In order to understand the complex interaction within MSC, we conducted affinity purification-mass spectrometry (AP-MS) using each of AIMP1, AIMP2 and KARS as a bait protein.
Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): a triad for cellular homeostasis.
Review
Kim et al., Seoul, South Korea. In Iubmb Life, 2010
In higher eukaryotic systems, several different ARSs including glutamyl-prolyl-, isoelucyl-, leucyl-, methionyl-, glutaminyl-, lysyl-, arginyl-, and aspartyl-tRNA synthetase form a macromolecular protein complex with three nonenzymatic cofactors (AIMP1/p43, AIMP2/p38, and AIMP3/p18).
Multidirectional tumor-suppressive activity of AIMP2/p38 and the enhanced susceptibility of AIMP2 heterozygous mice to carcinogenesis.
GeneRIF
Kim et al., Seoul, South Korea. In Carcinogenesis, 2009
functional significance of AIMP2 in determination of cell proliferation and death, and as a haploinsufficient tumor suppressor.
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