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    AIMP2 aminoacyl tRNA synthetase complex interacting multifunctional protein 2 [ Homo sapiens (human) ]

    Gene ID: 7965, updated on 5-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.

    Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.
    Jaramillo Ponce JR, Kapps D, Paulus C, Chicher J, Frugier M., Free PMC Article

    07/2/2022
    AIMP2-DX2 provides therapeutic interface to control KRAS-driven tumorigenesis.

    AIMP2-DX2 provides therapeutic interface to control KRAS-driven tumorigenesis.
    Kim DG, Choi Y, Lee Y, Lim S, Kong J, Song J, Roh Y, Harmalkar DS, Lee K, Goo JI, Cho HY, Mushtaq AU, Lee J, Park SH, Kim D, Min BS, Lee KY, Jeon YH, Lee S, Lee K, Kim S., Free PMC Article

    06/11/2022
    Single-cell analysis of AIMP2 splice variants informs on drug sensitivity and prognosis in hematologic cancer.

    Single-cell analysis of AIMP2 splice variants informs on drug sensitivity and prognosis in hematologic cancer.
    Ku J, Kim R, Kim D, Kim D, Song S, Lee K, Lee N, Kim M, Yoon SS, Kwon NH, Kim S, Kim Y, Koh Y., Free PMC Article

    07/3/2021
    An Isoform of the Oncogenic Splice Variant AIMP2-DX2 Detected by a Novel Monoclonal Antibody.

    An Isoform of the Oncogenic Splice Variant AIMP2-DX2 Detected by a Novel Monoclonal Antibody.
    Kim DG, Nguyen TTH, Kwon NH, Sung J, Lim S, Kang EJ, Lee J, Seo WY, Kim A, Chang YS, Shim H, Kim S., Free PMC Article

    04/13/2021
    Structural insight into the interaction between p53 TAD1 and AIMP2-DX2 by NMR.

    Structural insight into the interaction between p53 TAD1 and AIMP2-DX2 by NMR.
    Cho HY, Jha R, Mushtaq AU, Oh SH, Jeon YH.

    01/23/2021
    developed a label-free method based on the formation of split G-quadruplex in the presence of target DNA combined with strand displacement to detect exon 2 deletion of AIMP2 (DE2) sensitively and selectively

    Label-free molecular probe based on G-quadruplex and strand displacement for sensitive and selective detection and naked eye discrimination of exon 2 deletion of AIMP2.
    Zang R, Wang X, Zhu Y, Yao T, Shi S.

    05/9/2020
    heat-shock protein HSP70 is a critical determinant for the level of AIMP2-DX2

    Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development.
    Lim S, Cho HY, Kim DG, Roh Y, Son SY, Mushtaq AU, Kim M, Bhattarai D, Sivaraman A, Lee Y, Lee J, Yang WS, Kim HK, Kim MH, Lee K, Jeon YH, Kim S.

    04/25/2020
    Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex.

    Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex.
    Hei Z, Wu S, Liu Z, Wang J, Fang P., Free PMC Article

    10/19/2019
    AIMP2-DX2 plays an important role in the regulation of Nasopharyngeal carcinoma.

    AIMP2-DX2 Promotes the Proliferation, Migration, and Invasion of Nasopharyngeal Carcinoma Cells.
    Cao Q, Zhang J, Zhang T., Free PMC Article

    10/6/2018
    Homozygosity for a nonsense variant in AIMP2 is associated with a progressive neurodevelopmental disorder with microcephaly, seizures, and spastic quadriparesis.

    Homozygosity for a nonsense variant in AIMP2 is associated with a progressive neurodevelopmental disorder with microcephaly, seizures, and spastic quadriparesis.
    Shukla A, Das Bhowmik A, Hebbar M, Rajagopal KV, Girisha KM, Gupta N, Dalal A.

    07/28/2018
    These findings provide new mechanistic insights into the role of VPS35 in the regulation of AIMP2 levels and cell death.

    VPS35 regulates parkin substrate AIMP2 toxicity by facilitating lysosomal clearance of AIMP2.
    Yun SP, Kim H, Ham S, Kwon SH, Lee GH, Shin JH, Lee SH, Ko HS, Lee Y., Free PMC Article

    11/25/2017
    AIMP2 underexpression is associated with lung neoplasms.

    Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2.
    Kim DG, Lee JY, Lee JH, Cho HY, Kang BS, Jang SY, Kim MH, Guo M, Han JM, Kim SJ, Kim S.

    07/29/2017
    our findings show how DX2 promotes lung cancer progression and how its activity may be thwarted as a strategy to treat patients with lung cancers exhibiting elevated DX2 levels

    Inhibiting DX2-p14/ARF Interaction Exerts Antitumor Effects in Lung Cancer and Delays Tumor Progression.
    Oh AY, Jung YS, Kim J, Lee JH, Cho JH, Chun HY, Park S, Park H, Lim S, Ha NC, Park JS, Park CS, Song GY, Park BJ.

    07/22/2017
    These data indicate monomer-dimer equilibrium of AIMP2-DX2 in solution. These results form the basis for the structure-function study of oncogenic AIMP2-DX2.

    Purification and biophysical characterization of the AIMP2-DX2 protein.
    Jha R, Cho HY, Mushtaq AU, Lee K, Kim DG, Kim S, Jeon YH.

    07/8/2017
    analysis of 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

    Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.
    Cho HY, Maeng SJ, Cho HJ, Choi YS, Chung JM, Lee S, Kim HK, Kim JH, Eom CY, Kim YG, Guo M, Jung HS, Kang BS, Kim S., Free PMC Article

    04/23/2016
    Ubiquitin and SUMO compete for the same lysine (K242) on influenza A virus M1 and the interaction of viral NS2 with human AIMP2 facilitates the switch of the M1 modification from ubiquitination to SUMOylation, thus increasing viral replication.

    Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to SUMOylation of M1 in influenza A virus-infected cells.
    Gao S, Wu J, Liu RY, Li J, Song L, Teng Y, Sheng C, Liu D, Yao C, Chen H, Jiang W, Chen S, Huang W., Free PMC Article

    03/21/2015
    These findings suggested that, although excessive accumulation of oxidative DNA damage was present in LSCs, the relatively decreased phosphorylation of p38 might help leukemic cells escape senescence and apoptosis.

    Lower phosphorylation of p38 MAPK blocks the oxidative stress-induced senescence in myeloid leukemic CD34(+)CD38 (-) cells.
    Xiao Y, Zou P, Wang J, Song H, Zou J, Liu L.

    09/13/2014
    Transgeneic overexpression of AIMP2 led to a selective, age-dependent, progressive loss of dopaminergic neurons.

    Parthanatos mediates AIMP2-activated age-dependent dopaminergic neuronal loss.
    Lee Y, Karuppagounder SS, Shin JH, Lee YI, Ko HS, Swing D, Jiang H, Kang SU, Lee BD, Kang HC, Kim D, Tessarollo L, Dawson VL, Dawson TM., Free PMC Article

    11/30/2013
    The tumorigenic activity of AIMP2-DX2 can be controlled by the small chemical BC-DXI01, which can selectively suppress the AIMP2-DX2 mRNA transcript.

    Chemical suppression of an oncogenic splicing variant of AIMP2 induces tumour regression.
    Lee HS, Kim DG, Oh YS, Kwon NH, Lee JY, Kim D, Park SH, Song JH, Lee S, Han JM, Park BJ, Lee J, Kim S.

    11/16/2013
    AIMP2-DX2, a splicing variant of tumor suppressor AIMP2, can be a therapeutic target to control chemoresistant epithelial ovarian cancer .

    Splicing variant of AIMP2 as an effective target against chemoresistant ovarian cancer.
    Choi JW, Lee JW, Kim JK, Jeon HK, Choi JJ, Kim DG, Kim BG, Nam DH, Kim HJ, Yun SH, Kim S.

    11/17/2012
    downregulation of AIMP2 lacking exon 2 (AIMP2-DX2), expressed in different cancer cells, suppressed the epidermal growth factor receptor/mitogen activated protein kinase signaling pathway

    Lentiviral vector-mediated shRNA against AIMP2-DX2 suppresses lung cancer cell growth through blocking glucose uptake.
    Chang SH, Chung YS, Hwang SK, Kwon JT, Minai-Tehrani A, Kim S, Park SB, Kim YS, Cho MH., Free PMC Article

    10/20/2012
    ribozyme could selectively deliver the activity of a suicide gene into the AIMP2-DX2 RNA expressing lung cancer cells and thereby specifically and effectively retard the growth of the cancer cells with prodrug treatment.

    Selective regression of cancer cells expressing a splicing variant of AIMP2 through targeted RNA replacement by trans-splicing ribozyme.
    Won YS, Lee SW.

    08/4/2012
    a splicing variant of AIMP2 lacking exon 2 (AIMP2-DX2) is highly expressed by alternative splicing in human lung cancer cells and patient's tissues

    Cancer-associated splicing variant of tumor suppressor AIMP2/p38: pathological implication in tumorigenesis.
    Choi JW, Kim DG, Lee AE, Kim HR, Lee JY, Kwon NH, Shin YK, Hwang SK, Chang SH, Cho MH, Choi YL, Kim J, Oh SH, Kim B, Kim SY, Jeon HS, Park JY, Kang HP, Park BJ, Han JM, Kim S., Free PMC Article

    07/30/2011
    Observational study of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Polymorphisms in innate immunity genes and lung cancer risk in Xuanwei, China.
    Shen M, Vermeulen R, Rajaraman P, Menashe I, He X, Chapman RS, Yeager M, Thomas G, Burdett L, Hutchinson A, Yuenger J, Chanock S, Lan Q., Free PMC Article

    04/7/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (3) articles

    Genetic susceptibility to distinct bladder cancer subphenotypes.
    Guey LT, García-Closas M, Murta-Nascimento C, Lloreta J, Palencia L, Kogevinas M, Rothman N, Vellalta G, Calle ML, Marenne G, Tardón A, Carrato A, García-Closas R, Serra C, Silverman DT, Chanock S, Real FX, Malats N, EPICURO/Spanish Bladder Cancer Study investigators.

    PTEN identified as important risk factor of chronic obstructive pulmonary disease.
    Hosgood HD 3rd, Menashe I, He X, Chanock S, Lan Q.

    Pathway-based evaluation of 380 candidate genes and lung cancer susceptibility suggests the importance of the cell cycle pathway.
    Hosgood HD 3rd, Menashe I, Shen M, Yeager M, Yuenger J, Rajaraman P, He X, Chatterjee N, Caporaso NE, Zhu Y, Chanock SJ, Zheng T, Lan Q.

    09/24/2008
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