更新于：2024-11-01

AIMP2

更新于：2024-11-01

基本信息

别名

AIMP2、Aminoacyl tRNA synthase complex-interacting multifunctional protein 2、aminoacyl tRNA synthetase complex interacting multifunctional protein 2

+ [6]

简介

Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.

关联

项与 AIMP2 相关的药物

NM-DXARFI-01

靶点

AIMP2

作用机制

AIMP2基因抑制剂

在研机构

Neomics Co., Ltd.

原研机构

Neomics Co., Ltd.

在研适应症

肿瘤

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

EMAP II antibody(Allinaire Therapeutics)

靶点

AIMP2

作用机制

AIMP2 inhibitors

在研机构

Allinaire Therapeutics LLC初创企业

原研机构

Allinaire Therapeutics LLC初创企业

在研适应症

肺动脉高压

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

BC-DX101

靶点

AIMP2

作用机制

AIMP2基因抑制剂

在研机构

Excubio Pharmaceuticals, Inc.

原研机构

Excubio Pharmaceuticals, Inc.

在研适应症

肿瘤

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

100 项与 AIMP2 相关的临床结果

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100 项与 AIMP2 相关的转化医学

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0 项与 AIMP2 相关的专利（医药）

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108

项与 AIMP2 相关的文献（医药）

2024-12-01·Molecular Therapy: Oncology

The therapeutic effect of DX2 inhibition in nicotine-induced lung cancer progression

Article

作者: Kim, Bae-Hoon ; Hong, Byung-Su ; Kwon, Yonghoon ; Woo, Tae-Gyun ; Shin, Yun-Jeong ; Jeong, Jiwon ; Seo, Hyunghwan ; Oh, Ah-Young ; Park, Bum-Joon ; Kang, So-Mi ; Park, Soyoung ; Park, Hyo-Pin ; Kim, Hye-Ju ; Jang, Hyewon

Alternative splicing products of AIMP2 and AIMP2-DX2 (DX2) have been reported to be associated with human lung cancer. In fact, DX2 expression is elevated in human lung cancers, and DX2 transgenic mice also develop lung cancer, in particular small cell lung cancer (SCLC). However, the mechanism by which DX2 is induced during cancer progression has not been clearly elucidated. Here, we show that DX2 is induced by nicotine, the main component of smoking-related chemicals, which can stabilize the human epidermal growth factor receptor 2 (HER2) protein and transcriptionally increase sonic hedgehog (Shh). Indeed, nicotine showed tumorigenicity via DX2 by promoting spheroid formation and in vivo lung and kidney cancer progression. Moreover, the elimination of DX2 using small interfering RNA (siRNA) or an optimized inhibitor (SNU-14) blocked the induction of HER2 and Shh and completely suppressed tumor sphere formation in response to nicotine. These results indicate that DX2 is critical for lung cancer progression, and a specific DX2 inhibitor would be useful for the treatment of human cancers, including SCLC and non-SCLC (NSCLC).

2024-09-03·Cell chemical biology

Chemical induction of the interaction between AIMP2-DX2 and Siah1 to enhance ubiquitination.

Article

作者: Choi, Won Jun ; Lu, Qili ; Nada, Hossam ; Harmalkar, Dipesh S ; Sivaraman, Aneesh ; Song, Mo Eun ; Kim, Sunghoon ; Choi, Yongseok ; Han, Kang-Hyun ; Kim, Woojin ; Lee, Hwayoung ; Lee, Chang Hoon ; Song, Eunjoo ; Goo, Ja-Il ; Lee, Sunkyung ; Kong, Jiwon ; Kim, Pilhan ; Kim, Minkyoung ; Godesi, Sreenivasulu ; Lee, Kyeong ; Kim, Dae Gyu

AIMP2-DX2 (hereafter DX2) is an oncogenic variant of aminoacyl-tRNA synthetase-interacting multifunctional protein 2 (AIMP2) that mediates tumorigenic interactions with various factors involved in cancer. Reducing the levels of DX2 can effectively inhibit tumorigenesis. We previously reported that DX2 can be degraded through Siah1-mediated ubiquitination. In this study, we identified a compound, SDL01, which enhanced the interaction between DX2 and Siah1, thereby facilitating the ubiquitin-dependent degradation of DX2. SDL01 was found to bind to the pocket surrounding the N-terminal flexible region and GST domain of DX2, causing a conformational change that stabilized its interaction with Siah1. Our findings demonstrate that protein-protein interactions (PPIs) can be modulated through chemically induced conformational changes.

2024-08-01·Virologica Sinica

AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase

Article

作者: Ren, Pengyu ; Cai, Yumeng ; Wu, Shuwen ; Zhang, Qiuhan ; Yu, Lei ; Wang, Xueyun ; Lan, Ke ; Ren, Junrui

Hand, foot and mouth disease (HFMD), mainly caused by enterovirus 71 (EV71), has frequently occurred in the Asia-Pacific region, posing a significant threat to the health of infants and young children. Therefore, research on the infection mechanism and pathogenicity of enteroviruses is increasingly becoming important. The 3D polymerase, as the most critical RNA-dependent RNA polymerase (RdRp) for EV71 replication, is widely targeted to inhibit EV71 infection. In this study, we identified a novel host protein, AIMP2, capable of binding to 3D polymerase and inhibiting EV71 infection. Subsequent investigations revealed that AIMP2 recruits the E3 ligase SMURF2, which mediates the polyubiquitination and degradation of 3D polymerase. Furthermore, the antiviral effect of AIMP2 extended to the CVA16 and CVB1 serotypes. Our research has uncovered the dynamic regulatory function of AIMP2 during EV71 infection, revealing a novel antiviral mechanism and providing new insights for the development of antienteroviral therapeutic strategies.