[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"detail-sidebar-cat-0-en-105":3,"doc-seo-331044-105":59,"doc-detail-331044-en":130},{"code":4,"msg":5,"data":6},0,"success",[7,13,18,23,28,33,38,43,48,51,55],{"id":8,"doc_module":4,"doc_module_name":9,"category_name":10,"show_sort_weight":11,"slug":12},1,"Document","Story & Novel",90,"story-novel",{"id":14,"doc_module":4,"doc_module_name":9,"category_name":15,"show_sort_weight":16,"slug":17},2,"Literature",80,"literature",{"id":19,"doc_module":4,"doc_module_name":9,"category_name":20,"show_sort_weight":21,"slug":22},4,"Exam",70,"exam",{"id":24,"doc_module":4,"doc_module_name":9,"category_name":25,"show_sort_weight":26,"slug":27},5,"Comic",60,"comic",{"id":29,"doc_module":4,"doc_module_name":9,"category_name":30,"show_sort_weight":31,"slug":32},6,"Technology",50,"technology",{"id":34,"doc_module":4,"doc_module_name":9,"category_name":35,"show_sort_weight":36,"slug":37},7,"Healthcare",40,"healthcare",{"id":39,"doc_module":4,"doc_module_name":9,"category_name":40,"show_sort_weight":41,"slug":42},8,"Research & Report",30,"research-report",{"id":44,"doc_module":4,"doc_module_name":9,"category_name":45,"show_sort_weight":46,"slug":47},9,"Religion & Spirituality",20,"religion-spirituality",{"id":46,"doc_module":4,"doc_module_name":9,"category_name":49,"show_sort_weight":46,"slug":50},"World Cup","world-cup",{"id":52,"doc_module":4,"doc_module_name":9,"category_name":53,"show_sort_weight":52,"slug":54},10,"Lifestyle","lifestyle",{"id":56,"doc_module":4,"doc_module_name":9,"category_name":57,"show_sort_weight":24,"slug":58},19,"General","general",{"code":4,"msg":60,"data":61},"ok",{"site_id":62,"language":63,"slug":64,"title":65,"keywords":66,"description":67,"schema_data":68,"social_meta":123,"head_meta":125,"extra_data":127,"updated_unix":129},105,"en","identification-and-structure-of-aimp2-dx2-for-therapeutic-perspectives","Identification and structure of AIMP2-DX2 for therapeutic perspectives","","Regulation of cell fate and lung cell differentiation is linked to the aminoacyl-tRNA synthetases-interacting multifunctional protein 2 (AIMP2), a non-enzymatic component of the multi-tRNA synthetase complex. Following DNA damage, AIMP2 dissociates, binds p53, blocks MDM2-mediated degradation, and promotes apoptosis. Alternative splicing produces AIMP2-DX2, which lacks exon 2 and competitively binds FBP, TRAF2, and p53, weakening AIMP2’s tumor-suppressive activity. AIMP2-DX2 is reported to be overexpressed across multiple cancers and is increasingly investigated as a biomarker and therapeutic inhibition target.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":40,"@type":76,"position":81},"https://docshare.wps.com/document/research-report/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/identification-and-structure-of-aimp2-dx2-for-therapeutic-perspectives/331044/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/identification-and-structure-of-aimp2-dx2-for-therapeutic-perspectives/331044.png","ImageObject",300,407,{"name":92,"@type":93},"Liam","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-11-05","2026-09-21",true,{"@type":102,"interactionType":103,"userInteractionCount":29},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What is AIMP2’s role in cell fate and apoptosis after DNA damage?","Question",{"text":112,"@type":113},"AIMP2 separates from the multi-tRNA synthetase complex, binds p53, and prevents its degradation by MDM2, thereby inducing apoptosis.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"How does AIMP2-DX2 differ from AIMP2 and what is its key functional impact?",{"text":117,"@type":113},"AIMP2-DX2 is an alternative splicing variant lacking exon 2; it binds target proteins (FBP, TRAF2, p53) competitively, impairing AIMP2’s tumor-suppressive activity.",{"name":119,"@type":110,"acceptedAnswer":120},"Why is AIMP2-DX2 considered a promising biomarker or therapeutic target?",{"text":121,"@type":113},"AIMP2-DX2 is specifically expressed in diverse cancer cells and is associated with cancer aggressiveness, making inhibition a potential therapeutic strategy.","https://schema.org",{"og:url":83,"og:type":124,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":126,"canonical":83},"index,follow",{"doc_id":128,"site_id":62},331044,1790185326,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":133,"doc_module":4,"category_id":39,"category_name":40,"doc_title":65,"doc_description":67,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":29,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":29,"language":139,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":140,"faqs":141,"seo_title":142,"seo_description":67,"update_tm":143,"read_time":144,"preview_page_count":4},8796095461564,"https://ap-avatar.wpscdn.com/davatar_155a257f0dc6eb9ab79c44ca47cae57d","BMB Reports  \nBMB Rep. 2024; 57(7): 318-323  \n[www.bmbreports.org](www.bmbreports.org)  \nContributed Mini Review  \nIdentification and structure of AIMP2-DX2 for therapeutic perspectives  \nHyeon Jin Kim1, Mi Suk Jeong1 & Se Bok Jang1,2, *  \n1Insitute of Systems Biology, Pusan National University, Busan 46241, 2Department of Molecular Biology, College of Natural Sciences, Pusan National University, Busan 46241, Korea  \nRegulation of cell fate and lung cell differentiation is associated with Aminoacyl-tRNA synthetases (ARS)-interacting multifunctional protein 2 (AIMP2), which acts as a non-enzymatic component required for the multi-tRNA synthetase complex. In response to DNA damage, a component of AIMP2 separates from the multi-tRNA synthetase complex, binds to p53, and preventsits degradation by MDM2, inducing apoptosis. Additionally, AIMP2 reduces proliferation in TGF-􀁅 and Wnt pathways, while enhancing apoptotic signaling induced by tumor necrosis factor-􀁄. Given the crucial role of these pathways in tumorigenesis, AIMP2 is expected to function as a broad-spectrum tumor suppressor. The full-length AIMP2 transcript consists of four exons, with a small section of the pre-mRNA undergoing alternative splicing to produce a variant (AIMP2-DX2) lacking the second exon. AIMP2-DX2 binds to FBP, TRAF2, and p53 similarly to AIMP2, but competes with AIMP2 for binding to these target proteins, thereby impairing its tumor-suppressive activity. AIMP2-DX2 is specifically expressed in a diverse range of cancer cells, including breast cancer, liver cancer, bone cancer, and stomach cancer. There is growing interest in AIMP2-DX2 as a promising biomarker for prognosis and diagnosis, with AIMP2-DX2 inhibition attracting significant interest as a potentially effective therapeutic approach for the treatment of lung, ovarian, prostate, and nasopharyngeal cancers. [BMB Reports 2024; 57(7): 318-323]  \nINTRODUCTION  \nMulti-tRNA synthetase complex (MSC), a macromolecular protein complex, is composed of minoacyl-transfer RNA synthetase-interacting multifunctional protein 2 (AIMP2) (1) . When AIMP2 separates from the MSC, it affects the p53, TGF-􀁅, TNF-􀁄,  \n*Corresponding author. Tel: +82-51-510-2523; Fax: +82-51-581-2545; E-mail: [sbjang@pusan.ac.kr](sbjang@pusan.ac.kr)  \n[https://doi.org/10.5483/BMBRep.2024-0053](https://doi.org/10.5483/BMBRep.2024-0053)  \nReceived 10 April 2024, Revised 30 April 2024, Accepted 7 May 2024, Published online 26 June 2024  \nKeywords: AIMP2, AIMP2-DX2, Drug, Inhibitor, Oncogene  \nand WNT signaling pathways, each of which functions to prevent tumorigenesis (2-4) . AIMP2-DX2, an alternative splicing variant of AIMP2 generated by pre-mRNA splicing that eliminates exon 2, correlates positively with the aggressiveness of certain cancers. AIMP2-DX2 interacts competitively with p53, FBP, and TRAF2 to reduce the tumor-suppressive activity of native AIMP2 (5) . AIMP2-DX2 is a tumorigenic factor that is frequently upregulated in a variety of cancers. AIMP2-DX2 is highly expressed in the tissues of colon, lung, and pancreatic cancers (6) . Despite its significance as a therapeutic target against cancer, the structure and mechanism of AIMP2-DX2 are not yet known. Here, we elucidate structural insight into AIMP2-DX2 as a potential target for cancer.  \nAIMPs  \nAminoacyl-tRNA synthetases (ARSs) are essential enzymes that join amino acids to tRNAs in the initial step of protein translation. In mammal, eight different ARSs form a complex with three proteins: glutamyl-prolyl-tRNA synthetase (EPRS), isoleucyltRNA synthetase (IRS), leucyl-tRNA synthetase (LRS), glutaminyltRNA synthetase (QRS), lysyl-tRNA synthetase (KRS), arginyltRNA synthetase (RRS), aspartyl-tRNA synthetase (DRS), and methionyl-tRNA synthetase (MRS), along with AIMP1/p43, AIMP2/ p38, and AIMP3/p18 (7) .  \nAIMP1, comprising 312 amino acids, binds in particular to RRS in the MRS. It is secreted upon hypoxia or cytokine stimulation, and acts as a cytokine on diverse target cells,","cbCaik4Q5kt7x7DP","https://ap.wps.com/l/cbCaik4Q5kt7x7DP","pdf",2361193,"English","# Introduction\n## AIMPs","[{\"question\":\"What is AIMP2’s role in cell fate and apoptosis after DNA damage?\",\"answer\":\"AIMP2 separates from the multi-tRNA synthetase complex, binds p53, and prevents its degradation by MDM2, thereby inducing apoptosis.\"},{\"question\":\"How does AIMP2-DX2 differ from AIMP2 and what is its key functional impact?\",\"answer\":\"AIMP2-DX2 is an alternative splicing variant lacking exon 2; it binds target proteins (FBP, TRAF2, p53) competitively, impairing AIMP2’s tumor-suppressive activity.\"},{\"question\":\"Why is AIMP2-DX2 considered a promising biomarker or therapeutic target?\",\"answer\":\"AIMP2-DX2 is specifically expressed in diverse cancer cells and is associated with cancer aggressiveness, making inhibition a potential therapeutic strategy.\"}]","Identification and structure of AIMP2-DX2 for therapeutic perspectives | PDF",1789991334,15]