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This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

 
Identification and structure of AIMP2-DX2 for therapeutic perspectives
Hyeon Jin Kim1 (Post-Doc.), Mi Suk Jeong1 (researcher), Se Bok Jang1,* (Professor)
1Department of Molecular Biology and 2Insitute of Systems Biology, Pusan National University
Abstract
The multi-tRNA synthetase complex (MSC), a macromolecular protein complex, is composed of minoacyl-transfer RNA synthetase-interacting multifunctional protein 2 (AIMP2). When AIMP2 separates from the MSC, it affects the p53, TGF-モ, TNF-メ, and WNT signaling pathways, which each function to prevent tumorigenesis. AIMP2-DX2, an alternative splicing variant of AIMP2 that eliminates exon 2, has a positive correlation with the aggressiveness of cancer. AIMP2-DX2 interacts competitively with p53, FBP, and TRAF2 to reduce the tumor-suppressive activity of native AIMP2. AIMP2-DX2 is a tumorigenic factor that is frequently upregulated in a variety of cancers. AIMP2-DX2 is highly expressed in colon, lung, and pancreatic cancer tissues, implying that AIMP2-DX2 is a potential target for cancer control.
Abstract, Accepted Manuscript [Submitted on April 10, 2024, Accepted on May 7, 2024]
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