Aminoacyl-tRNA synthetase–interacting multifunctional proteins (AIMPs): A triad for cellular homeostasis

✍ Scribed by Sang Gyu Park; Eung-Chil Choi; Sunghoon Kim

• Book ID: 102281786
• Publisher: John Wiley and Sons
• Year: 2010
• Tongue: English
• Weight: 405 KB
• Volume: 62
• Category: Article
• ISSN: 1521-6543
• DOI: 10.1002/iub.324

✦ Synopsis

Abstract

Aminoacyl‐tRNA synthetases (ARSs) are highly conserved for efficient and precise translation of genetic codes. 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). Although the structure and functional implications for this complex formation are not completely understood, rapidly accumulating evidences suggest that this complex would work as a molecular hub linked to the multiple signaling pathways that involve the components of enzymes and cofactors. In this article, the roles of three nonenzymatic components of the multi‐tRNA synthetase complex in the assembly of the components and in cell regulation are addressed. © 2010 IUBMB IUBMB Life, 62(4): 296–302, 2010