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

Sang Gyu Park, Eung Chil Choi, Sunghoon Kim

Research output: Contribution to journalReview articlepeer-review

70 Citations (Scopus)


Aminoacyl-tRNA synthetases (ARSs) are highly conserved for efficient and precise translation of genetic codes. In higher eukaryotic systems, several different ARSs including glutamylprolyl-, 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.

Original languageEnglish
Pages (from-to)296-302
Number of pages7
JournalIUBMB Life
Issue number4
Publication statusPublished - 2010

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology


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