Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs) are auxiliary factors involved in protein synthesis related to aminoacyl-tRNA synthetases (ARSs). AIMPs, which are well known as nonenzymatic factors, include AIMP1/p43, AIMP2/p38, and AIMP3/p18. The canonical functions of AIMPs include not only protein synthesis via multisynthetase complexes but also maintenance of the structural stability of these complexes. Several recent studies have demonstrated nontypical (noncanonical) functions of AIMPs, such as roles in apoptosis, inflammatory processes, DNA repair, and so on. However, these noncanonical functions of AIMPs have not been studied in peripheral nerves related to motor and sensory functions. Peripheral nerves include two types of structures: peripheral axons and Schwann cells. The myelin sheath formed by Schwann cells produces saltatory conduction, and these rapid electrical signals control motor and sensory functioning in the service of survival in mammals. Schwann cells play roles not only in myelin sheath formation but also as modulators of nerve degeneration and regeneration. Therefore, it is important to identify the main functions of Schwann cells in peripheral nerves. Here, using immunofluorescence technique, we demonstrated that AIMPs are essential morphological indicators of peripheral nerve degeneration, and their actions are limited to peripheral nerves and not the dorsal root ganglion and the ventral horn of the spinal cord.
Keywords: Schwann cells; Wallerian degeneration; aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs); fluorescence-based analysis; noncanonical functions.
Conflict of interest statement
The authors declare no conflicts of interest.
Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): a triad for cellular homeostasis.IUBMB Life. 2010 Apr;62(4):296-302. doi: 10.1002/iub.324. IUBMB Life. 2010. PMID: 20306515 Review.
Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein.Acta Crystallogr D Struct Biol. 2020 Feb 1;76(Pt 2):135-146. doi: 10.1107/S2059798319016413. Epub 2020 Jan 30. Acta Crystallogr D Struct Biol. 2020. PMID: 32038044
Expression of AIMP1, 2 and 3, the scaffolds for the multi-tRNA synthetase complex, is downregulated in gastric and colorectal cancer.Tumori. 2011 May-Jun;97(3):380-5. doi: 10.1700/912.10038. Tumori. 2011. PMID: 21789020
Symmetric Assembly of a Decameric Subcomplex in Human Multi-tRNA Synthetase Complex Via Interactions between Glutathione Transferase-Homology Domains and Aspartyl-tRNA Synthetase.J Mol Biol. 2019 Nov 8;431(22):4475-4496. doi: 10.1016/j.jmb.2019.08.013. Epub 2019 Aug 29. J Mol Biol. 2019. PMID: 31473157
Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers.Trends Biochem Sci. 2005 Oct;30(10):569-74. doi: 10.1016/j.tibs.2005.08.004. Trends Biochem Sci. 2005. PMID: 16125937 Review.
- Kim J.Y., Kang Y.S., Lee J.W., Kim H.J., Ahn Y.H., Park H., Ko Y.G., Kim S. p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: Implications for its physiological significance. Proc. Natl. Acad. Sci. 2002;99:7912–7916. doi: 10.1073/pnas.122110199. - DOI - PMC - PubMed
- 2018R1A2B6001123/the National Research Foundation of Korea (NRF) grant
- 2015R1C1A1A02036863/the National Research Foundation of Korea (NRF) grant
- 2018R1D1A1B07040282/the National Research Foundation of Korea (NRF) grant
- 2015R1A2A2A01002735/the National Research Foundation of Korea (NRF) grant
- 2018R1C1B5029745/the National Research Foundation of Korea (NRF) grant