Amino Acids

, Volume 44, Issue 4, pp 1241–1245 | Cite as

Contributions of aminoacyl-tRNA synthetase-interacting multifunctional protein-3 to mammalian translation initiation

  • Min Jeong Ku
  • Sang Yeol Lee
Short Communication


Aminoacyl-tRNA synthetase-interacting multifunctional protein-3 (AIMP3) stabilizes and protects mammalian methionyl-tRNA synthetase (MRS) and eukaryotic initiation factor 2 subunit gamma (eIF2γ), factors involved in the formation and the delivery of Met-tRNA i Met respectively, through the binding interactions. Due to the protections that MRS and eIF2γ are provided from the interactions with AIMP3, cellular levels of MRS and eIF2γ may be able to be maintained high enough for their canonical and/or non-canonical functions.


Aminoacyl-tRNA synthetase-interacting multifunctional protein-3 (AIMP3) Methionyl-tRNA synthetase (MRS) Eukaryotic initiation factor 2 subunit gamma (eIF2γ) Protein–protein interaction Translation initiation 



This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology of Korea (2010-0023292).


  1. Han JM, Lee MJ, Park SG, Lee SH, Razin E, Choi EC, Kim S (2006) Hierarchical network between the components of the multi-tRNA synthetase complex: implications for complex formation. J Biol Chem 281(50):38663–38667PubMedCrossRefGoogle Scholar
  2. He R, Zu LD, Yao P, Chen X, Wang ED (2009) Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multi-synthetase complex incorporation and enzyme activity. Biochim Biophys Acta 1794(2):347–354PubMedCrossRefGoogle Scholar
  3. Kang T, Kwon NH, Lee JY, Park MC, Kang E, Kim HH, Kang TJ, Kim S (2012) AIMP3/p18 controls translational initiation by mediating the delivery of charged initiator tRNA to initiation complex. J Mol Biol 423(4):475–481PubMedCrossRefGoogle Scholar
  4. Kim KJ, Park MC, Choi SJ, Oh YS, Choi EC, Cho HJ, Kim MH, Kim SH, Kim DW, Kim S, Kang BS (2008) Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM. J Biol Chem 283(20):14032–14040PubMedCrossRefGoogle Scholar
  5. Kwon NH, Kang T, Lee JY, Kim HH, Kim HR, Hong J, Oh YS, Han JM, Ku MJ, Lee SY, Kim S (2011) Dual role of methionyl-tRNA synthetase in the regulation of translation and tumor suppressor activity of aminoacyl-tRNA synthetase-interacting multifunctional protein-3. Proc Natl Acad Sci USA 108(49):19635–19640PubMedCrossRefGoogle Scholar
  6. Lee SW, Cho BH, Park SG, Kim S (2004) Aminoacyl-tRNA synthetase complexes: beyond translation. J Cell Sci 117(Pt 17):3725–3734PubMedCrossRefGoogle Scholar
  7. Marshall L, Kenneth NS, White RJ (2008) Elevated tRNA(iMet) synthesis can drive cell proliferation and oncogenic transformation. Cell 133(1):78–89PubMedCrossRefGoogle Scholar
  8. Park BJ, Kang JW, Lee SW, Choi SJ, Shin YK, Ahn YH, Choi YH, Choi D, Lee KS, Kim S (2005a) The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR. Cell 120(2):209–221PubMedCrossRefGoogle Scholar
  9. Park SG, Ewalt KL, Kim S (2005b) Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers. Trends Biochem Sci 30(10):569–574PubMedCrossRefGoogle Scholar
  10. Park SG, Choi EC, Kim S (2010) Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): a triad for cellular homeostasis. IUBMB Life 62(4):296–302PubMedGoogle Scholar
  11. Rho SB, Kim MJ, Lee JS, Seol W, Motegi H, Kim S, Shiba K (1999) Genetic dissection of protein–protein interactions in multi-tRNA synthetase complex. Proc Natl Acad Sci USA 96(8):4488–4493PubMedCrossRefGoogle Scholar
  12. Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136(4):731–745PubMedCrossRefGoogle Scholar
  13. Stolboushkina EA, Garber MB (2011) Eukaryotic type translation initiation factor 2: structure-functional aspects. Biochemistry (Mosc) 76(3):283–294CrossRefGoogle Scholar
  14. Suragani RN, Ghosh S, Ehtesham NZ, Ramaiah KV (2006) Expression and purification of the subunits of human translational initiation factor 2 (eIF2): phosphorylation of eIF2 alpha and beta. Protein Expr Purif 47(1):225–233PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Wien 2013

Authors and Affiliations

  1. 1.Department of Life ScienceGachon UniversitySeongnam-SiKorea

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