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Function of membranous lysyl-tRNA synthetase and its implication for tumorigenesis
- Authors
- Jeon, Young Ho; Lee, Jung Weon; Kim, Sunghoon
- Issue Date
- 12월-2016
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Lysyl-tRNA synthetase; Laminin receptor; Cancer metastasis; Protein-protein interaction; Anti-cancer drug; Membrane localization
- Citation
- BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v.1864, no.12, pp.1707 - 1713
- Indexed
- SCIE
SCOPUS
- Volume
- 1864
- Number
- 12
- Start Page
- 1707
- End Page
- 1713
- ISSN
- 1570-9639
- Abstract
- Aminoacyl-tRNA synthetases (ARSs) are essential enzymes that conjugate specific amino acids to their cognate tRNAs for protein synthesis. Besides their catalytic activity, recent studies have uncovered many additional functions of these enzymes through their interactions with diverse cellular factors. Among human ARSs, cytosolic lysyl-tRNA synthetase (KRS) is often highly expressed in cancer cells and tissues, and facilitates cancer cell migration and invasion through the interaction with the 67 kDa laminin receptor on the plasma membrane. Specific modulation of this interaction by small molecule inhibitors has revealed a new way to control metastasis. Here, we summarize the pro-metastatic functions of KRS and their patho-physiological implications. (C) 2016 Elsevier B.V. All rights reserved.
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