Function of membranous lysyl-tRNA synthetase and its implication for tumorigenesis.

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 67kDa 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.

• Authors: Ho Jeon Young, Jung Weon Lee, Sunghoon Kim
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1864 Issue 12 Pg. 1707-1713 (12 2016) ISSN: 0006-3002 [Print] Netherlands
• PMID: 27663887 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
• Copyright: Copyright © 2016 Elsevier B.V. All rights reserved.

Chemical References

• Receptors, Laminin
• Amino Acyl-tRNA Synthetases
• Lysine-tRNA Ligase

Topics

• Active Transport, Cell Nucleus
• Amino Acyl-tRNA Synthetases (chemistry, metabolism)
• Biocatalysis
• Carcinogenesis (metabolism)
• Cell Membrane (enzymology)
• Cell Movement
• Epithelial-Mesenchymal Transition
• Humans
• Lysine-tRNA Ligase (chemistry, metabolism)
• Models, Biological
• Models, Molecular
• Neoplasm Invasiveness
• Neoplasm Metastasis
• Protein Interaction Domains and Motifs
• Receptors, Laminin (chemistry, metabolism)