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

Biochim Biophys Acta. 2016 Dec;1864(12):1707-1713. doi: 10.1016/j.bbapap.2016.09.009. Epub 2016 Sep 20.

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.

Keywords: Anti-cancer drug; Cancer metastasis; Laminin receptor; Lysyl-tRNA synthetase; Membrane localization; Protein-protein interaction.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

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

Substances

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