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

Ho Jeon Young, Jung Weon Lee, Sunghoon Kim

Journal: Biochimica et biophysica acta 2019;1864(12):1707-1713

PMID: 27663887

Full Text on Elsevier Science View on PubMed

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.

Address: College of Pharmacy, Korea University, Sejong 30019, Republic of Korea; Medicinal Bioconvergence Research Center, Seoul National University, Seoul 08826, Republic of Korea.; Medicinal Bioconvergence Research Center, Seoul National University, Seoul 08826, Republic of Korea; Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea. Electronic address: [email protected].; Medicinal Bioconvergence Research Center, Seoul National University, Seoul 08826, Republic of Korea; Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.

DOI: 10.1016/j.bbapap.2016.09.009

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MeSH Terms: Active Transport, Cell Nucleus, Amino Acyl-tRNA Synthetases, Biocatalysis, Carcinogenesis, Cell Membrane, Cell Movement, Epithelial-Mesenchymal Transition, Humans, Lysine-tRNA Ligase, Models, Biological, Models, Molecular, Neoplasm Invasiveness, Neoplasm Metastasis, Protein Interaction Domains and Motifs, Receptors, Laminin