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

Ho Jeon Young, Jung Weon Lee, Sunghoon Kim

Research output: Contribution to journalReview articlepeer-review

10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1707-1713
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number12
Publication statusPublished - 2016 Dec 1

Bibliographical note

Publisher Copyright:
© 2016

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Function of membranous lysyl-tRNA synthetase and its implication for tumorigenesis'. Together they form a unique fingerprint.

Cite this