Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis

H. J. Kim, Y. M. Kim, S. Lim, Y. K. Nam, J. Jeong, H. J. Kim, K. J. Lee

Research output: Contribution to journalArticlepeer-review

131 Scopus citations


Ubiquitin C-terminal hydrolase-L1 (UCH-L1) catalyses the hydrolysis of ubiquitin ester and amide mainly in neuronal cells. Recently it was proposed as a marker with a potential role in carcinogenesis. However, the molecular mechanism underlying the biological function of UCH-L1 in tumor cells is poorly understood. We found that UCH-L1 is highly expressed in non-small lung cancer cell line H157, having high invasive potential, and that the expression of UCH-L1 in tumor cells enhances their invasive potential in vitro and in vivo. UCH-L1 changes cell morphology by regulating cell adhesion through Akt-mediated pathway. Suppressing UCH-L1 expression by RNAi significantly suppressed the invasion in vitro and in vivo, and the activation of Akt and downstream mitogen activated protein kinases c-Jun N-terminal kinases and p38, but not ERK. In Akt-negative mutants, overexpression of UCH-L1 does not affect the invasion and migration capability of H157 cells. These results suggest that UCH-L1 is a key molecule to regulate tumor-cell invasion by upstream activation of Akt.

Original languageEnglish (US)
Pages (from-to)117-127
Number of pages11
Issue number1
StatePublished - Jan 8 2009
Externally publishedYes


  • Akt activation
  • Deubiquitinating enzyme
  • Lung cancer
  • Metastasis
  • Proteomics
  • Tumor invasion
  • UCH-L1

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research


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