Phosphorylation of focal adhesion kinase at Tyrosine 407 negatively regulates Ras transformation of fibroblasts

Jihyun Jeon, Hyangjin Lee, Haein Park, Jung hyun Lee, Sojoong Choi, Jisun Hwang, Inn Oc Han, Eok Soo Oh

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7 Scopus citations


Focal adhesion kinase (FAK) mediates signal transduction in response to multiple extracellular inputs, via tyrosine phosphorylation at specific residues. We recently reported that FAK Tyr-407 phosphorylation negatively regulates the enzymatic and biological activities of FAK, unlike phosphorylation of other tyrosine residues. In this study, we further investigated the effect of FAK Tyr-407 phosphorylation on cell transformation. We found that FAK Tyr-407 phosphorylation was lower in H-Ras transformed NIH3T3 and K-Ras transformed rat-2 fibroblasts than in the respective untransformed control cells. Consistently, FAK Tyr-407 phosphorylation was decreased in parallel with cell transformation in H-Ras-inducible NIH3T3 cells and increased during trichostatin A-induced detransformation of both K-Ras transformed rat-2 fibroblasts and H-Ras transformed NIH3T3 cells. In addition, overexpression of a phosphorylation-mimicking FAK Tyr-407 mutant inhibited morphological transformation of H-Ras-inducible NIH3T3 cells and inhibited invasion activity and anchorage-independent growth of H-Ras-transformed NIH3T3 cells. Taken together, these data strongly suggest that FAK Tyr-407 phosphorylation negatively regulates transformation of fibroblasts.

Original languageEnglish
Pages (from-to)1062-1066
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 28 Dec 2007

Bibliographical note

Funding Information:
This study was supported by a grant of the Molecular and Cellular BioDiscovery Research Program (CBM-01B-2-1 to E.S.O.), and in part by a grant of the National R&D Program for Cancer Control, Ministry of Health & Welfare, Republic of Korea (0420070-1 to E.S.O.) and Grant No. R15-2006-020 from the NCRC program of the MOST and the KOSEF through the Center for Cell Signaling & Drug Discovery Research at Ewha Womans University.


  • Focal adhesion kinase
  • Signal transduction
  • Transformation
  • Tyrosine phosphorylation


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