Tensin can induce JNK and p38 activation

Ben Zion Katz*, Muriel Zohar, Hidemi Teramoto, Kazue Matsumoto, J. Silvio Gutkind, Diane C. Lin, Shin Lin, Kenneth M. Yamada

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Cells organize diverse types of specialized adhesion sites upon attachment to extracellular matrix (ECM) components. One of the physiological roles of such cell-ECM interactions is to initiate and regulate adhesion-mediated signal transduction responses. The association of cells with fibronectin fibrils has been shown to regulate the JNK and p38 signaling pathways. We tested whether tensin, a cytoskeletal component localized to both focal contacts and fibronectin-associated fibrillar adhesions, can induce these signaling pathways. We found that tensin overexpression resulted in activation of both the c-Jun amino-terminal kinase (JNK) and p38 pathways. Tensin-mediated JNK activation was independent of the activities of the small GTP binding proteins Rac and Cdc42, but did depend on SEK, a kinase involved in the JNK pathway. We suggest that tensin may directly activate the JNK and p38 pathways, acting downstream or independent of the activities of the small GTP binding proteins Rac and Cdc42. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)717-720
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 16 Jun 2000
Externally publishedYes


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