JNK phosphorylates paxillin and regulates cell migration

Cal Huang, Zenon Rajfur, Christoph Borchers, Michael D. Schaller, Ken Jacobson

Research output: Contribution to journalArticlepeer-review

411 Citations (Scopus)

Abstract

The c-Jun amino-terminal kinase (JNK) is generally thought to be involved in inflammation, proliferation and apoptosis. Accordingly, its substrates are transcription factors and antiapoptotic proteins. However, JNK has also been shown to be required for Drosophila dorsal closure, and MAP kinase/ERK kinase kinase 1, an upstream kinase in the JNK pathway, has been shown to be essential for cell migration. Both results imply that JNK is important in cell migration. Here we show that JNK1 is required for the rapid movement of both fish keratocytes and rat bladder tumour epithelial cells (NBT-II). Moreover, JNK1 phosphorylates serine 178 on paxillin, a focal adhesion adaptor, both in vitro and in intact cells. NBT-II cells expressing the Ser 178 → Ala mutant of paxillin (PaxS178A) formed focal adhesions and exhibited the limited movement associated with such contacts in both single-cell-migration and wound-healing assays. In contrast, cells expressing wild-type paxillin moved rapidly and retained dose contacts as the predominant adhesion. Expression of PaxS178A also inhibited the migration of two other cell lines. Thus, phosphorylation of paxillin by JNK seems essential for maintaining the labile adhesions required for rapid cell migration.

Original languageEnglish
Pages (from-to)219-223
Number of pages5
JournalNature
Volume424
Issue number6945
DOIs
Publication statusPublished - 10 Jul 2003
Externally publishedYes

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