JNK phosphorylates paxillin and regulates cell migration

Cai Huang, Zenon Rajfur, Christoph Borchers, Michael D. Schaller and Ken Jacobson ()
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Cai Huang: University of North Carolina
Zenon Rajfur: University of North Carolina
Christoph Borchers: University of North Carolina
Michael D. Schaller: University of North Carolina
Ken Jacobson: University of North Carolina

Nature, 2003, vol. 424, issue 6945, 219-223

Abstract: Abstract The c-Jun amino-terminal kinase (JNK) is generally thought to be involved in inflammation, proliferation and apoptosis1,2. Accordingly, its substrates are transcription factors and anti-apoptotic proteins2. However, JNK has also been shown to be required for Drosophila dorsal closure3,4, and MAP kinase/ERK kinase kinase 1, an upstream kinase in the JNK pathway, has been shown to be essential for cell migration5,6. 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 close 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.

Date: 2003
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DOI: 10.1038/nature01745

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