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JNK phosphorylates paxillin and regulates cell migration

Cai Huang1, Zenon Rajfur, Christoph Borchers

  • 1Department of Cell and Developmental Biology, Comprehensive Center for Inflammatory Disorders, University of North Carolina, Chapel Hill, North Carolina 27599-7090, USA.

Nature
|July 11, 2003
PubMed

Insights

The c-Jun amino-terminal kinase (JNK) pathway regulates cell migration by phosphorylating paxillin. This phosphorylation is crucial for forming the dynamic focal adhesions necessary for rapid cell movement.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The c-Jun amino-terminal kinase (JNK) pathway is traditionally linked to inflammation, proliferation, and apoptosis.
  • Emerging evidence suggests JNK's involvement in cell migration, notably in Drosophila dorsal closure and via upstream kinases like MAP kinase/ERK kinase kinase 1.

Purpose of the Study:

  • To investigate the role of JNK1 in cell migration.
  • To identify JNK1 substrates involved in regulating cell movement.
  • To elucidate the mechanism by which JNK1 influences cell adhesion dynamics.

Main Methods:

  • Utilized fish keratocytes and rat bladder tumour epithelial cells (NBT-II) to study cell migration.
  • Employed in vitro and in vivo phosphorylation assays to examine JNK1 activity on paxillin.
  • Generated and analyzed cells expressing a serine 178 alanine mutant of paxillin (Pax(S178A)) in migration assays.

Main Results:

  • JNK1 is essential for the rapid migration of fish keratocytes and NBT-II cells.
  • JNK1 directly phosphorylates serine 178 on the focal adhesion adaptor protein paxillin.
  • Pax(S178A) mutant cells displayed impaired migration, forming stable focal adhesions and exhibiting reduced movement compared to wild-type cells.

Conclusions:

  • Phosphorylation of paxillin by JNK1 is a critical step for maintaining the transient focal adhesions required for efficient cell migration.
  • This finding highlights a novel role for the JNK pathway in regulating cell motility through modulation of adhesion turnover.

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