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J Cell Sci. 2012 Aug 15;125(Pt 16):3733-8. doi: 10.1242/jcs.089557. Epub 2012 May 2.

Binding of dynein intermediate chain 2 to paxillin controls focal adhesion dynamics and migration.

Author information

1
Protein Phosphorylation Laboratory, Cancer Research UK, London Research Institute, London WC2A 3PX, UK. carine.rosse@curie.fr

Abstract

In migrating NRK cells, aPKCs control the dynamics of turnover of paxillin-containing focal adhesions (FA) determining migration rate. Using a proteomic approach (two-dimensional fluorescence difference gel electrophoresis), dynein intermediate chain 2 (dynein IC2) was identified as a protein that is phosphorylated inducibly during cell migration in a PKC-regulated manner. By gene silencing and co-immunoprecipitation studies, we show that dynein IC2 regulates the speed of cell migration through its interaction with paxillin. This interaction is controlled by serine 84 phosphorylation, which lies on the aPKC pathway. The evidence presented thus links aPKC control of migration to the dynein control of FA turnover through paxillin.

PMID:
22553211
DOI:
10.1242/jcs.089557
[Indexed for MEDLINE]
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