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Updated: May 22, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
Binding of dynein intermediate chain 2 to paxillin controls focal adhesion dynamics and migration
Carine Rosse1, Katrina Boeckeler, Mark Linch
1Protein 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.
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