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

Rosse, Carine, Boeckeler, Katrina, Linch, Mark, Radtke, Simone, Frith, David, Barnouin, Karin, Morsi, Ali Sayed, Hafezparast, Majid, Howell, Michael and Parker, Peter J (2012) Binding of dynein intermediate chain 2 to paxillin controls focal adhesion dynamics and migration. Journal of Cell Science, 125 (16). pp. 3733-3738. ISSN 0021-9533

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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

Item Type: Article
Schools and Departments: School of Life Sciences > Neuroscience
Subjects: Q Science > QH Natural history > QH0301 Biology
Depositing User: Majid Hafezparast
Date Deposited: 05 Dec 2012 11:43
Last Modified: 05 Dec 2012 11:43
URI: http://sro.sussex.ac.uk/id/eprint/43288
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