I evaluated the following article for Faculty of 1000. The original evaluation is available at:
C Rosse,K Boeckeler,M Linch,S Radtke,D Frith,K Barnouin,AS Morsi,M Hafezparast,M Howell,PJ Parker
Binding of Dynein Intermediate Chain 2 to Paxillin controls Focal adhesion dynamics and migration.
J Cell Sci 2012 PMID: 22553211 DOI: 10.1242/jcs.089557
This article nicely defines a role for dynein phosphorylation in cell migration through interaction with the focal adhesion protein paxillin. The authors show that dynein is phosphorylated during cell migration, using an unbiased proteomic approach. The dynein intermediate chain is phosphorylated in serine-84 by atypical protein kinase C isoforms, as shown by mutagenesis and inhibitor studies. The data show that dynein has a role in controlling the stability of focal adhesions and suggest a model in which phosphorylation of dynein on its intermediate chain subunit decreases its affinity for paxillin. While the work leaves many questions unanswered, it provides a nice piece in the puzzle of how dynein regulates focal adhesion dynamics.