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Published online May 7, 2007
doi:10.1083/jcb.200609004
The Journal of Cell Biology, Vol. 177, No. 3, 515-525
The Rockefeller University Press, 0021-9525 $30.00
© 2007 White et al.
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Article

 {alpha}vß3 and {alpha}5ß1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration

Dominic P. White, Patrick T. Caswell, and Jim C. Norman

Integrin Cell Biology Laboratory, Beatson Institute for Cancer Research, Bearsden, Glasgow G61 1BD, Scotland, UK

Correspondence to Jim C. Norman: j.norman{at}beatson.gla.ac.uk

Accumulating evidence suggests that integrin recycling regulates cell migration. However, the lack of reagents to selectively target the trafficking of individual heterodimers, as opposed to endocytic transport as a whole, has made it difficult to define the contribution made by particular recycling pathways to directional cell movement. We show that autophosphorylation of protein kinase D1 (PKD1) at Ser916 is necessary for its association with {alpha}vß3 integrin. Expression of PKD1916A or the use of mutants of ß3 that do not bind to PKD1 selectively inhibits short-loop, Rab4-dependent recycling of {alpha}vß3, and this suppresses the persistence of fibroblast migration. However, we report that short-loop recycling does not directly contribute to fibroblast migration by moving {alpha}vß3 to the cell front, but by antagonizing {alpha}5ß1 recycling, which, in turn, influences the cell's decision to migrate with persistence or to move randomly.

Abbreviations used in this paper: MTOC, microtubule organizing center; PKD1, protein kinase D1; PMA, phorbol myristate acetate; ROCK, Rho kinase; shRNA, short hairpin RNA; ts, temperature-sensitive; VSVG, vesicular stomatitis virus G protein.


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