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Published online 28 December 2004. doi:10.1083/jcb.200406174
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 1, 155-163
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Article

 Cortactin and dynamin are required for the clathrin-independent endocytosis of {gamma}c cytokine receptor

Nathalie Sauvonnet, Annick Dujeancourt, and Alice Dautry-Varsat

Unité de Biologie des Interactions Cellulaires, Institut Pasteur, Centre National de la Recherche Scientifique, URA 2582, 75724 Paris, Cedex 15, France

Correspondence to Alice Dautry-Varsat: adautry{at}pasteur.fr

Endocytosis is critical for many cellular functions. We show that endocytosis of the common {gamma}c cytokine receptor is clathrin independent by using a dominant-negative mutant of Eps15 or RNA interference to knock down clathrin heavy chain. This pathway is synaptojanin independent and requires the GTPase dynamin. In addition, this process requires actin polymerization. To further characterize the function of dynamin in clathrin-independent endocytosis, in particular its connection with the actin cytoskeleton, we focused on dynamin-binding proteins that interact with F-actin. We compared the involvement of these proteins in the clathrin-dependent and -independent pathways. Thus, we observed that intersectin, syndapin, and mAbp1, which are necessary for the uptake of transferrin (Tf), a marker of the clathrin route, are not required for {gamma}c receptor endocytosis. Strikingly, cortactin is needed for both {gamma}c and Tf internalizations. These results reveal the ubiquitous action of cortactin in internalization processes and suggest its role as a linker between actin dynamics and clathrin-dependent and -independent endocytosis.

Abbreviations used in this paper: GPI, glycosylphosphatidylinositol; IL, interleukin; PI, phosphatidylinositol; PRD, proline-rich domain; SH3, Src homology 3; Tf, transferrin.


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