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

• Published in: The Journal of cell biology Vol. 168; no. 1; pp. 155 - 163
• Main Authors: Sauvonnet, Nathalie, Dujeancourt, Annick, Dautry-Varsat, Alice
• Format: Journal Article
• Language: English
• Published: 2005
• ISSN: 0021-9525; 1540-8140

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.