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© Research
Publication : Molecular cell

Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular cell - 01 Mar 2001

Lamaze C, Dujeancourt A, Baba T, Lo CG, Benmerah A, Dautry-Varsat A

Link to Pubmed [PMID] – 11463390

Mol. Cell 2001 Mar;7(3):661-71

Clathrin-dependent endocytosis has long been presented as the only efficient mechanism by which transmembrane receptors are internalized. We selectively blocked this process using dominant-negative mutants of Eps15 and showed that clathrin-mediated endocytosis of transferrin was inhibited, while endocytosis of interleukin 2 (IL2) receptors proceeded normally. Ultrastructural and biochemical experiments showed that clathrin-independent endocytosis of IL2 receptors exists constitutively in lymphocytes and is coupled to their association with detergent-resistant membrane domains. Finally, clathrin-independent endocytosis requires dynamin and is specifically regulated by Rho family GTPases. These results define novel properties of receptor-mediated endocytosis and establish that the IL2 receptor is efficiently internalized through this clathrin-independent pathway.

http://www.ncbi.nlm.nih.gov/pubmed/11463390