Abstract:
: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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Lamaze C,Dujeancourt A,Baba T,Lo CG,Benmerah A,Dautry-Varsat Adoi
10.1016/s1097-2765(01)00212-xsubject
Has Abstractpub_date
2001-03-01 00:00:00pages
661-71issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00212-Xjournal_volume
7pub_type
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