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

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 Cell

journal_title

Molecular cell

authors

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

doi

10.1016/s1097-2765(01)00212-x

subject

Has Abstract

pub_date

2001-03-01 00:00:00

pages

661-71

issue

3

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00212-X

journal_volume

7

pub_type

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