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A tubular EHD1‐containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane

Caplan, Steve, Naslavsky, Naava, Hartnell, Lisa M., Lodge, Robert, Polishchuk, Roman S., Donaldson, Julie G., Bonifacino, Juan S.·2002·The EMBO Journal
DOI 10.1093/emboj/21.11.2557
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Abstract

The Eps15 homology (EH) domain-containing protein, EHD1, has recently been ascribed a role in the recycling of receptors internalized by clathrin-mediated endocytosis. A subset of plasma membrane proteins can undergo internalization by a clathrin-independent pathway regulated by the small GTP-binding protein ADP-ribosylation factor 6 (Arf6). Here, we report that endogenous EHD proteins, as well as transgenic tagged EHD1, are associated with long, membrane-bound tubules containing Arf6. EHD1 appears to induce tubule formation, which requires nucleotide cycling on Arf6 and intact microtubules. Mutations in the N-terminal P-loop domain or deletion of the C-terminal EH domain of EHD1 prevent association of EHD1 with tubules or induction of tubule formation. The EHD1 tubules contain internalized major histocompatibility complex class I (MHC-I) molecules that normally traffic through the Arf6 pathway. Recycling assays show that overexpression of EHD1 enhances MHC-I recycling. These observations suggest an additional function of EHD1 as a tubule-inducing factor in the Arf6 pathway for recycling of plasma membrane proteins internalized by clathrin-independent endocytosis.

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Metadata

Authors
Caplan, S., Naslavsky, N., Hartnell, L. M., Lodge, R., Polishchuk, R. S., Donaldson, J. G., & Bonifacino, J. S.
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2002-06-03
Volume
21
Issue
11
Pages
2557-2567
ISSN
  • 0261-4189
  • 1460-2075
DOI
10.1093/emboj/21.11.2557
Cited by
270
References
1
Language
en
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