Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat

Author:

Hooy Richard M.12ORCID,Iwamoto Yuichiro12ORCID,Tudorica Dan A.23ORCID,Ren Xuefeng12ORCID,Hurley James H.1234ORCID

Affiliation:

1. Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.

2. California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA.

3. Graduate Group in Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA.

4. Helen Wills Neuroscience Institute, University of California, Berkeley, Berkeley, CA 94720, USA.

Abstract

The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to sequester major histocompatibility complex class I (MHC-I), evading immune detection. We found that AP-1:Arf1:Nef:MHC-I forms a coat on tubulated membranes without clathrin and determined its structure. The coat assembles via Arf1 dimer interfaces. AP-1–positive tubules are enriched in cells upon clathrin knockdown. Nef localizes preferentially to AP-1 tubules in cells, explaining how Nef sequesters MHC-I. Coat contact residues are conserved across Arf isoforms and the Arf-dependent AP complexes AP-1, AP-3, and AP-4. Thus, AP complexes can self-assemble with Arf1 into tubular coats without clathrin or other scaffolding factors. The AP-1:Arf1 coat defines the structural basis of a broader class of tubulovesicular membrane coats as an intermediate in clathrin vesicle formation from internal membranes and as an MHC-I sequestration mechanism in HIV-1 infection.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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