Structural highlights
Function
A0A8C2UGL4_CHILA GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.[RuleBase:RU369003]
Publication Abstract from PubMed
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.
Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat.,Hooy RM, Iwamoto Y, Tudorica DA, Ren X, Hurley JH Sci Adv. 2022 Oct 21;8(42):eadd3914. doi: 10.1126/sciadv.add3914. Epub 2022 Oct, 21. PMID:36269825[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hooy RM, Iwamoto Y, Tudorica DA, Ren X, Hurley JH. Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat. Sci Adv. 2022 Oct 21;8(42):eadd3914. doi: 10.1126/sciadv.add3914. Epub 2022 Oct, 21. PMID:36269825 doi:http://dx.doi.org/10.1126/sciadv.add3914
