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TitleHIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation.
Journal, issue, pagesCell, Vol. 174, Issue 3, Page 659-671.e14, Year 2018
Publish dateJul 26, 2018
AuthorsKyle L Morris / Cosmo Z Buffalo / Christina M Stürzel / Elena Heusinger / Frank Kirchhoff / Xuefeng Ren / James H Hurley /
PubMed AbstractThe HIV accessory protein Nef counteracts immune defenses by subverting coated vesicle pathways. The 3.7 Å cryo-EM structure of a closed trimer of the clathrin adaptor AP-1, the small GTPase Arf1, ...The HIV accessory protein Nef counteracts immune defenses by subverting coated vesicle pathways. The 3.7 Å cryo-EM structure of a closed trimer of the clathrin adaptor AP-1, the small GTPase Arf1, HIV-1 Nef, and the cytosolic tail of the restriction factor tetherin suggested a mechanism for inactivating tetherin by Golgi retention. The 4.3 Å structure of a mutant Nef-induced dimer of AP-1 showed how the closed trimer is regulated by the dileucine loop of Nef. HDX-MS and mutational analysis were used to show how cargo dynamics leads to alternative Arf1 trimerization, directing Nef targets to be either retained at the trans-Golgi or sorted to lysosomes. Phosphorylation of the NL4-3 M-Nef was shown to regulate AP-1 trimerization, explaining how O-Nefs lacking this phosphosite counteract tetherin but most M-Nefs do not. These observations show how the higher-order organization of a vesicular coat can be allosterically modulated to direct cargoes to distinct fates.
External linksCell / PubMed:30053425 / PubMed Central
MethodsEM (single particle)
Resolution3.73 - 6.8 Å
Structure data

EMDB-7453: Structure of the HIV-Nef dileucine mutant bound AP-1:Arf1 dimer monomeric subunit
PDB-6d83: Structure of the cargo bound AP-1:Arf1:tetherin-Nef (L164A, L165A) dileucine mutant dimer monomeric subunit
Method: EM (single particle) / Resolution: 4.27 Å

EMDB-7454: Structure of the HIV-Nef dileucine mutant bound AP-1:Arf1 dimer
PDB-6d84: Structure of the cargo bound AP-1:Arf1:tetherin-Nef (L164A, L165A) dileucine mutant dimer
Method: EM (single particle) / Resolution: 6.72 Å

EMDB-7455, PDB-6dff:
Structure of the cargo bound AP-1:Arf1:tetherin-Nef monomer
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-7456:
Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer monomeric subunit after focussed classification
Method: EM (single particle) / Resolution: 4.05 Å

EMDB-7457: Structure of the HIV-Nef bound AP-1:Arf1 closed trimer monomeric subunit
PDB-6cm9: Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer monomeric subunit
Method: EM (single particle) / Resolution: 3.73 Å

EMDB-7458:
Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer
Method: EM (single particle) / Resolution: 4.27 Å

EMDB-7563: Structure of the HIV-Nef tetherin cargo bound AP-1:Arf1 stable closed trimer
PDB-6cri: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer
Method: EM (single particle) / Resolution: 6.8 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN / PROTEIN TRANSPORT / AP / HIV / Nef / trafficking / TRANSPORT PROTEIN

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