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Cited by 50Cellular transport and secretionHIV Research and TreatmentUbiquitin and proteasome pathways

Contribution of the clathrin adaptor AP-1 subunit µ1 to acidic cluster protein sorting

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Navarro Negredo, Paloma, Edgar, James R., Wrobel, Antoni G., Zaccai, Nathan R., Antrobus, Robin, Owen, David J., Robinson, Margaret S.·2017·Journal of Cell Biology
DOI 10.1083/jcb.201602058PMC PMC5584140
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Abstract

Acidic clusters act as sorting signals for packaging cargo into clathrin-coated vesicles (CCVs), and also facilitate down-regulation of MHC-I by HIV-1 Nef. To find acidic cluster sorting machinery, we performed a gene-trap screen and identified the medium subunit (µ1) of the clathrin adaptor AP-1 as a top hit. In µ1 knockout cells, intracellular CCVs still form, but acidic cluster proteins are depleted, although several other CCV components were either unaffected or increased, indicating that cells can compensate for long-term loss of AP-1. In vitro experiments showed that the basic patch on µ1 that interacts with the Nef acidic cluster also contributes to the binding of endogenous acidic cluster proteins. Surprisingly, µ1 mutant proteins lacking the basic patch and/or the tyrosine-based motif binding pocket could rescue the µ1 knockout phenotype completely. In contrast, these mutants failed to rescue Nef-induced down-regulation of MHC class I, suggesting a possible mechanism for attacking the virus while sparing the host cell.

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  • The basic patch of AP-1μ subunit is required for binding of acidic cluster sequences.

    “The basic patch (Lys274, Lys298, Lys302, Arg303, and Arg304) of the AP-1μ subunit has been shown to be required for the binding of acidic cluster sequences (Navarro Negredo et al., 2017).”

    From Distinct anterograde trafficking pathways of BACE1 and amyloid precursor protein from the TGN and the regulation of amyloid-β production (2020) · cites this paper as Navarro Negredo et al., 2017

    The Results identify Lys274, Lys298, Lys302, Arg303, and Arg304 as the basic patch and report that mutating them reduces binding. The Discussion says the patch is required for optimal binding, not that binding cannot occur without it; the claim overstates its necessity. Page numbers are not available in our copy. (LLM, conf=0.88)

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Authors
Navarro Negredo, P., Edgar, J. R., Wrobel, A. G., Zaccai, N. R., Antrobus, R., Owen, D. J., & Robinson, M. S.
Affiliations
  • Cambridge Institute for Medical Research, University of Cambridge, Cambridge, England, UK
  • University of Cambridge (GB)
Corresponding author
Robinson, Margaret S.
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2017-07-25
Volume
216
Issue
9
Pages
2927-2943
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201602058
PMC
PMC5584140
OpenAlex
W2736608801
Cited by
50
References
5
Citations by year
2026: 8 · 2025: 6 · 2024: 7 · 2022: 5 · 2021: 4 · 2020: 3 · 2019: 9 · 2018: 6 · 2017: 1 · 2015: 1
FWCI
2.71
Type
journal article
Language
en
Open access
Licence
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
  • Apollo (University of Cambridge) (submittedVersion, cc-by-nc-sa)
  • Apollo
Funders
  • Wellcome Trust (086598)
  • Cambridge Institute for Medical Research (100140)
  • Medical Research Council
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
clathrin-coated vesicles, HIV-1 Nef, MHC class I downregulation, tyrosine-based motif, cargo sorting, host-virus interaction
MeSH terms
Flow Cytometry, Genotype, HeLa Cells, Humans, Models, Molecular, Mutation, Phenotype, Protein Binding, Structure-Activity Relationship, Time Factors, Transfection, Histocompatibility Antigens Class I, HIV-1, Protein Transport, Clathrin-Coated Vesicles, Adaptor Protein Complex 1, Adaptor Protein Complex mu Subunits, nef Gene Products, Human Immunodeficiency Virus, Protein Interaction Domains and Motifs, Host-Pathogen Interactions, Gene Knockdown Techniques, HEK293 Cells, CRISPR-Cas Systems

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