Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I.

Molecular biology of the cell - 1 Jun 2012

Dikeakos Jimmy D, Thomas Laurel, Kwon Grace, Elferich Johannes, Shinde Ujwal, Thomas Gary

Abstract excerpt

The human immunodeficiency virus type 1 (HIV-1) accessory protein Nef directs virus escape from immune surveillance by subverting host cell intracellular signaling and membrane traffic to down-regulate cell-surface major histocompatibility complex class I (MHC-I). The interaction of Nef with the sorting proteins PACS-1 and PACS-2 mediates key signaling and trafficking steps required for Nef-mediated MHC-I...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Down-Regulation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endosomes

Share to Histocompatibility Antigens Class I

Share to nef Gene Products, Human Immunodeficiency Virus

Share to Protein Structure, Secondary

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22496420
DOI: 10.1091/mbc.E11-11-0928
PMCID: PMC3364181

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I.PMID 22496420Read ↗

HIV-1 Nef disrupts intracellular trafficking of major histocompatibility complex class I, CD4, CD8, and CD28 by distinct pathways that share common elements.Semantic proximity Read ↗

HIV ‐1 Nef: Taking Control of Protein TraffickingSemantic proximity Read ↗

Functional characterization of the human immunodeficiency virus type 1 Nef acidic domain.Semantic proximity Read ↗

Human Immunodeficiency Virus Type 1 Nef: Adapting to Intracellular Trafficking PathwaysSemantic proximity Read ↗

Human immunodeficiency virus type 1 Nef domains required for disruption of major histocompatibility complex class I trafficking are also necessary for coprecipitation of Nef with HLA-A2.Semantic proximity Read ↗

How HIV Nef Proteins Hijack Membrane Traffic To Promote InfectionSemantic proximity Read ↗

HIV-1 Nef sequesters MHC-I intracellularly by targeting early stages of endocytosis and recyclingSemantic proximity Read ↗

Identification of a novel binding site between HIV type 1 Nef C-terminal flexible loop and AP2 required for Nef-mediated CD4 downregulation.Semantic proximity Read ↗

Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3.Semantic proximity Read ↗

Dynamic Evolution of the Human Immunodeficiency Virus Type 1 Pathogenic Factor, NefSemantic proximity Read ↗

The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail.Semantic proximity Read ↗

An MHC-I Cytoplasmic Domain/HIV-1 Nef Fusion Protein Binds Directly to the μ Subunit of the AP-1 Endosomal Coat ComplexSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.