Evidence map›Paper›PMID 28134256›Full record

ArticleNature communications2017

The tumour suppressor APC promotes HIV-1 assembly via interaction with Gag precursor protein.

Kei Miyakawa, Mayuko Nishi, Satoko Matsunaga, Akiko Okayama, Masaki Anraku, Ayumi Kudoh, Hisashi Hirano, Hirokazu Kimura, Yuko Morikawa, Naoki Yamamoto and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 14 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 3 countries.

Kei MiyakawaDepartment of Microbiology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
Mayuko NishiDepartment of Microbiology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
Satoko MatsunagaDepartment of Microbiology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
Akiko OkayamaAdvanced Medical Research Center, Yokohama City University, Yokohama 236-0004, Japan.
Masaki AnrakuDepartment of Microbiology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
Ayumi KudohDepartment of Microbiology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
Hisashi HiranoAdvanced Medical Research Center, Yokohama City University, Yokohama 236-0004, Japan.
Hirokazu KimuraInfectious Disease Surveillance Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.
Yuko MorikawaKitasato Institute for Life Sciences and Graduate School for Infection Control, Kitasato University, Tokyo 108-8641, Japan.
Naoki YamamotoDepartment of Microbiology, National University of Singapore, Singapore 117597, Singapore.
Akira OnoDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Akihide RyoDepartment of Microbiology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
Yokohama City University · JPKitasato University · JPNational Institute of Infectious Diseases · JPNational University of Singapore · SGUniversity of Michigan–Ann Arbor · USYokohama City University Medical Center · JP

Funding

Mechanisms that determine subcellular sites of HIV-1 assemblyR01AI071727 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ONO, AKIRA · 2007 to 2016
$3.6M
NIAID NIH HHS R01 AI071727
6 · The paper itself

Abstract

Diverse cellular proteins and RNAs are tightly regulated in their subcellular localization to exert their local function. Here we report that the tumour suppressor adenomatous polyposis coli protein (APC) directs the localization and assembly of human immunodeficiency virus (HIV)-1 Gag polyprotein at distinct membrane components to enable the efficient production and spread of infectious viral particles. A proteomic analysis and subsequent biomolecular interaction assay reveals that the carboxyl terminus of APC interacts with the matrix region of Gag. Ectopic expression of APC, but not its familial adenomatous polyposis-related truncation mutant, prominently enhances HIV-1 production. Conversely, the depletion of APC leads to a significant decrease in membrane targeting of viral components, resulting in the severe loss of production of infectious virions. Furthermore, APC promotes the directional assembly of viral components at virological synapses, thereby facilitating cell-to-cell viral transmission. These findings reveal an unexpected role of APC in the directional spread of HIV-1.

Indexed as

Host-Pathogen InteractionsAcquired Immunodeficiency SyndromeAdenomatous Polyposis Coli ProteinCell Line, Tumorgag Gene Products, Human Immunodeficiency VirusHEK293 CellsHIV-1HumansMutationProtein BindingProteomicsRNA, Small InterferingVirus AssemblyAdenomatous Polyposis Coli ProteinAPC protein, humangag Gene Products, Human Immunodeficiency VirusRNA, Small Interfering

Identifiers

PMID28134256
PMCPMC5290283
OpenAlexW2582569562

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.