Evidence map›Paper›PMID 28056051›Full record

ArticlePloS one2017

Mapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90.

Feng Hong, Saleh Mohammad Rachidi, Debbie Lundgren, David Han, Xiu Huang, Hongyu Zhao, Yayoi Kimura, Hisashi Hirano, Osamu Ohara, Heichiiro Udono and 3 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 29 citations in OpenAlex.

  1. Cnpy1 is a candidate endoplasmic reticulum chaperone of vomeronasal type 2 GPCRs.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
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  5. CCDC134 controls TLR biogenesis through the ER chaperone Gp96.The Journal of experimental medicine · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Chemical Biology Framework to Illuminate Proteostasis.Annual review of biochemistry · 2020
    Review
  13. Article
  14. Article
  15. Characterization of CNPY5 and its family members.Protein science : a publication of the Protein Society · 2019
    Article
  16. Mechanisms protecting host cells against bacterial pore-forming toxins.Cellular and molecular life sciences : CMLS · 2019
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

13 authors at 7 institutions in 3 countries.

Feng HongDepartment of Microbiology & Immunology, Medical University of South Carolina, Charleston, United States of America.
Saleh Mohammad RachidiDepartment of Microbiology & Immunology, Medical University of South Carolina, Charleston, United States of America.
Debbie LundgrenCenter for Vascular Biology, University of Connecticut Health Center, Farmington, Connecticut, United States of America.
David HanCenter for Vascular Biology, University of Connecticut Health Center, Farmington, Connecticut, United States of America.
Xiu HuangDepartment of Epidemiology and Public Health, Yale University, School of Medicine, New Haven, Connecticut, United States of America.
Hongyu ZhaoDepartment of Epidemiology and Public Health, Yale University, School of Medicine, New Haven, Connecticut, United States of America.
Yayoi KimuraLaboratory for Immunogenomics, RIKEN Research Center for Allergy and Immunology, Tsurumi-ku, Yokohama, Kanagawa, Japan.
Hisashi HiranoLaboratory for Immunogenomics, RIKEN Research Center for Allergy and Immunology, Tsurumi-ku, Yokohama, Kanagawa, Japan.
Osamu OharaGraduate School of Nanobioscience, Yokohama City University, Tsurumi-ku, Yokohama, Kanagawa, Japan.
Heichiiro UdonoDepartment of Immunology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Japan.
Songdong MengCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.
Bei LiuDepartment of Microbiology & Immunology, Medical University of South Carolina, Charleston, United States of America.
Zihai LiDepartment of Microbiology & Immunology, Medical University of South Carolina, Charleston, United States of America.
Medical University of South Carolina · USRIKEN Center for Integrative Medical Sciences · JPUConn Health · USYale University · USChinese Academy of Sciences · CNOkayama University · JPYokohama City University · JP

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Translational Science Laboratory Shared ResourceP30CA138313 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI RAYMOND N. DUBOIS · 2009 to 2026
$42.7M
Project 3: Structural Basis for grp94 Drug Development and Chaperone FunctionP01CA186866 · NCI · OHIO STATE UNIVERSITY · PI LI, ZIHAI · 2015 to 2019
$6.7M
Roles and Mechanisms of gp96 in Chaperoning Innate ImmunityR01AI070603 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI LI, ZIHAI · 2007 to 2016
$3.8M
Molecular chaperones and immune toleranceR01AI077283 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI LI, ZIHAI · 2009 to 2021
$3.7M
STATISTICAL METHODS TO MAP GENES FOR COMPLEX TRAITSR01GM059507 · NIGMS · YALE UNIVERSITY · PI ZHAO, HONGYU · 1999 to 2013
$3.6M
Extrinsic and intrinsic factors regulating commensal-specific T helper-17 cellsU01AI125859 · NIAID · OHIO STATE UNIVERSITY · PI LIU, BEI · 2016 to 2020
$2.5M
Thrombocytes in Cancer ImmunityR01CA188419 · NCI · OHIO STATE UNIVERSITY · PI LI, ZIHAI · 2015 to 2019
$1.9M
Mechanism of gp96/grp94 in regulating plasma cells and myelomaR01CA193939 · NCI · OHIO STATE UNIVERSITY · PI LIU, BEI · 2016 to 2020
$1.7M
NCATS NIH HHS UL1 TR001863NCI NIH HHS P01 CA186866NCI NIH HHS P30 CA138313NCI NIH HHS R01 CA188419NCI NIH HHS R01 CA193939NIAID NIH HHS R01 AI070603NIAID NIH HHS R01 AI077283NIAID NIH HHS U01 AI125859NIGMS NIH HHS R01 GM059507
6 · The paper itself

Abstract

Up to 10% of cytosolic proteins are dependent on the mammalian heat shock protein 90 (HSP90) for folding. However, the interactors of its endoplasmic reticulum (ER) paralogue (gp96, Grp94 and HSP90b1) has not been systematically identified. By combining genetic and biochemical approaches, we have comprehensively mapped the interactome of gp96 in macrophages and B cells. A total of 511 proteins were reduced in gp96 knockdown cells, compared to levels observed in wild type cells. By immunoprecipitation, we found that 201 proteins associated with gp96. Gene Ontology analysis indicated that these proteins are involved in metabolism, transport, translation, protein folding, development, localization, response to stress and cellular component biogenesis. While known gp96 clients such as integrins, Toll-like receptors (TLRs) and Wnt co-receptor LRP6, were confirmed, cell surface HSP receptor CD91, TLR4 pathway protein CD180, WDR1, GANAB and CAPZB were identified as potentially novel substrates of gp96. Taken together, our study establishes gp96 as a critical chaperone to integrate innate immunity, Wnt signaling and organ development.

Indexed as

AnimalsBlotting, WesternB-LymphocytesCell LineCell MembraneChromatography, LiquidElectrophoresis, Gel, Two-DimensionalEndoplasmic ReticulumGenotypeHSP90 Heat-Shock ProteinsImmunoprecipitationMembrane GlycoproteinsMiceMolecular ChaperonesSignal TransductionTandem Mass SpectrometryHSP90 Heat-Shock ProteinsMembrane GlycoproteinsMolecular Chaperones

Identifiers

PMID28056051
PMCPMC5215799
OpenAlexW2567958543

What OpenQuestion 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 OpenQuestion graph.