Evidence map›Paper›PMID 42321214›Full record

ArticleNature communications2026

FKBP8 connects the Hsp70-Hsp90 chaperone machinery to the folding of membrane proteins.

Man-Xi Ge, Ming-Zhi Wu, Jia Ji, Zhao-Peng Li, Zhongjian Bai, Jieyan He, Josefa Chuh, Yixiao Zhang, Jing Li, Zai-Rong Zhang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Man-Xi Ge *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0009-0009-6103-534X
Ming-Zhi Wu *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Jia Ji *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Zhao-Peng Li *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Zhongjian Bai *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Jieyan HeBiochemical and Cellular Pharmacology, Genentech, South San Francisco, CA, USA.
Josefa ChuhBiochemical and Cellular Pharmacology, Genentech, South San Francisco, CA, USA.ORCID http://orcid.org/0000-0001-5417-8750
Yixiao ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China. yzhang@sioc.ac.cn.
Jing LiBiochemical and Cellular Pharmacology, Genentech, South San Francisco, CA, USA. jing.li@gene.com.ORCID http://orcid.org/0000-0003-0138-1688
Zai-Rong ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China. zrzhang@sioc.ac.cn.ORCID http://orcid.org/0000-0001-9768-0548

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32570911
6 · The paper itself

Abstract

The folding of membrane protein cytoplasmic domains on the endoplasmic reticulum (ER) surface, and their coordination with transmembrane and exoplasmic regions, remains poorly understood. Through a genome-wide CRISPR-Cas9 screen, we identified the ER-anchored FK506 binding protein 8 (FKBP8) as a chaperone essential for membrane protein folding and assembly. Using ABC transporters as model substrates, we show that FKBP8 cooperates with Hsp70-Hsp90 machinery to remodel nascent or misfolded cytosolic domains into their native conformations. Cryo-EM analysis reveals that FKBP8 employs a conserved hydrophobic ϕ

Indexed as

HSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMembrane ProteinsTacrolimus Binding ProteinsATP-Binding Cassette TransportersCryoelectron MicroscopyCytosolEndoplasmic ReticulumHumansProtein BindingProtein FoldingATP-Binding Cassette TransportersFKBP8 protein, humanHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMembrane ProteinsTacrolimus Binding Proteins

Identifiers

PMID42321214
PMCPMC13470449

What OpenQuestion holds

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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.