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TitleFKBP8 connects the Hsp70-Hsp90 chaperone machinery to the folding of membrane proteins.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateJun 19, 2026
AuthorsMan-Xi Ge / Ming-Zhi Wu / Jia Ji / Zhao-Peng Li / Zhongjian Bai / Jieyan He / Josefa Chuh / Yixiao Zhang / Jing Li / Zai-Rong Zhang /
PubMed AbstractThe 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 ...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 ϕϕϕ/ϕϕ cluster to help form a large client-binding cavity within the FKBP8-Hsp90 complex that captures folding intermediates. FKBP8 deficiency, disruption of this cluster, or disease-associated mutations within FKBP8 abolish substrate maturation, leading to ER retention and degradation. Reconstitution with purified components demonstrates that FKBP8 and Hsp40-Hsp70-HOP-Hsp90 constitute a minimal machinery capable of restoring the native structure of a misfolded ABC transporter. These findings uncover a dedicated folding module at the ER-cytosol interface that bridges cytosolic chaperones with membrane protein quality control, suggesting a broad role for FKBP8 in safeguarding the biogenesis of complex membrane proteins.
External linksNat Commun / PubMed:42321214 / PubMed Central
MethodsEM (single particle)
Resolution4.09 Å
Structure data

66931

9xj8

EMDB-66931, PDB-9xj8:
Cryo-EM structure of Hsp90(E47A)-FKBP8 complex
Method: EM (single particle) / Resolution: 4.09 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsCHAPERONE / Hsp90 / Fkbp8 / Molecular chaperone / Complex

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