Evidence map›Paper›PMID 42190603›Full record

ArticleBiochemical and biophysical research communications2026

Dual proximity-based interactome mapping of FKBP51 and FKBP52 uncovers shared metabolic networks.

Shannon E Hill, Priyanshi Parikh, Niat T Gebru, Sanam Banjade, Jennifer Guergues, Jessica Wohlfahrt, Stanley M Stevens, Laura J Blair

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical and biophysical research 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

8 authors.

Shannon E HillByrd Alzheimer's Center and Research Institute, Tampa, FL, USA; Department of Molecular Medicine, University of South Florida, Tampa, FL, USA; Department of Chemistry, University of South Florida, Tampa, FL, USA. Electronic address: sehill2@usf.edu.
Priyanshi ParikhByrd Alzheimer's Center and Research Institute, Tampa, FL, USA; Department of Molecular Medicine, University of South Florida, Tampa, FL, USA.
Niat T GebruByrd Alzheimer's Center and Research Institute, Tampa, FL, USA; Department of Molecular Medicine, University of South Florida, Tampa, FL, USA.
Sanam BanjadeDepartment of Chemistry, University of South Florida, Tampa, FL, USA.
Jennifer GuerguesDepartment of Molecular Biosciences, University of South Florida, Tampa, FL, USA.
Jessica WohlfahrtDepartment of Molecular Biosciences, University of South Florida, Tampa, FL, USA.
Stanley M StevensDepartment of Molecular Biosciences, University of South Florida, Tampa, FL, USA.
Laura J BlairByrd Alzheimer's Center and Research Institute, Tampa, FL, USA; Department of Molecular Medicine, University of South Florida, Tampa, FL, USA; Research & Development, James A. Haley Veterans Hospital, Tampa, FL, USA. Electronic address: laurablair@usf.edu.

Funding

The Hsp90 cochaperone FKBP51 regulates tau structure and functionR01NS073899 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI Laura J Blair · 2011 to 2026
$6.9M
BLRD VA I01 BX004626NINDS NIH HHS R01 NS073899
6 · The paper itself

Abstract

The 51 kDa FK506-binding protein (FKBP51) has been studied for its involvement in regulating multiple biological systems, particularly as a regulator of steroid hormone receptors, but roles in metabolism, pain response, cell survival, protein turnover, autophagy, immune response, and insulin signaling have also been described. Genetic variants of FKBP51 are associated with various stress-related mental disorders. While recent research has clarified aspects of these processes, the complete range of FKBP51 interactions remains undetermined. FKBP52, a closely related homolog, also affects similar pathways. Recent studies have identified new protein partners for FKBP51 and FKBP52, suggesting an even broader interactome with transient associations. To further characterize interactions, TurboID-based proximity labeling was performed in HeLa cells. Proteomic analysis confirmed known FKBP51 and FKBP52 interactions, while also identifying additional shared and unique binding partners with strong enrichment in metabolic pathways, amino acid biosynthesis, and carbon metabolism. Although FKBP51 and FKBP52 proximal proteins were primarily cytosolic, FKBP51 showed additional associations with exosomal proteins while FKBP52 engaged with additional nuclear proteins. These findings highlight the overlapping roles in metabolic signaling and differentiate pathway-specific partners.

Indexed as

Metabolic Networks and PathwaysProtein Interaction MappingTacrolimus Binding ProteinsHeLa CellsHumansProtein BindingProteomicsTacrolimus Binding Protein 5tacrolimus binding protein 4Tacrolimus Binding Protein 5Tacrolimus Binding ProteinsFK506-Binding proteinFKBP51FKBP52Hsp90 co-chaperoneInteractomeMass spectrometryMetabolic pathwaysMolecular chaperonesProximity labelingTurboID

Identifiers

PMID42190603
PMCPMC13568283

What OpenQuestion holds

Textmetadata
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.