ArticleThe Journal of biological chemistry2012
The FKBP38 catalytic domain binds to Bcl-2 via a charge-sensitive loop.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Dysferlin Protein-Protein Interaction Pathways in the Organ of Corti and Spiral Ganglion Intersect with Alzheimer's Protein Pathways.International journal of molecular sciences · 2025Article
- Analysis of Dysferlin Direct Interactions with Putative Repair Proteins Links Apoptotic Signaling to CaInternational journal of molecular sciences · 2023Article
- Prohibitin regulates mTOR pathway via interaction with FKBP8.Frontiers of medicine · 2021Article
- The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer.Biomolecules · 2018Review
- FKBP8 protects the heart from hemodynamic stress by preventing the accumulation of misfolded proteins and endoplasmic reticulum-associated apoptosis in mice.Journal of molecular and cellular cardiology · 2018Article
- FKBP8 recruits LC3A to mediate Parkin-independent mitophagy.EMBO reports · 2017Article
- FK506-Binding Proteins and Their Diverse Functions.Current molecular pharmacology · 2015Review
- Direct Interaction between Ras Homolog Enriched in Brain and FK506 Binding Protein 38 in Cashmere Goat Fetal Fibroblast Cells.Asian-Australasian journal of animal sciences · 2014Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FKBP38 is a regulator of the prosurvival protein Bcl-2, but in the absence of detailed structural insights, the molecular mechanism of the underlying interaction has remained unknown. Here, we report the contact regions between Bcl-2 and the catalytic domain of FKBP38 derived by heteronuclear NMR spectroscopy. The data reveal that a previously identified charge-sensitive loop near the putative active site of FKBP38 is mainly responsible for Bcl-2 binding. The corresponding binding epitope of Bcl-2 could be identified via a peptide library-based membrane assay. Site-directed mutagenesis of the key residues verified the contact sites of this electrostatic protein/protein interaction. The derived structure model of the complex between Bcl-2 and the FKBP38 catalytic domain features both electrostatic and hydrophobic intermolecular contacts and provides a rationale for the regulation of the FKBP38/Bcl-2 interaction by Ca(2+).
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