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Updated: Jun 23, 2025
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Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
Published on: June 16, 2023
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PDZD8-FKBP8 tethering complex at ER-mitochondria contact sites regulates mitochondrial complexity.
Biorxiv : the Preprint Server for Biology
|June 19, 2024
Summary
Researchers identified FKBP8 as the outer mitochondrial membrane (OMM) protein that tethers to the ER protein PDZD8, forming crucial mitochondria-ER membrane contact sites (MERCS) and regulating mitochondrial morphology.
Area of Science:
- Cell Biology
- Molecular Biology
- Mitochondrial Biology
Background:
- Mitochondria-ER membrane contact sites (MERCS) are vital for cellular biochemistry and physiology.
- The ER protein PDZD8 is essential for MERCS formation, but its mitochondrial tethering partner was unknown.
Purpose of the Study:
- To identify the outer mitochondrial membrane (OMM) protein that interacts with PDZD8.
- To elucidate the role of this interaction in MERCS formation and mitochondrial morphology.
Main Methods:
- Unbiased proximity proteomics
- CRISPR-Cas9 endogenous protein tagging
- Cryo-Electron Microscopy (Cryo-EM) tomography
- Correlative light-EM (CLEM)
- Single molecule tracking
Main Results:
- FKBP8 was identified as the OMM tethering partner of PDZD8.
- PDZD8 exhibits dynamic diffusion on the ER membrane, pausing at MERCS.
- FKBP8 modulates ER-OMM distance; both proteins are interdependent for MERCS formation.
- PDZD8 enhances mitochondrial complexity in a FKBP8-dependent manner.
Conclusions:
- A novel ER-mitochondria tethering complex involving PDZD8 and FKBP8 has been identified.
- This complex plays a critical role in regulating mitochondrial morphology in mammalian cells.
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