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TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
Published on: May 17, 2020
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Identification of the Bok Interactome Using Proximity Labeling
Laura M Szczesniak1, Caden G Bonzerato1, Richard J H Wojcikiewicz1
1Department of Pharmacology, SUNY Upstate Medical University, Syracuse, NY, United States.
Frontiers in Cell and Developmental Biology
|June 17, 2021
Summary
The Bcl-2 family member Bok
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The precise function of Bcl-2 family member Bok remains unclear, with diverse reported roles.
- Previous studies suggest Bok's involvement in apoptosis, mitochondrial morphology, and metabolic regulation.
Purpose of the Study:
- To elucidate the functional roles of Bok by investigating its protein interactome.
- To define Bok's interactions within the cell using proximity labeling techniques.
Main Methods:
- Utilized TurboID-mediated proximity labeling in HeLa cells to identify Bok's interacting partners.
- Performed knock-out and overexpression studies to assess Bok's cellular effects.
- Compared Bok's interactome with those of Mcl-1 and Bak.
Main Results:
- Bok proximity labeling identified interactions with proteins involved in mitochondrial fission (Drp1) and ER-plasma membrane junctions (Stim1).
- Bok's interactome is largely distinct from Mcl-1 and Bak, with specific overlaps indicating key interactions.
- Overexpressed Mcl-1 and Bok exhibit physical and functional interaction dependent on Bok's transmembrane domain.
Conclusions:
- Bok's interactome differs significantly from Mcl-1 and Bak, revealing novel interaction points for Bcl-2 family members.
- Bok may regulate mitochondrial fission through interactions with Mcl-1 and Drp1.
- These findings provide new insights into the complex roles of Bcl-2 family proteins in cellular processes.
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