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A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
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p97 and p47 function in membrane tethering in cooperation with FTCD during mitotic Golgi reassembly
Yayoi Kaneko1, Kyohei Shimoda1, Rafael Ayala2
1Department of Molecular Cell Biology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.
The EMBO Journal
|February 8, 2021
Summary
Formiminotransferase cyclodeaminase (FTCD) acts as a novel tethering factor. It forms a complex with p97/p47 to mediate Golgi membrane fusion and reassembly during mitosis.
Area of Science:
- Cell Biology
- Molecular Biology
- Membrane Trafficking
Background:
- p97 ATPase-mediated membrane fusion is crucial for Golgi biogenesis.
- The p97/p47 complex is involved in SNARE priming, but its tethering complex is unknown.
Purpose of the Study:
- To identify the tethering complex involved in p97/p47-mediated membrane fusion.
- To elucidate the role of novel binding partners in Golgi reassembly.
Main Methods:
- Protein-protein interaction studies to identify p47-binding proteins.
- Localization studies using immunofluorescence microscopy.
- In vivo and in vitro assays for Golgi reassembly and membrane tethering.
- Mitochondrial aggregation assays.
Main Results:
- Formiminotransferase cyclodeaminase (FTCD) was identified as a novel p47-binding protein.
- FTCD localizes to the Golgi and binds p97/p47 via polyglutamate motifs.
- FTCD facilitates p97/p47-mediated Golgi reassembly and forms a large tethering complex (FTCD-p97/p47-FTCD).
- FTCD can mediate mitochondrial aggregation, supporting its role in membrane tethering.
Conclusions:
- FTCD functions as a critical tethering factor in p97/p47-mediated Golgi membrane fusion.
- The FTCD-p97/p47-FTCD complex is essential for Golgi reassembly during mitosis.
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