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p47 is a cofactor for p97-mediated membrane fusion
H Kondo1, C Rabouille, R Newman
1Cell Biology Laboratory, Imperial Cancer Research Fund, London, UK.
Nature
|July 3, 1997
Summary
Researchers identified p47, the first accessory protein for the p97 ATPase pathway, crucial for Golgi regrowth in animal cells. This discovery suggests p47 may also mediate other p97-driven membrane fusion events, like yeast karyogamy.
Area of Science:
- Cell Biology
- Molecular Biology
- Membrane Trafficking
Background:
- Two main ATPases, NSF and p97, mediate membrane fusion events like vesicle transport and compartment fusion.
- The NSF-mediated fusion pathway is well-understood, but accessory proteins for p97-mediated fusion remain unidentified.
Purpose of the Study:
- To identify accessory proteins involved in the p97-mediated membrane fusion pathway.
- To characterize the function of newly identified components in cellular processes.
Main Methods:
- Biochemical complex formation analysis between p97 and potential accessory proteins.
- Functional assays investigating the role of identified proteins in Golgi regrowth and membrane fusion.
Main Results:
- Identification of p47 as the first accessory protein for p97, forming a stoichiometric complex (one p47 trimer per p97 hexamer).
- p47 is essential for the p97-mediated regrowth of Golgi cisternae from mitotic Golgi fragments in animal cells.
- Homolog of p47 found in yeast suggests a conserved role in p97-catalyzed fusion.
Conclusions:
- p47 is the first identified accessory protein for the p97 ATPase in membrane fusion.
- p47 plays a critical role in Golgi reassembly post-mitosis, a process specific to animal cells.
- The existence of a p47 homolog in yeast implies its involvement in other p97-mediated fusion processes, including karyogamy.