p47 is a cofactor for p97-mediated membrane fusion

Hisao Kondo, Catherine Rabouille, Richard Newman, Timothy P. Levine, Darryl Pappin, Paul Freemont and Graham Warren ()
Additional contact information
Hisao Kondo: *Cell Biology Laboratory Imperial Cancer Research Fund
Catherine Rabouille: *Cell Biology Laboratory Imperial Cancer Research Fund
Richard Newman: †Protein Structure Laboratory Imperial Cancer Research Fund
Timothy P. Levine: ‡MRC Laboratory of Molecular Biology
Darryl Pappin: §Protein Sequencing Laboratory, Imperial Cancer Research Fund
Paul Freemont: †Protein Structure Laboratory Imperial Cancer Research Fund
Graham Warren: *Cell Biology Laboratory Imperial Cancer Research Fund

Nature, 1997, vol. 388, issue 6637, 75-78

Abstract: Abstract At least two distinct ATPases, NSF and p97, are known to be involved in the heterotypic fusion of transport vesicles with their target membranes and the homotypic fusion of membrane compartments1. The NSF-mediated fusion pathway is the best characterized, many of the components having been identified and their functions analysed2,3,4,5,6,7. In contrast, none of the accessory proteins for the p97-mediated fusion pathway has been identified8,9,10. Now we have identified the first such component, a protein of relative molecular mass 47,000 (p47), which forms a tight, stoichiometric complex with cytosolic p97 (one trimer of p47 per hexamer of p97). It is essential for the p97-mediated regrowth of Golgi cisternae from mitotic Golgi fragments, a process restricted to animal cells11. As a homologue of p47 exists in budding yeast, this indicates that it might also be involved in other membrane fusion reactions catalysed by p97, such as karyogamy10.

Date: 1997
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/40411 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:388:y:1997:i:6637:d:10.1038_40411

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/40411

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().