p47 is a cofactor for p97-mediated membrane fusion View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-07

AUTHORS

Hisao Kondo, Catherine Rabouille, Richard Newman, Timothy P. Levine, Darryl Pappin, Paul Freemont, Graham Warren

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 compartments. The NSF-mediated fusion pathway is the best characterized, many of the components having been identified and their functions analysed. In contrast, none of the accessory proteins for the p97-mediated fusion pathway has been identified. 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 cells. 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 karyogamy. More... »

PAGES

75-78

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

6637

VOLUME

388

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/40411

DOI

http://dx.doi.org/10.1038/40411

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010703254

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9214505


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