NSF and p97 are ATPases required for the heterotypic fusion of transport vesicles with their target membranes and the homotypic fusion of organelles. NSF uses ATP hydrolysis to dissociate NSF/SNAPs/SNAREs complexes, separating the v- and t-SNAREs, which are then primed for subsequent rounds of fusion. In contrast, p97 does not dissociate the p97/p47/SNARE complex even in the presence of ATP. Now we have identified a novel essential factor for p97/p47-mediated membrane fusion, named VCIP135 (valosin-containing protein [VCP][p97]/p47 complex-interacting protein, p135), and show that it binds to the p97/p47/syntaxin5 complex and dissociates it via p97 catalyzed ATP hydrolysis. In living cells, VCIP135 and p47 are shown to function in Golgi and ER assembly.
VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
The online version of this article contains supplemental material.
E. Jokitalo and F. Kano contributed equally to this work.
Abbreviations used in this paper: GalT, β1,4-galactosyltransferase; PDI, protein disulfide isomerase; SAND, sulfosuccinimidyl 2-[m-azio-o-nitrobenzamido]ethyl-1,3′-dithiopropionate; VCIP135, VCP(p97)/p47 complex-interacting protein, p135; VCP, valosin-containing protein.
Keiji Uchiyama, Eija Jokitalo, Fumi Kano, Masayuki Murata, Xiaodong Zhang, Benito Canas, Richard Newman, Catherine Rabouille, Darryl Pappin, Paul Freemont, Hisao Kondo; VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo . J Cell Biol 9 December 2002; 159 (5): 855–866. doi: https://doi.org/10.1083/jcb.200208112
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