VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo

نویسندگان

  • Keiji Uchiyama
  • Eija Jokitalo
  • Fumi Kano
  • Masayuki Murata
  • Xiaodong Zhang
  • Benito Canas
  • Richard Newman
  • Catherine Rabouille
  • Darryl Pappin
  • Paul Freemont
  • Hisao Kondo
چکیده

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.

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VCIP135 deubiquitinase and its binding protein, WAC, in p97ATPase-mediated membrane fusion.

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p97/p47-Mediated biogenesis of Golgi and ER.

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Cell cycle regulation of VCIP135 deubiquitinase activity and function in p97/p47-mediated Golgi reassembly

In mammalian cells, the inheritance of the Golgi apparatus into the daughter cells during each cycle of cell division is mediated by a disassembly and reassembly process, and this process is precisely controlled by phosphorylation and ubiquitination. VCIP135 (valosin-containing protein p97/p47 complex-interacting protein, p135), a deubiquitinating enzyme required for p97/p47-mediated postmitoti...

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عنوان ژورنال:
  • The Journal of Cell Biology

دوره 159  شماره 

صفحات  -

تاریخ انتشار 2002