Syntaxin 5 Is a Common Component of the NSF- and p97-Mediated Reassembly Pathways of Golgi Cisternae from Mitotic Golgi Fragments In Vitro

Rabouille, Cathérine; Kondo, Hisao; Newman, Richard; Hui, Norman; Freemont, Paul S.; Warren, Graham

doi:10.1016/s0092-8674(00)81128-9

Cited by 244 publications

(269 citation statements)

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“…p97 participates in reassembly of ilimaquinone dispersed Golgi membranes into Golgi stacks (Acharya et al, 1995), reformation of unfenestrated Golgi cisternae from mitotic Golgi fragments (Rabouille et al, 1995(Rabouille et al, , 1998, fusion of yeast ER membranes (Latterich et al, 1995;Lin et al, 2001), formation but not maintenance of tubulated ER from low-density microsomes Roy et al, 2000), and formation and growth of the nuclear envelope and associated ER network (Hetzer et al, 2001). These in vitro assays all reconstitute complex processes related to organelle assembly.…”

Section: P97 and Membrane Fusionmentioning

confidence: 87%

“…A break in the mystery of p97's function came when it turned up as a factor involved in NSF-independent in vitro fusion between membranes of the ER (Latterich et al, 1995), mitotic Golgi fragments (Rabouille et al, 1995), ilimaquinone-generated Golgi fragments (Acharya et al, 1995), lowdensity microsomes , and fragments of the nuclear envelope (Hetzer et al, 2001). The additional finding that p97 could bind to syntaxin 5 in vitro (Rabouille et al, 1998) led to the proposal that p97 might carry out a reaction similar to the SNARE complex disassembly mediated by NSF, but on different SNAREs (Patel et al, 1998;Rabouille et al, 1998). However, although p97 has been shown to release the t-SNARE syntaxin 5 from a complex with p47 and VCIP135 (Uchiyama et al, 2002), it has so far not been found to disassemble complexes consisting of multiple SNARE proteins.…”

Section: Introductionmentioning

confidence: 99%

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Distinct Roles for the AAA ATPases NSF and p97 in the Secretory Pathway

Dalal

Rosser

Cyr

et al. 2004

MBoC

165

175

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NSF and p97 are related AAA proteins implicated in membrane trafficking and organelle biogenesis. p97 is also involved in pathways that lead to ubiquitin-dependent proteolysis, including ER-associated degradation (ERAD). In this study, we have used dominant interfering ATP-hydrolysis deficient mutants (NSF(E329Q) and p97(E578Q)) to compare the function of these AAA proteins in the secretory pathway of mammalian cells. Expressing NSF(E329Q) promotes disassembly of Golgi stacks into dispersed vesicular structures. It also rapidly inhibits glycosaminoglycan sulfation, reflecting disruption of intra-Golgi transport. In contrast, expressing p97(E578Q) does not affect Golgi structure or function; glycosaminoglycans are normally sulfated and secreted, as is the VSV-G ts045 protein. Instead, expression of p97(E578Q) causes ubiquitinated proteins to accumulate on ER membranes and slows degradation of the ERAD substrate cystic-fibrosis transmembrane-conductance regulator. In addition, expression of p97(E578Q) eventually causes the ER to swell. More specific assessment of effects of p97(E578Q) on organelle assembly shows that the Golgi apparatus disperses and reassembles normally after treatment with brefeldin A and during mitosis. These findings demonstrate that ATPhydrolysis-dependent activities of NSF and p97 in the cell are not equivalent and suggest that only NSF is directly involved in regulating membrane fusion. INTRODUCTIONMembrane fusion is an essential step in all forms of vesicle trafficking and organelle assembly. Fusion is driven by a series of regulated protein-protein interactions. Many participating proteins have been identified, and their specific roles are gradually coming to light (reviewed in Jahn et al., 2003). Among these proteins are a number of ATPases.N-ethyl maleimide sensitive factor (NSF) was one of the first proteins specifically linked to membrane fusion (Wilson et al., 1989). It belongs to a family of chaperone-like ATPases known as AAA (ATPases associated with a variety of cellular activities) proteins (Neuwald et al., 1999). NSF together with ␣-SNAP (soluble NSF attachment protein) dissociates the SNARE (SNAP receptor) complexes that promote association and fusion of cellular membranes. More recently, NSF has also been implicated in other cellular processes on the basis of its ability to bind the AMPA receptor GluR2, ␤-arrestin 1, and GATE-16 (reviewed in Whiteheart et al., 2001). However, its role in SNARE disassembly and membrane fusion remains its best understood function.Not all ATP-requiring steps that lead to membrane fusion can be attributed to NSF (Goda and Pfeffer, 1991;Latterich and Schekman, 1994;Rodriguez et al., 1994;Wilson, 1995).Other ATPases must therefore be involved. One AAA protein thought to be an alternate to NSF is known as p97 (also referred to as valosin-containing protein, VCP). p97 is an abundant and highly conserved protein (Peters et al., 1990) whose cellular function has been the subject of much debate. A break in the mystery of p97's function came when it turn...

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Section: P97 and Membrane Fusionmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Distinct Roles for the AAA ATPases NSF and p97 in the Secretory Pathway

Dalal

Rosser

Cyr

et al. 2004

MBoC

165

175

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“…However, it has been recently reported that ERresident mannosidase I is regulated by proteolysis mediated by the lysosomal compartment [52]. Since VCP is required for homotypic vesicle fusion in the ER and Golgi [53,54], VCP depletion likely diminishes the traffic of ER proteins to lysosomes providing an alternative explanation to increased levels of demannosylation of N-glycans in the absence of any direct effect of VCP on ERAD.…”

Section: Discussionmentioning

confidence: 99%

“…Those changes may either reflect the different abundance of coreglycosylated precursors trafficked from the ER or -alternatively -they may indicate that VCP controls different aspects of glycosylation, for example the regulated degradation of glycosylation enzymes within a lysosomal compartment [52]. The latter possibility is supported by the fact that VCP is the major ATP-ase associated with transitional ER and the Golgi involved in homotypic membrane fusion within that compartment [53,54]. Depletion of VCP by RNAi may therefore affect the distribution of different glycosylation enzymes within cis, medial and trans cisternae of the Golgi apparatus.…”

Section: Discussionmentioning

confidence: 99%

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum

Lass

McConnell

Nowis

et al. 2007

Archives of Biochemistry and Biophysics

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Summaryα chain of T-cell receptor (TCR) is a typical ERAD (ER-associated degradation) substrate degraded in the absence of other TCR subunits. Depletion of derlin1 fails to induce accumulation of αTCR despite inducing accumulation of α1-antitrypsin, another ERAD substrate. Furthermore, while depletion of VCP does not affect levels of α1-antitrypsin, it induces an increase in levels of αTCR. RNAi of VCP induces preferential accumulation of αTCR with less mannose residues, suggesting its retention within the ER. Mass spectrometric analysis of cellular N-linked glycans revealed that depletion of VCP decreases the level of high mannose glycoproteins, increases the levels of truncated low-mannose glycoproteins and induces changes in the abundance of complex glycans assembled in post-ER compartments. Since proteasome inhibition was unable to mimic those changes, they can not be regarded as a simple consequence of inhibited ERAD but represent a complex effect of VCP on the function of the ER.

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“…VCP has been associated with several essential cell protein pathways 11 : cell cycle, homotypic membrane fusion, nuclear envelope reconstruction, postmitotic Golgi reassembly, DNA damage response, suppressor of apoptosis and ubiquitin-dependent protein degradation [12][13][14][15][16][17][18] . VCP also binds to expanded polyglutamine (poly-Q) protein aggregates 18,19 .…”

mentioning

confidence: 99%

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

et al. 2004

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Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia (IBMPFD) is a dominant progressive disorder that maps to chromosome 9p21.1-p12. We investigated 13 families with IBMPFD linked to chromosome 9 using a candidate-gene approach. We found six missense mutations in the gene encoding valosincontaining protein (VCP, a member of the AAA-ATPase superfamily) exclusively in all 61 affected individuals. Haplotype analysis indicated that descent from two founders in two separate North American kindreds accounted for IBMPFD in ~50% of affected families. VCP is associated with a variety of cellular activities, including cell cycle control, membrane fusion and the ubiquitin-proteasome degradation pathway. Identification of VCP as causing IBMPFD has important implications for other inclusion-body diseases, including myopathies, dementias and Paget disease of bone (PDB), as it may define a new common pathological ubiquitin-based pathway.Hereditary inclusion body myopathy (IBM) associated with PDB and frontotemporal dementia (FTD), or IBMPFD, is a rare, complex and ultimately lethal autosomal dominant disorder (OMIM 605382; ref. 1). IBMPFD features adult-onset proximal and distal muscle weakness (clinically resembling limb girdle muscular dystrophy), early-onset PDB in most cases and 'premature' FTD 2 . Although the disorder was mapped to chromosome 9p21-p12, the genetic basis was not known.Within 13 families (12 from the United States and 1 from Canada, Fig. 1 and Supplementary Fig. 1 online), 82% of individuals had myopathy, 49% had PDB and 30% had early-onset FTD. The mean age of presentation was 42 years for both IBM and PDB, whereas FTD typically presented at age 53 years. In IBMPFD myopathic muscle and PDB osteoclasts, inclusions appear similar, suggestive of disruptions in the same pathological pathway.Haplotype analysis of the families with IBMPFD identified two ancestral, disease-associated haplotypes, distinguishing families 1, 3, 7 and 16 (group A) from families 2 and 5 (group B), both groups of Northern European ancestry ( Table 1

show abstract

Syntaxin 5 Is a Common Component of the NSF- and p97-Mediated Reassembly Pathways of Golgi Cisternae from Mitotic Golgi Fragments In Vitro

Cited by 244 publications

References 61 publications

Distinct Roles for the AAA ATPases NSF and p97 in the Secretory Pathway

Distinct Roles for the AAA ATPases NSF and p97 in the Secretory Pathway

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

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