Evidence map›Paper›PMID 14617820›Full record

ArticleMolecular biology of the cell2004

Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway.

Seema Dalal, Meredith F N Rosser, Douglas M Cyr, Phyllis I Hanson

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

110 citing papers in PubMed, 1 synthesis or guideline pooled it, 180 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The p97 Inhibitor UPCDC-30245 Blocks Endo-Lysosomal Degradation.Pharmaceuticals (Basel, Switzerland) · 2022
    Article
  18. Probing allosteric interactions in homo-oligomeric molecular machines using solution NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Article

50 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Seema DalalWashington University School of Medicine, Department of Cell Biology and Physiology, St. Louis, Missouri 63110, USA.
Meredith F N Rosser
Douglas M Cyr
Phyllis I Hanson
University of North Carolina at Chapel Hill · USWashington University in St. Louis · US

Funding

Roles for Hsp70 and Hsp40 in Membrane Protein TriageR01GM056981 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CYR, DOUGLAS M · 1998 to 2019
$6.1M
STRUCTURE/FUNCTION OF THE SNARE COMPLEXR01NS038058 · NINDS · WASHINGTON UNIVERSITY · PI HANSON, PHYLLIS I · 1999 to 2002
$663k
Defining the Substrate Range of AAA Proteins in VivoF32NS041709 · NINDS · WASHINGTON UNIVERSITY · PI DALAL, SEEMA R · 2001 to 2003
$127k
NIGMS NIH HHS R01 GM056981NINDS NIH HHS F32 NS041709NINDS NIH HHS NS38058NINDS NIH HHS NS41709NINDS NIH HHS R01 NS038058
6 · The paper itself

Abstract

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 ATP-hydrolysis-dependent activities of NSF and p97 in the cell are not equivalent and suggest that only NSF is directly involved in regulating membrane fusion.

Indexed as

Adenosine TriphosphatasesAnimalsBrefeldin ACells, CulturedCloning, MolecularEndoplasmic ReticulumGlycosaminoglycansGolgi ApparatusGreen Fluorescent ProteinsHumansIntracellular MembranesLuminescent ProteinsMembrane FusionMicroscopy, ElectronMutationNuclear ProteinsAdenosine TriphosphatasesBrefeldin AGlycosaminoglycansGreen Fluorescent ProteinsLuminescent ProteinsNuclear Proteinsp97 ATPase

Identifiers

PMID14617820
PMCPMC329284
OpenAlexW2151540861

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.