Evidence map›Paper›PMID 21454883›Full record

ArticleMolecular & cellular proteomics : MCP2011

A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae.

Svetlana Dokudovskaya, Francois Waharte, Avner Schlessinger, Ursula Pieper, Damien P Devos, Ileana M Cristea, Rosemary Williams, Jean Salamero, Brian T Chait, Andrej Sali and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 2 pooled it
6.5field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 2 syntheses or guidelines pooled it, 143 citations in OpenAlex.

  1. Guideline
  2. Guideline
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. The 50-nm Free Vesicles Visible inCurrent issues in molecular biology · 2025
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Wdr59 promotes or inhibits TORC1 activity depending on cellular context.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Coatomer in the universe of cellular complexity.Molecular biology of the cell · 2022
    Article
  20. Article

34 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

13 authors at 7 institutions in 4 countries.

Svetlana DokudovskayaInstitut Jacques Monod, CNRS UMR 7592, Bâtiment Buffon, Paris, France. svetlana.dokudovskaya@igr.fr
Francois Waharte
Avner Schlessinger
Ursula Pieper
Damien P Devos
Ileana M Cristea
Rosemary Williams
Jean Salamero
Brian T Chait
Andrej Sali
Mark C Field
Michael P Rout
Catherine Dargemont
New York Structural Biology Center · USEuropean Molecular Biology Organization · DEInstitut Jacques Monod · FRPrinceton University · USRockefeller University · USUniversité Paris Cité · FRUniversity of Cambridge · GB

Funding

NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
YNG1 PHD BINDING TO H3 3METHYL AT K4 PROMOTES TRANSCRIPTION AT TARGETED ORFSP41RR000862 · NCRR · ROCKEFELLER UNIVERSITY · PI DARNELL, JAMES E · 1985 to 2011
$16.1M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
Proteomic Tools to Uncover the Role of Chromatin Remodeling in HIV-1 InfectionDP1DA026192 · NIDA · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2008 to 2012
$3.9M
DISSECTING THE MOLECULAR MACHINERY OF NUCLEAR TRANSPORTR01GM062427 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2001 to 2010
$2.7M
Protein Modeling by Satisfaction of Spatial RestraintsR01GM054762 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2001 to 2008
$2.1M
Description of substrate specificity determinants in Solute Carrier TransportersF32GM088991 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SCHLESSINGER, AVNER · 2010 to 2011
$104k
NCRR NIH HHS P41 RR000862NCRR NIH HHS RR00862NCRR NIH HHS U54 RR022220NIDA NIH HHS DP1 DA026192NIDA NIH HHS DP1DA026192NIGMS NIH HHS F32 GM088991NIGMS NIH HHS F32 GM088991-01A1NIGMS NIH HHS R01 GM054762NIGMS NIH HHS R01 GM062427NIGMS NIH HHS R01 GM083960NIGMS NIH HHS R01 GM54762NIGMS NIH HHS R01 GM62427Wellcome Trust 090007
6 · The paper itself

Abstract

The presence of multiple membrane-bound intracellular compartments is a major feature of eukaryotic cells. Many of the proteins required for formation and maintenance of these compartments share an evolutionary history. Here, we identify the SEA (Seh1-associated) protein complex in yeast that contains the nucleoporin Seh1 and Sec13, the latter subunit of both the nuclear pore complex and the COPII coating complex. The SEA complex also contains Npr2 and Npr3 proteins (upstream regulators of TORC1 kinase) and four previously uncharacterized proteins (Sea1-Sea4). Combined computational and biochemical approaches indicate that the SEA complex proteins possess structural characteristics similar to the membrane coating complexes COPI, COPII, the nuclear pore complex, and, in particular, the related Vps class C vesicle tethering complexes HOPS and CORVET. The SEA complex dynamically associates with the vacuole in vivo. Genetic assays indicate a role for the SEA complex in intracellular trafficking, amino acid biogenesis, and response to nitrogen starvation. These data demonstrate that the SEA complex is an additional member of a family of membrane coating and vesicle tethering assemblies, extending the repertoire of protocoatomer-related complexes.

Indexed as

AutophagyImmunoprecipitationIntracellular MembranesModels, MolecularMultiprotein ComplexesNuclear Pore Complex ProteinsPhenotypePhylogenyProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Homology, ProteinSubcellular FractionsVacuolesMultiprotein ComplexesNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsSEC13 protein, S cerevisiaeSeh1 protein, S cerevisiae

Identifiers

PMID21454883
PMCPMC3108837
OpenAlexW1984000730

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.