Evidence map›Paper›PMID 21550981›Full record

ArticleThe Journal of biological chemistry2011

The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation.

Christoph T A Meiringer, Ralf Rethmeier, Kathrin Auffarth, Joshua Wilson, Angela Perz, Charles Barlowe, Hans Dieter Schmitt, Christian Ungermann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  9. Review
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  11. Review
  12. Autophagy requires Tip20 inJournal of biosciences · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016
    Review
  19. Review
  20. Article
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

8 authors at 3 institutions in 2 countries.

Christoph T A MeiringerDepartment of Biology and Chemistry, Biochemistry Section, University of Osnabrück, Barbarastrasse 13, 49076 Osnabrück, Germany.
Ralf Rethmeier
Kathrin Auffarth
Joshua Wilson
Angela Perz
Charles Barlowe
Hans Dieter Schmitt
Christian Ungermann
Osnabrück University · DEDartmouth College · USMax Planck Society · DE

Funding

Mechanisms of COPII-Dependent TransportR37GM052549 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 2007 to 2016
$5.3M
NIGMS NIH HHS R37 GM052549
6 · The paper itself

Abstract

Retrograde vesicular transport from the Golgi to the ER requires the Dsl1 tethering complex, which consists of the three subunits Dsl1, Dsl3, and Tip20. It forms a stable complex with the SNAREs Ufe1, Use1, and Sec20 to mediate fusion of COPI vesicles with the endoplasmic reticulum. Here, we analyze molecular interactions between five SNAREs of the ER (Ufe1, Use1, Sec20, Sec22, and Ykt6) and the Dsl1 complex in vitro and in vivo. Of the two R-SNAREs, Sec22 is preferred over Ykt6 in the Dsl-SNARE complex. The NSF homolog Sec18 can displace Ykt6 but not Sec22, suggesting a regulatory function for Ykt6. In addition, our data also reveal that subunits of the Dsl1 complex (Dsl1, Dsl3, and Tip20), as well as the SNAREs Ufe1 and Sec20, are ER-resident proteins that do not seem to move into COPII vesicles. Our data support a model, in which a tethering complex is stabilized at the organelle membrane by binding to SNAREs, recognizes the incoming vesicle via its coat and then promotes its SNARE-mediated fusion.

Indexed as

COP-Coated VesiclesEndoplasmic ReticulumMembrane FusionModels, BiologicalMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsDSL1 protein, S cerevisiaeMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiae ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

Identifiers

PMID21550981
PMCPMC3137077
OpenAlexW2080409718

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.