Evidence map›Paper›PMID 11739407›Full record

ArticleThe Journal of cell biology2001

A t-SNARE of the endocytic pathway must be activated for fusion.

F Paumet, B Brügger, F Parlati, J A McNew, T H Söllner, J E Rothman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Article
  7. Article
  8. Organization of SNAREs within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  18. Article
  19. Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  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

6 authors at 2 institutions in 1 country.

F PaumetCellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
B Brügger
F Parlati
J A McNew
T H Söllner
J E Rothman
Memorial Sloan Kettering Cancer Center · USRice University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The t-SNARE in a late Golgi compartment (Tlg2p) syntaxin is required for endocytosis and localization of cycling proteins to the late Golgi compartment in yeast. We show here that Tlg2p assembles with two light chains, Tlg1p and Vti1p, to form a functional t-SNARE that mediates fusion, specifically with the v-SNAREs Snc1p and Snc2p. In vitro, this t-SNARE is inert, locked in a nonfunctional state, unless it is activated for fusion. Activation can be mediated by a peptide derived from the v-SNARE, which likely bypasses additional regulatory proteins in the cell. Locking t-SNAREs creates the potential for spatial and temporal regulation of fusion by signaling processes that unleash their fusion capacity.

Indexed as

Membrane Transport ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAmino Acid SequenceCarrier ProteinsEndocytosisFungal ProteinsGolgi ApparatusMembrane FusionMembrane ProteinsMolecular Sequence DataProtein TransportQa-SNARE ProteinsQb-SNARE ProteinsR-SNARE ProteinsSaccharomyces cerevisiaeCarrier ProteinsFungal ProteinsMembrane ProteinsMembrane Transport ProteinsQa-SNARE ProteinsQb-SNARE ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSNC2 protein, S cerevisiaeTLG2 protein, S cerevisiaeVesicular Transport ProteinsVTI1 protein, S cerevisiae

Identifiers

PMID11739407
PMCPMC2150898
OpenAlexW2101532102

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.