Evidence map›Paper›PMID 11432826›Full record

ArticleThe EMBO journal2001

Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.

N J Bryant, D E James

Abstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
–field-weighted citation impact
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

54 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. CAPS and Munc13: CATCHRs that SNARE Vesicles.Frontiers in endocrinology · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Organization of SNAREs within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011
    Review
  17. Article
  18. Article
  19. 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

2 authors.

N J BryantInstitute for Molecular Biosciences, and Department of Physiology and Pharmacology, University of Queensland, St Lucia, Queensland, Australia 4072. n.bryant@imb.uq.edu.au
D E James

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sec1p-like/Munc-18 (SM) proteins bind to t-SNAREs and inhibit ternary complex formation. Paradoxically, the absence of SM proteins does not result in constitutive membrane fusion. Here, we show that in yeast cells lacking the SM protein Vps45p, the t-SNARE Tlg2p is down-regulated, to undetectable levels, by rapid proteasomal degradation. In the absence of Vps45p, Tlg2p can be stabilized through abolition of proteasome activity. Surprisingly, the stabilized Tlg2p was targeted to the correct intracellular location. However, the stabilized Tlg2p is non-functional and unable to bind its cognate SNARE binding partners, Tlg1p and Vti1p, in the absence of Vps45p. A truncation mutant lacking the first 230 residues of Tlg2p no longer bound Vps45p but was able to form complexes with Tlg1p and Vti1p in the absence of the SM protein. These data provide us with two valuable insights into the function of SM proteins. First, SM proteins act as chaperone-like molecules for their cognate t-SNAREs. Secondly, SM proteins play an essential role in the activation process allowing their cognate t-SNARE to participate in ternary complex formation.

Indexed as

Membrane Transport ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsCarrier ProteinsCell MembraneCysteine EndopeptidasesFungal ProteinsGenotypeMembrane ProteinsMultienzyme ComplexesOpen Reading FramesProteasome Endopeptidase ComplexProtein TransportQa-SNARE ProteinsQb-SNARE ProteinsRecombinant ProteinsCarrier ProteinsCysteine EndopeptidasesFungal ProteinsMembrane ProteinsMembrane Transport ProteinsMultienzyme ComplexesProteasome Endopeptidase ComplexQa-SNARE ProteinsQb-SNARE ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsTLG2 protein, S cerevisiaeVesicular Transport ProteinsVPS45 protein, S cerevisiaeVTI1 protein, S cerevisiae

Identifiers

PMID11432826
PMCPMC125511

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.