Evidence map›Paper›PMID 10747090›Full record

ArticleThe Journal of cell biology2000

The role of the COOH terminus of Sec2p in the transport of post-Golgi vesicles.

N B Elkind, C Walch-Solimena, P J Novick

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. Review
  6. Article
  7. Article
  8. Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Crystal structure of the Sec4p.Sec2p complex in the nucleotide exchanging intermediate state.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  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

3 authors at 1 institution in 1 country.

N B ElkindDepartment of Cell Biology, Yale University, New Haven, Connecticut, 06510, USA.
C Walch-Solimena
P J Novick
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sec2p is required for the polarized transport of secretory vesicles in S. cerevisiae. The Sec2p NH(2) terminus encodes an exchange factor for the Rab protein Sec4p. Sec2p associates with vesicles and in Sec2p COOH-terminal mutants Sec4p and vesicles no longer accumulate at bud tips. Thus, the Sec2p COOH terminus functions in targeting vesicles, however, the mechanism of function is unknown. We found comparable exchange activity for truncated and full-length Sec2 proteins, implying that the COOH terminus does not alter the exchange rate. Full-length Sec2-GFP, similar to Sec4p, concentrates at bud tips. A COOH-terminal 58-amino acid domain is necessary but not sufficient for localization. Sec2p localization depends on actin, Myo2p and Sec1p, Sec6p, and Sec9p function. Full-length, but not COOH-terminally truncated Sec2 proteins are enriched on membranes. Membrane association of full-length Sec2p is reduced in sec6-4 and sec9-4 backgrounds at 37 degrees C but unaffected at 25 degrees C. Taken together, these data correlate loss of localization of Sec2 proteins with reduced membrane association. In addition, Sec2p membrane attachment is substantially Sec4p independent, supporting the notion that Sec2p interacts with membranes via an unidentified Sec2p receptor, which would increase the accessibility of Sec2p exchange activity for Sec4p.

Indexed as

Saccharomyces cerevisiae ProteinsActinsBiological TransportCell DivisionCell MembraneCell PolarityCytoplasmic GranulesCytoskeletonFungal ProteinsGenes, FungalGolgi ApparatusGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsKineticsPhosphorylationProtein BindingActinsFungal ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSEC2 protein, S cerevisiaeSEC4 protein, S cerevisiae

Identifiers

PMID10747090
PMCPMC2175086
OpenAlexW2129741405

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.