Evidence map›Paper›PMID 23625923›Full record

ArticleThe Journal of biological chemistry2013

Tiered assembly of the yeast Far3-7-8-9-10-11 complex at the endoplasmic reticulum.

Tammy Pracheil, Zhengchang Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. STRIP1, a core component of STRIPAK complexes, is essential for normal mesoderm migration in the mouse embryo.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Article
  19. Article
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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 at 1 institution in 1 country.

Tammy PracheilDepartment of Biological Sciences, University of New Orleans, New Orleans, Louisiana 70148.
Zhengchang LiuDepartment of Biological Sciences, University of New Orleans, New Orleans, Louisiana 70148. Electronic address: zliu5@uno.edu.
University of New Orleans · US

Funding

Amino Acid Sensing and Signaling in YeastR15GM094772 · NIGMS · UNIVERSITY OF NEW ORLEANS · PI LIU, ZHENGCHANG · 2011 to 2011
$284k
NIGMS NIH HHS 1R15GM094772-01A1NIGMS NIH HHS R15 GM094772
6 · The paper itself

Abstract

Target of rapamycin signaling is a conserved, essential pathway integrating nutritional cues with cell growth and proliferation. The target of rapamycin kinase exists in two distinct complexes, TORC1 and TORC2. It has been reported that protein phosphatase 2A (PP2A) and the Far3-7-8-9-10-11 complex (Far complex) negatively regulate TORC2 signaling in yeast. The Far complex, originally identified as factors required for pheromone-induced cell cycle arrest, and PP2A form the yeast counterpart of the STRIPAK complex, which was first isolated in mammals. The cellular localization of the Far complex has yet to be fully characterized. Here, we show that the Far complex localizes to the endoplasmic reticulum (ER) by analyzing functional GFP-tagged Far proteins in vivo. We found that Far9 and Far10, two homologous proteins each with a tail-anchor domain, localize to the ER in mutant cells lacking the other Far complex components. Far3, Far7, and Far8 form a subcomplex, which is recruited to the ER by Far9/10. The Far3-7-8- complex in turn recruits Far11 to the ER. Finally, we show that the tail-anchor domain of Far9 is required for its optimal function in TORC2 signaling. Our study reveals tiered assembly of the yeast Far complex at the ER and a function for Far complex's ER localization in TORC2 signaling.

Indexed as

Cell Cycle ProteinsEndoplasmic ReticulumMechanistic Target of Rapamycin Complex 2Multiprotein ComplexesMutationProtein Phosphatase 2Protein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTOR Serine-Threonine KinasesTranscription FactorsCell Cycle ProteinsFAR11 protein, S cerevisiaeFAR3 protein, S cerevisiaeFAR7 protein, S cerevisiaeFAR9 protein, S cerevisiaeMechanistic Target of Rapamycin Complex 2Multiprotein ComplexesProtein Phosphatase 2Saccharomyces cerevisiae ProteinsTORC1 protein complex, S cerevisiaeTOR Serine-Threonine KinasesTranscription FactorsEndoplasmic Reticulum (ER)Far3-7-8-9-10-11PP2AProtein ComplexesSaccharomyces cerevisiaeSTRIPAK ComplexTail-anchored ProteinsTORC2 SignalingTOR Complex (TORC)Yeast

Identifiers

PMID23625923
PMCPMC3675630
OpenAlexW1979819188

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.