Evidence map›Paper›PMID 11950929›Full record

ArticleMolecular biology of the cell2002

Yeast genes controlling responses to topogenic signals in a model transmembrane protein.

Donald J Tipper, Carol A Harley

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. The structure and function of P5A-ATPases.Nature communications · 2024
    Article
  4. Review
  5. Review
  6. Article
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  8. Abolishing the prelamin A ZMPSTE24 cleavage site leads to progeroid phenotypes with near-normal longevity in mice.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.Acta crystallographica. Section D, Structural biology · 2018
    Article
  15. Article
  16. Article
  17. Inhibition of the Formation of the Spf1p Phosphoenzyme by Ca2.The Journal of biological chemistry · 2016
    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 at 1 institution in 1 country.

Donald J TipperDepartment of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655, USA. donald.tipper@umassmed.edu
Carol A Harley
University of Massachusetts Chan Medical School · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast protein insertion orientation (PIO) mutants were isolated by selecting for growth on sucrose in cells in which the only source of invertase is a C-terminal fusion to a transmembrane protein. Only the fraction with an exocellular C terminus can be processed to secreted invertase and this fraction is constrained to 2-3% by a strong charge difference signal. Identified pio mutants increased this to 9-12%. PIO1 is SPF1, encoding a P-type ATPase located in the endoplasmic reticulum (ER) or Golgi. spf1-null mutants are modestly sensitive to EGTA. Sensitivity is considerably greater in an spf1 pmr1 double mutant, although PIO is not further disturbed. Pmr1p is the Golgi Ca(2+) ATPase and Spf1p may be the equivalent ER pump. PIO2 is STE24, a metalloprotease anchored in the ER membrane. Like Spf1p, Ste24p is expressed in all yeast cell types and belongs to a highly conserved protein family. The effects of ste24- and spf1-null mutations on invertase secretion are additive, cell generation time is increased 60%, and cells become sensitive to cold and to heat shock. Ste24p and Rce1p cleave the C-AAX bond of farnesylated CAAX box proteins. The closest paralog of SPF1 is YOR291w. Neither rce1-null nor yor291w-null mutations affected PIO or the phenotype of spf1- or ste24-null mutants. Mutations in PIO3 (unidentified) cause a weaker Pio phenotype, enhanced by a null mutation in BMH1, one of two yeast 14-3-3 proteins.

Indexed as

Saccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesAdenosine Triphosphatasesbeta-Fructofuranosidasebeta-Galactosidasebeta-LactamasesCell MembraneDNA-Binding ProteinsEthyl MethanesulfonateFungal ProteinsGene LibraryGenes, ReporterGenetic Complementation TestGenetic VectorsGlycoside HydrolasesLigasesAdenosine Triphosphatasesbeta-Fructofuranosidasebeta-Galactosidasebeta-LactamasesDNA-Binding ProteinsEthyl MethanesulfonateFungal ProteinsGlycoside HydrolasesLigasesMembrane ProteinsMetalloendopeptidasesMutagensPlant ProteinsProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSPF1 protein, plantSTE24 protein, S cerevisiaeUBE2L3 protein, humanUbiquitin-Conjugating Enzymes

Identifiers

PMID11950929
PMCPMC102259
OpenAlexW2119055072

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.