Evidence map›Paper›PMID 11481477›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface.

X Gong, A Chang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Protein homeostasis at the plasma membrane.Physiology (Bethesda, Md.) · 2014
    Review
  11. Review
  12. Article
  13. Article
  14. Protein quality control at the plasma membrane.Current opinion in cell biology · 2011
    Review
  15. pH-dependent cargo sorting from the Golgi.The Journal of biological chemistry · 2011
    Article
  16. 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

2 authors at 1 institution in 1 country.

X GongDepartments of Anatomy and Structural Biology, and Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
A Chang
Albert Einstein College of Medicine · US

Funding

TRAFFICKING PATHWAYS TO THE CELL SURFACE IN YEASTR01GM058212 · NIGMS · YESHIVA UNIVERSITY · PI CHANG, AMY Y · 1999 to 2009
$2.4M
TRAFFICKING PATHWAYS TO THE CELL SURFACE IN YEASTR55GM058212 · NIGMS · YESHIVA UNIVERSITY · PI CHANG, AMY Y · 1998 to 1998
–
NIGMS NIH HHS GM 58212NIGMS NIH HHS R01 GM058212
6 · The paper itself

Abstract

Pma1 is a plasma membrane H(+)-ATPase whose activity at the cell surface is essential for cell viability. In this paper we describe a temperature-sensitive pma1 allele, pma1-10 (with two point mutations in the first cytoplasmic loop of Pma1), in which the newly synthesized mutant protein fails to remain stable at the cell surface at 37 degrees C. Instead, Pma1-10 appears to undergo internalization for vacuolar degradation in a manner dependent on End4, Vps27, Doa4, and Pep4. By contrast with wild-type Pma1, mutant Pma1-10 is hypophosphorylated and fails to associate with a Triton-insoluble fraction at 37 degrees C, suggesting failure to enter lipid rafts. Kinetic analysis reveals that, at the permissive temperature, newly synthesized Pma1-10 acquires Triton-insolubility before becoming stabilized. We suggest that phosphorylation and lipid raft association may play important roles in maintaining protein stability at the plasma membrane.

Indexed as

Saccharomyces cerevisiae ProteinsCell MembraneEnzyme StabilityFluorescent Antibody Technique, IndirectHydrolysisOctoxynolPhosphorylationProton-Translocating ATPasesSaccharomyces cerevisiaeVacuolesOctoxynolPMA1 protein, S cerevisiaePMA2 protein, S cerevisiaeProton-Translocating ATPasesSaccharomyces cerevisiae Proteins

Identifiers

PMID11481477
PMCPMC55380
OpenAlexW2080942166

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.