Evidence map›Paper›PMID 12475964›Full record

ArticleMolecular biology of the cell2002

Requirement of the N-terminal extension for vacuolar trafficking and transport activity of yeast Ycf1p, an ATP-binding cassette transporter.

Deborah L Mason, Susan Michaelis

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 19% 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, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Cadmium transport by mammalian ATP-binding cassette transporters.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Review
  4. Review
  5. Structure of Ycf1p reveals the transmembrane domain TMD0 and the regulatory region of ABCC transporters.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
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  9. Article
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  11. Article
  12. Article
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  14. Article
  15. Plant ABC Transporters.The arabidopsis book · 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.

Deborah L MasonDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Susan Michaelis
Johns Hopkins University · US

Funding

FOLDING AND ACTIVITY OF ABC PROTEINS IN YEASTR01DK058029 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MICHAELIS, SUSAN D. · 1999 to 2002
$661k
NIDDK NIH HHS DK-58029NIDDK NIH HHS R01 DK058029
6 · The paper itself

Abstract

Ycf1p is the prototypical member of the yeast multidrug resistance-associated protein (MRP) subfamily of ATP-binding cassette (ABC) transporters. Ycf1p resides in the vacuolar membrane and mediates glutathione-dependent transport processes that result in resistance to cadmium and other xenobiotics. A feature common to many MRP proteins that distinguishes them from other ABC transporters is the presence of a hydrophobic N-terminal extension (NTE), whose function is not clearly established. The NTE contains a membrane spanning domain (MSD0) with five transmembrane spans and a cytosolic linker region (L0). The goal of this study was to determine the functional significance of the NTE of Ycf1p by examining the localization and functional properties of Ycf1p partial molecules, expressed either singly or together. We show that MSD0 plays a critical role in the vacuolar membrane trafficking of Ycf1p, whereas L0 is dispensable for localization. On the other hand, L0 is required for transport function, as determined by monitoring cadmium resistance. We also examine an unusual aspect of Ycf1p biology, namely, the posttranslational proteolytic processing that occurs within a lumenal loop of Ycf1p. Processing is shown to be Pep4p dependent and thus serves as a convenient marker for proper vacuolar localization. The processed fragments associate with each other, suggesting that these natural cleavage products contribute together to Ycf1p function.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAspartic Acid EndopeptidasesATP-Binding Cassette TransportersCadmiumCell MembraneCycloheximideGenotypeGreen Fluorescent ProteinsHumansImmunoblottingLuminescent ProteinsMicroscopy, FluorescenceModels, BiologicalMolecular Sequence DataPlasmidsAdenosine TriphosphateAspartic Acid Endopeptidasesaspartic proteinase AATP-Binding Cassette TransportersCadmiumCycloheximideGreen Fluorescent ProteinsLuminescent ProteinsPEP4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsYCF1 protein, S cerevisiae

Identifiers

PMID12475964
PMCPMC138645
OpenAlexW2130417781

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.