Evidence map›Paper›PMID 15020711›Full record

ArticleMolecular biology of the cell2004

Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast.

Maddalena Pizzirusso, Amy Chang

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Protein quality control in the secretory pathway.The Journal of cell biology · 2019
    Review
  4. Article
  5. Article
  6. Article
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  8. Article
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  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Ubiquitin-dependent sorting in endocytosis.Cold Spring Harbor perspectives in biology · 2014
    Review
  17. Article
  18. Review
  19. Article
  20. Review
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.

Maddalena PizzirussoDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Amy Chang

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

Pma1-7 is a mutant plasma membrane ATPase that is impaired in targeting to the cell surface at 37 degrees C and is delivered instead to the endosomal/vacuolar pathway for degradation. We have proposed that Pma1-7 is a substrate for a Golgibased quality control mechanism. By contrast with wild-type Pma1, Pma1-7 is ubiquitinated. Ubiquitination and endosomal targeting of Pma1-7 is dependent on the Rsp5-Bul1-Bul2 ubiquitin ligase protein complex but not the transmembrane ubiquitin ligase Tul1. Analysis of Pma1-7 ubiquitination in mutants blocked in protein transport at various steps of the secretory pathway suggests that ubiquitination occurs after ER exit but before endosomal entry. In the absence of ubiquitination in rsp5-1 cells, Pma1-7 is delivered to the cell surface and remains stable. Nevertheless, Pma1-7 remains impaired in association with detergent-insoluble glycolipid-enriched complexes in rsp5-1 cells, suggesting that ubiquitination is not the cause of Pma1-7 exclusion from rafts. In vps1 cells in which protein transport into the endosomal pathway is blocked, Pma1-7 is routed to the cell surface. On arrival at the plasma membrane in vps1 cells, Pma1-7 remains stable and its ubiquitination disappears, suggesting deubiquitination activity at the cell surface. We suggest that Pma1-7 sorting and fate are regulated by ubiquitination.

Indexed as

Adaptor Proteins, Signal TransducingCell MembraneEndoplasmic ReticulumEndosomal Sorting Complexes Required for TransportEndosomesGolgi ApparatusGTP-Binding ProteinsMembrane ProteinsMutationProtein Sorting SignalsProtein TransportProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesAdaptor Proteins, Signal TransducingBUL1 protein, S cerevisiaeBUL2 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportGTP-Binding ProteinsMembrane ProteinsPMA1 protein, S cerevisiaeProtein Sorting SignalsProton-Translocating ATPasesRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTUL1 protein, S cerevisiaeUbiquitinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVesicular Transport ProteinsVPS1 protein, S cerevisiae

Identifiers

PMID15020711
PMCPMC404032

What OpenQuestion holds

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Registered trials

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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.