Evidence map›Paper›PMID 19114459›Full record

ArticleGenetics2009

A mutant plasma membrane protein is stabilized upon loss of Yvh1, a novel ribosome assembly factor.

Yu Liu, Amy Chang

Abstract read
In one paragraph

Article in Genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. 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.

Yu LiuDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, 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
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NIGMS NIH HHS GM 58212NIGMS NIH HHS R01 GM058212
6 · The paper itself

Abstract

Pma1-10 is a mutant plasma membrane ATPase defective at the restrictive temperature in stability at the cell surface. At 37 degrees, Pma1-10 is ubiquitinated and internalized from the plasma membrane for degradation in the vacuole. YVH1, encoding a tyrosine phosphatase, is a mutant suppressor of pma1-10; in the absence of Yvh1, Pma1-10 remains stable at the plasma membrane, thereby permitting cells to grow. The RING finger domain of Yvh1, but not its phosphatase domain, is required for removal of mutant Pma1-10 from the plasma membrane. Yvh1 is a novel ribosome assembly factor: in yvh1Delta cells, free 60S and 80S ribosomal subunits are decreased, free 40S subunits are increased, and half-mer polysomes are accumulated. Pma1-10 is also stabilized by deletion of 60S ribosomal proteins Rpl19a and Rpl35a. We propose that changes in ribosome biogenesis caused by loss of Yvh1 or specific ribosomal proteins have effects on the plasma membrane, perhaps by producing specific translational changes.

Indexed as

MutationDual-Specificity PhosphatasesMutant ProteinsProtein StabilityProtein Structure, TertiaryProton-Translocating ATPasesRibosomal ProteinsRibosomesRibosome Subunits, Large, EukaryoticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDual-Specificity PhosphatasesMutant ProteinsPMA1 protein, S cerevisiaeProton-Translocating ATPasesRibosomal ProteinsSaccharomyces cerevisiae ProteinsYVH1 protein, S cerevisiae

Identifiers

PMID19114459
PMCPMC2651063

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.