Evidence map›Paper›PMID 10490616›Full record

ArticleMolecular and cellular biology1999

Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae.

D J Bartels, D A Mitchell, X Dong, R J Deschenes

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

94 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
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  3. Article
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  6. Article
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  8. Open biology · 2022
    Review
  9. Review
  10. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  11. Article
  12. Article
  13. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  14. Review
  15. Review
  16. Regulation of large and small G proteins by ubiquitination.The Journal of biological chemistry · 2019
    Review
  17. Review
  18. Article
  19. Review
  20. Review

34 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

D J BartelsDepartment of Biochemistry, University of Iowa, Iowa City, Iowa 52242, USA.
D A Mitchell
X Dong
R J Deschenes
University of Iowa · US

Funding

STRUCTURAL CHANGES AND THE FUNCTION OF RAS ONCOGENESR01CA050211 · NCI · UNIVERSITY OF SOUTH FLORIDA · PI DESCHENES, ROBERT J · 1990 to 2010
$2.2M
NCI NIH HHS CA50211NCI NIH HHS R01 CA050211
6 · The paper itself

Abstract

Plasma membrane localization of Ras requires posttranslational addition of farnesyl and palmitoyl lipid moieties to a C-terminal CaaX motif (C is cysteine, a is any aliphatic residue, X is the carboxy terminal residue). To better understand the relationship between posttranslational processing and the subcellular localization of Ras, a yeast genetic screen was undertaken based on the loss of function of a palmitoylation-dependent RAS2 allele. Mutations were identified in an uncharacterized open reading frame (YLR246w) that we have designated ERF2 and a previously described suppressor of hyperactive Ras, SHR5. ERF2 encodes a 41-kDa protein with four predicted transmembrane (TM) segments and a motif consisting of the amino acids Asp-His-His-Cys (DHHC) within a cysteine-rich domain (CRD), called DHHC-CRD. Mutations within the DHHC-CRD abolish Erf2 function. Subcellular fractionation and immunolocalization experiments reveal that Erf2 tagged with a triply iterated hemagglutinin epitope is an integral membrane protein that colocalizes with the yeast endoplasmic reticulum marker Kar2. Strains lacking ERF2 are viable, but they have a synthetic growth defect in the absence of RAS2 and partially suppress the heat shock sensitivity resulting from expression of the hyperactive RAS2(V19) allele. Ras2 proteins expressed in an erf2Delta strain have a reduced level of palmitoylation and are partially mislocalized to the vacuole. Based on these observations, we propose that Erf2 is a component of a previously uncharacterized Ras subcellular localization pathway. Putative members of an Erf2 family of proteins have been uncovered in yeast, plant, worm, insect, and mammalian genome databases, suggesting that Erf2 plays a role in Ras localization in all eucaryotes.

Indexed as

GTP-Binding Protein alpha SubunitsProtein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsAcyltransferasesAmino Acid SequenceBiological TransportCell CompartmentationFungal ProteinsGene DeletionHeat-Shock ResponseHeterotrimeric GTP-Binding ProteinsMembrane ProteinsMolecular Sequence DataMutationPalmitic AcidProtein Structure, TertiaryAcyltransferasesERF2 protein, S cerevisiaeFungal ProteinsGpa2 protein, S cerevisiaeGTP-Binding Protein alpha SubunitsHeterotrimeric GTP-Binding ProteinsMembrane ProteinsPalmitic AcidRAS2 protein, S cerevisiaeras ProteinsRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10490616
PMCPMC84674
OpenAlexW2168457547

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.