Evidence map›Paper›PMID 36602340›Full record

ArticleMicrobiology spectrum2023

Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function.

Rajani Ravishankar, Emily R Hildebrandt, Grace Greenway, Nadeem Asad, Sangram Gore, Timothy M Dore, Walter K Schmidt

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Rajani RavishankarDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-7605-4804
Emily R HildebrandtDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
Grace GreenwayDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
Nadeem AsadNew York University Abu Dhabi, Abu Dhabi, United Arab Emirates.
Sangram GoreNew York University Abu Dhabi, Abu Dhabi, United Arab Emirates.
Timothy M DoreNew York University Abu Dhabi, Abu Dhabi, United Arab Emirates.
Walter K SchmidtDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0002-3359-3434
University of Georgia · USNew York University Abu Dhabi · AE

Funding

Determining the scope of prenylatable protein sequencesR01GM132606 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, SCHMIDT, WALTER K · 2019 to 2022
$1.6M
Role of Proteolysis in Regulating CaaX Protein FunctionR01GM117148 · NIGMS · UNIVERSITY OF GEORGIA · PI SCHMIDT, WALTER K · 2016 to 2019
$1.2M
NIGMS NIH HHS R01 GM132606
6 · The paper itself

Abstract

Many CAAX proteins, such as Ras GTPase, undergo a series of posttranslational modifications at their carboxyl terminus (i.e., cysteine prenylation, endoproteolysis of AAX, and carboxylmethylation). Some CAAX proteins, however, undergo prenylation-only modification, such as Saccharomyces cerevisiae Hsp40 Ydj1. We previously observed that altering the CAAX motif of Ydj1 from prenylation-only to canonical resulted in altered Ydj1 function and localization. Here, we investigated the effects of a reciprocal change that altered the well-characterized canonical CAAX motif of S. cerevisiae Ras2 to prenylation-only. We observed that the type of CAAX motif impacted Ras2 protein levels, localization, and function. Moreover, we observed that using a prenylation-only sequence to stage hyperactive Ras2-G19V as a farnesylated and nonproteolyzed intermediate resulted in a different phenotype relative to staging by a genetic

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCysteineEndopeptidasesProtein Processing, Post-TranslationalProteinsProteolysisras ProteinsCysteineEndopeptidasesProteinsRAS2 protein, S cerevisiaeras ProteinsSaccharomyces cerevisiae ProteinsCAAX pathwayCAAX proteolysislipidationpalmitoylationproteolysisRasRas2Ras signalingRce1shunt pathwayyeast

Identifiers

PMID36602340
PMCPMC9927470
OpenAlexW4313546141

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.