Evidence map›Paper›PMID 18809726›Full record

ArticleThe Journal of cell biology2008

Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase.

Christopher L Brett, Rachael L Plemel, Braden T Lobingier, Braden T Lobinger, Marissa Vignali, Stanley Fields, Alexey J Merz

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

93 citing papers in PubMed, 149 citations in OpenAlex.

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  13. PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023
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  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
    Lobinger, Braden T [corrected to Lobingier, Braden T]
5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Christopher L BrettDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Rachael L Plemel
Braden T Lobingier
Braden T Lobinger
Marissa Vignali
Stanley Fields
Alexey J Merz
Laboratoire de Biochimie · FRHuman Genome Sciences (United States) · USUniversity of Washington · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR011823NCRR NIH HHS P41 RR11823NIGMS NIH HHS GM077349NIGMS NIH HHS R01 GM077349
6 · The paper itself

Abstract

Rab guanosine triphosphatases (GTPases) are pivotal regulators of membrane identity and dynamics, but the in vivo pathways that control Rab signaling are poorly defined. Here, we show that the GTPase-activating protein Gyp7 inactivates the yeast vacuole Rab Ypt7 in vivo. To efficiently terminate Ypt7 signaling, Gyp7 requires downstream assistance from an inhibitory casein kinase I, Yck3. Yck3 mediates phosphorylation of at least two Ypt7 signaling targets: a tether, the Vps-C/homotypic fusion and vacuole protein sorting (HOPS) subunit Vps41, and a SNARE, Vam3. Phosphorylation of both substrates is opposed by Ypt7-guanosine triphosphate (GTP). We further demonstrate that Ypt7 binds not one but two Vps-C/HOPS subunits: Vps39, a putative Ypt7 nucleotide exchange factor, and Vps41. Gyp7-stimulated GTP hydrolysis on Ypt7 therefore appears to trigger both passive termination of Ypt7 signaling and active kinase-mediated inhibition of Ypt7's downstream targets. We propose that signal propagation through the Ypt7 pathway is controlled by integrated feedback and feed-forward loops. In this model, Yck3 enforces a requirement for the activated Rab in docking and fusion.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsCasein Kinase IEnzyme ActivationEpistasis, GeneticMembrane FusionMembrane ProteinsProtein SubunitsQa-SNARE Proteinsrab GTP-Binding Proteinsras GTPase-Activating ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTwo-Hybrid System TechniquesAdaptor Proteins, Vesicular TransportCasein Kinase IGyp7 protein, S cerevisiaeMembrane ProteinsProtein SubunitsQa-SNARE Proteinsrab GTP-Binding Proteinsras GTPase-Activating ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsVAM3 protein, S cerevisiaeVAM6 protein, S cerevisiaeVesicular Transport ProteinsVPS41 protein, S cerevisiaeYCK3 protein, S cerevisiaeYPT7 protein, S cerevisiae

Identifiers

PMID18809726
PMCPMC2542475
OpenAlexW2140324218

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.