Evidence map›Paper›PMID 21931684›Full record

ArticlePloS one2011

Phosphorylation provides a negative mode of regulation for the yeast Rab GTPase Sec4p.

Christopher D Heger, Christiane D Wrann, Ruth N Collins

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 15 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

3 authors at 2 institutions in 1 country.

Christopher D HegerGraduate Program in Pharmacology, Cornell University, Ithaca, New York, United States of America.
Christiane D Wrann
Ruth N Collins
Cornell University · USNew York State College of Veterinary Medicine · US

Funding

Mechanisms of Rab Protein Activation and FunctionR01GM069596 · NIGMS · CORNELL UNIVERSITY ITHACA · PI COLLINS, RUTH N · 2005 to 2009
$1.4M
BIOPHYSICAL AND BIOCHEMICAL PHARMACOLOGYT32GM008210 · NIGMS · CORNELL UNIVERSITY ITHACA · PI SHARP, GEOFFREY W · 1988 to 2007
$1.3M
Molecular analysis of Elp complex function in health and diseaseR01GM087812 · NIGMS · CORNELL UNIVERSITY · PI COLLINS, RUTH N · 2009 to 2012
$1.2M
NIGMS NIH HHS 5R01GM069596NIGMS NIH HHS 5T32GM008210-18NIGMS NIH HHS R01 GM069596NIGMS NIH HHS R01 GM087812NIGMS NIH HHS T32 GM008210
6 · The paper itself

Abstract

The Rab family of Ras-related GTPases are part of a complex signaling circuitry in eukaryotic cells, yet we understand little about the mechanisms that underlie Rab protein participation in such signal transduction networks, or how these networks are integrated at the physiological level. Reversible protein phosphorylation is widely used by cells as a signaling mechanism. Several phospho-Rabs have been identified, however the functional consequences of the modification appear to be diverse and need to be evaluated on an individual basis. In this study we demonstrate a role for phosphorylation as a negative regulatory event for the action of the yeast Rab GTPase Sec4p in regulating polarized growth. Our data suggest that the phosphorylation of the Rab Sec4p prevents interactions with its effector, the exocyst component Sec15p, and that the inhibition may be relieved by a PP2A phosphatase complex containing the regulatory subunit Cdc55p.

Indexed as

Amino Acid SequenceCell Cycle ProteinsComputational BiologyDNA Mutational AnalysisExocytosisMolecular Sequence DataPhosphorylationPhosphoserineProtein BindingProtein Phosphatase 2Protein Transportrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsCDC55 protein, S cerevisiaeCell Cycle ProteinsPhosphoserineProtein Phosphatase 2rab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSEC15 protein, S cerevisiaeSEC4 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID21931684
PMCPMC3171412
OpenAlexW2001019258

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.