Evidence map›Paper›PMID 12857883›Full record

ArticleMolecular biology of the cell2003

Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation.

Helena Friesen, Kelly Murphy, Ashton Breitkreutz, Mike Tyers, Brenda Andrews

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

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  18. The BAR domain proteins: molding membranes in fission, fusion, and phagy.Microbiology and molecular biology reviews : MMBR · 2006
    Review
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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

5 authors at 1 institution in 1 country.

Helena FriesenDepartment of Molecular and Medical Genetics, University of Toronto, Toronto, Canada, M5S 1A8.
Kelly Murphy
Ashton Breitkreutz
Mike Tyers
Brenda Andrews
University of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast amphiphysin homologue Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. Rvs167p is a phosphoprotein in vegetatively growing cells and shows increased phosphorylation upon treatment with mating pheromone. Previous work has shown that Rvs167p can be phosphorylated in vitro by the cyclin-dependent kinase Pho85p complexed with its cyclin Pcl2p. Using chymotryptic phosphopeptide mapping, we have identified the sites on which Rvs167p is phosphorylated in vitro by Pcl2p-Pho85p. We have shown that these same sites are phosphorylated in vivo during vegetative growth and that phosphorylation at two of these sites is Pcl-Pho85p dependent. In cells treated with mating pheromone, the MAP kinase Fus3p is needed for full phosphorylation of Rvs167p. Functional genomics and genetics experiments revealed that mutation of other actin cytoskeleton genes compromises growth of a strain in which phosphorylation of Rvs167p is blocked by mutation. Phosphorylation of Rvs167p inhibits its interaction in vitro with Las17p, an activator of the Arp2/3 complex, as well as with a novel protein, Ymr192p. Our results suggest that phosphorylation of Rvs167p by a cyclin-dependent kinase and by a MAP kinase is an important mechanism for regulating protein complexes involved in actin cytoskeleton function.

Indexed as

Actin-Related Protein 2Actin-Related Protein 3ActinsAnimalsCells, CulturedCyclin-Dependent KinasesCyclinsCytoskeletal ProteinsInsect VirusesMicrofilament ProteinsMitogen-Activated Protein KinasesMutationPhosphorylationRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActin-Related Protein 2Actin-Related Protein 3ActinsARP2 protein, S cerevisiaeARP3 protein, S cerevisiaeCyclin-Dependent KinasesCyclinsCytoskeletal ProteinsFUS3 protein, S cerevisiaeLAS17 protein, S cerevisiaeMicrofilament ProteinsMitogen-Activated Protein KinasesPCL2 protein, S cerevisiaePHO85 protein, S cerevisiaeRecombinant ProteinsRVS167 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsWiskott-Aldrich Syndrome Protein

Identifiers

PMID12857883
PMCPMC165695
OpenAlexW2110380412

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.