Evidence map›Paper›PMID 26447709›Full record

ArticlePLoS genetics2015

Large-Scale Analysis of Kinase Signaling in Yeast Pseudohyphal Development Identifies Regulation of Ribonucleoprotein Granules.

Christian A Shively, Hye Kyong Kweon, Kaitlyn L Norman, Dattatreya Mellacheruvu, Tao Xu, Daniel T Sheidy, Craig J Dobry, Ivan Sabath, Eric E P Cosky, Elizabeth J Tran and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Roles of P-body factors inbioRxiv : the preprint server for biology · 2025
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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

13 authors at 3 institutions in 1 country.

Christian A ShivelyProgram in Cellular and Molecular Biology, University of Michigan, Ann Arbor, Michigan, United States of America; Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Hye Kyong KweonDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Kaitlyn L NormanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Dattatreya MellacheruvuDepartment of Pathology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America; Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Tao XuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Daniel T SheidyDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Craig J DobryDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Ivan SabathDepartment of Biochemistry, Purdue University, West Lafayette, Indiana, United States of America.
Eric E P CoskyDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Elizabeth J TranDepartment of Biochemistry, Purdue University, West Lafayette, Indiana, United States of America.
Alexey NesvizhskiiDepartment of Pathology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America; Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Philip C AndrewsDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, United States of America; Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.
Anuj KumarProgram in Cellular and Molecular Biology, University of Michigan, Ann Arbor, Michigan, United States of America; Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
University of Michigan–Ann Arbor · USMichigan United · USPurdue University West Lafayette · US

Funding

University of Michigan Center for Gastrointestinal ResearchP30DK034933 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OWYANG, CHUNG · 1986 to 2021
$22.5M
CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
The Role of DEAD-box Proteins in Gene ExpressionR01GM097332 · NIGMS · PURDUE UNIVERSITY · PI TRAN, ELIZABETH J · 2011 to 2025
$4.1M
NIDDK NIH HHS P30 DK034933NIGMS NIH HHS 2R01GM094231-05NIGMS NIH HHS R01 GM094231NIGMS NIH HHS R01 GM097332NIGMS NIH HHS T32 GM007315PHS HHS 1R01-A1098450-01A1
6 · The paper itself

Abstract

Yeast pseudohyphal filamentation is a stress-responsive growth transition relevant to processes required for virulence in pathogenic fungi. Pseudohyphal growth is controlled through a regulatory network encompassing conserved MAPK (Ste20p, Ste11p, Ste7p, Kss1p, and Fus3p), protein kinase A (Tpk2p), Elm1p, and Snf1p kinase pathways; however, the scope of these pathways is not fully understood. Here, we implemented quantitative phosphoproteomics to identify each of these signaling networks, generating a kinase-dead mutant in filamentous S. cerevisiae and surveying for differential phosphorylation. By this approach, we identified 439 phosphoproteins dependent upon pseudohyphal growth kinases. We report novel phosphorylation sites in 543 peptides, including phosphorylated residues in Ras2p and Flo8p required for wild-type filamentous growth. Phosphoproteins in these kinase signaling networks were enriched for ribonucleoprotein (RNP) granule components, and we observe co-localization of Kss1p, Fus3p, Ste20p, and Tpk2p with the RNP component Igo1p. These kinases localize in puncta with GFP-visualized mRNA, and KSS1 is required for wild-type levels of mRNA localization in RNPs. Kss1p pathway activity is reduced in lsm1Δ/Δ and pat1Δ/Δ strains, and these genes encoding P-body proteins are epistatic to STE7. The P-body protein Dhh1p is also required for hyphal development in Candida albicans. Collectively, this study presents a wealth of data identifying the yeast phosphoproteome in pseudohyphal growth and regulatory interrelationships between pseudohyphal growth kinases and RNPs.

Indexed as

Candida albicansGene Expression Regulation, FungalHyphaePhenotypePhosphorylationPhosphotransferasesRibonucleoproteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionPhosphotransferasesRibonucleoproteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID26447709
PMCPMC4598065
OpenAlexW2135597140

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.