Evidence map›Paper›PMID 27911772›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

C-terminal domain (CTD) phosphatase links Rho GTPase signaling to Pol II CTD phosphorylation in Arabidopsis and yeast.

Bo Zhang, Guohua Yang, Yu Chen, Yihong Zhao, Peng Gao, Bo Liu, Haiyang Wang, Zhi-Liang Zheng

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 20 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

8 authors at 7 institutions in 2 countries.

Bo ZhangPlant Nutrient Signaling and Fruit Quality Improvement Laboratory, Citrus Research Institute, Southwest University, Beibei, Chongqing 400712, China.
Guohua YangDepartment of Biological Sciences, Lehman College, City University of New York, Bronx, NY 10468.
Yu ChenDepartment of Biological Sciences, Lehman College, City University of New York, Bronx, NY 10468.
Yihong ZhaoDivision of Biostatistics, Department of Child and Adolescent Psychiatry, New York University Langone Medical Center, New York, NY 10016.
Peng GaoDepartment of Biological Sciences, Lehman College, City University of New York, Bronx, NY 10468.
Bo LiuDepartment of Plant Biology, University of California, Davis, CA 95616.
Haiyang WangBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Zhi-Liang ZhengDepartment of Biological Sciences, Lehman College, City University of New York, Bronx, NY 10468; zhiliang.zheng@lehman.cuny.edu.
Lehman College · USBiotechnology Research Institute · CNCitrus Research Institute · CNCity University of New York · USNYU Langone Health · USSouthwest University · CNUniversity of California, Davis · US

Funding

TARGET SITES AND COMPARTMENTALIZATION IN HEAVY METAL EXPOSED CELLSS06GM008225 · NIGMS · HERBERT H. LEHMAN COLLEGE · PI JONES, LIESL B · 1989 to 2007
$16.0M
NIGMS NIH HHS S06 GM008225
6 · The paper itself

Abstract

Rho GTPases, including the Rho, Cdc42, Rac, and ROP subfamilies, act as pivotal signaling switches in various growth and developmental processes. Compared with the well-defined role of cytoskeletal organization in Rho signaling, much less is known regarding transcriptional regulation. In a mutant screen for phenotypic enhancers of transgenic Arabidopsis plants expressing a constitutively active form of ROP2 (designated CA1-1), we identified RNA polymerase II (Pol II) C-terminal domain (CTD) phosphatase-like 1 (CPL1) as a transcriptional regulator of ROP2 signaling. We show that ROP2 activation inhibits CPL1 activity by promoting its degradation, leading to an increase in CTD Ser5 and Ser2 phosphorylation. We also observed similar modulation of CTD phosphorylation by yeast Cdc42 GTPase and enhanced degradation of the yeast CTD phosphatase Fcp1 by activated ROP2 signaling. Taken together, our results suggest that modulation of the Pol II CTD code by Rho GTPase signaling represents an evolutionarily conserved mechanism in both unicellular and multicellular eukaryotes.

Indexed as

ArabidopsisArabidopsis Proteinscdc42 GTP-Binding ProteinGenes, PlantGTP-Binding ProteinsModels, BiologicalMutationPhosphoprotein PhosphatasesPhosphorylationPlants, Genetically ModifiedProteolysisrho GTP-Binding ProteinsRNA-Binding ProteinsRNA Polymerase IISaccharomycetalesSchizosaccharomycesArabidopsis ProteinsAT1G20090 protein, Arabidopsiscarboxy-terminal domain phosphatasecdc42 GTP-Binding ProteinCPL1 protein, ArabidopsisCPL2 protein, ArabidopsisGTP-Binding ProteinsPhosphoprotein Phosphatasesrho GTP-Binding ProteinsRNA-Binding ProteinsRNA Polymerase IISchizosaccharomyces pombe ProteinsSerineTranscription FactorsCPL1CTD codePol IIRho GTPaseROP GTPase

Identifiers

PMID27911772
PMCPMC5167197
OpenAlexW2558680753

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.