Evidence map›Paper›PMID 32715625›Full record

ArticleEMBO reports2020

Key phosphorylation sites in GPCRs orchestrate the contribution of β-Arrestin 1 in ERK1/2 activation.

Mithu Baidya, Punita Kumari, Hemlata Dwivedi-Agnihotri, Shubhi Pandey, Madhu Chaturvedi, Tomasz Maciej Stepniewski, Kouki Kawakami, Yubo Cao, Stéphane A Laporte, Jana Selent and 2 more

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 64 citations in OpenAlex.

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  15. G protein-biased GPR3 signaling ameliorates amyloid pathology in a preclinical Alzheimer's disease mouse model.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  20. Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins.International journal of molecular sciences · 2022
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 5 countries.

Mithu Baidya *Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.
Punita Kumari *Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.ORCID 0000-0003-1834-0962
Hemlata Dwivedi-Agnihotri *Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.
Shubhi PandeyDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.ORCID 0000-0001-7909-5505
Madhu ChaturvediDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.
Tomasz Maciej StepniewskiResearch Programme on Biomedical Informatics (GRIB), Department of Experimental and Health Sciences of Pompeu, Fabra University (UPF)-Hospital del Mar Medical Research Institute (IMIM), Barcelona, Spain.
Kouki KawakamiGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Yubo CaoDepartment of Pharmacology and Therapeutics, McGill University, Montréal, QC, Canada.
Stéphane A LaporteDepartment of Pharmacology and Therapeutics, McGill University, Montréal, QC, Canada.
Jana SelentResearch Programme on Biomedical Informatics (GRIB), Department of Experimental and Health Sciences of Pompeu, Fabra University (UPF)-Hospital del Mar Medical Research Institute (IMIM), Barcelona, Spain.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Arun K ShuklaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.ORCID 0000-0003-2910-8288
Indian Institute of Technology Kanpur · INTohoku University · JPUniversitat Pompeu Fabra · ESMcGill University · CAMcGill University Health Centre · CA

Funding

Council of Scientific and Industrial Research, India (CSIR) 09/092(0976/2017-EMR-I)Department of Biotechnology, Ministry of Science and Technology (DBT) BT/PR29041/BRB/10/1697/20Department of Biotechnology, Ministry of Science and Technology (DBT) BT/PR31791/BIC/101/1228/2019Department of Science and Technology, Ministry of Science and Technology (DST) DST/SJF/LSA-03/2017-18DST | Science and Engineering Research Board (SERB) EMR/2017/003804DST | Science and Engineering Research Board (SERB) PDF/2016/002930DST | Science and Engineering Research Board (SERB) PDF/2016/2893ERA-NET NEURON & Ministry of Economy, Industry and Competitiveness AC18/00030Fonds de recherche santé QuébecGouvernement du Canada | Canadian Institutes of Health Research (CIHR) MOP-74603Indian Institute of Technology, KanpurJapan Agency for Medical Research and Development (AMED) LEAP JP19gm0010004Japan Agency for Medical Research and Development (AMED) PRIME JP19gm5910013Lady TATA Memorial TrustMEC | Instituto de Salud Carlos III (ISCIII) PI15/00460MEC | Instituto de Salud Carlos III (ISCIII) PI18/00094MEXT | Japan Society for the Promotion of Science (JSPS) 19J11256MEXT | Japan Society for the Promotion of Science (JSPS) KAKENHI 17K08264Nacional Center of Science, Poland 2017/27/N/NZ2/02571The Wellcome Trust DBT India Alliance (India Alliance) IA/I/14/1/501285Wellcome Trust
6 · The paper itself

Abstract

β-arrestins (βarrs) are key regulators of G protein-coupled receptor (GPCR) signaling and trafficking, and their knockdown typically leads to a decrease in agonist-induced ERK1/2 MAP kinase activation. Interestingly, for some GPCRs, knockdown of βarr1 augments agonist-induced ERK1/2 phosphorylation although a mechanistic basis for this intriguing phenomenon is unclear. Here, we use selected GPCRs to explore a possible correlation between the spatial positioning of receptor phosphorylation sites and the contribution of βarr1 in ERK1/2 activation. We discover that engineering a spatially positioned double-phosphorylation-site cluster in the bradykinin receptor (B

Indexed as

MAP Kinase Signaling SystemReceptors, G-Protein-Coupledbeta-Arrestin 1beta-ArrestinsHEK293 CellsHumansPhosphorylationbeta-Arrestin 1beta-ArrestinsReceptors, G-Protein-Coupledbiased agonismcellular signalingERK1/2 MAP kinaseG protein-coupled receptorsβ-arrestins

Identifiers

PMID32715625
PMCPMC7507470
OpenAlexW3044480534

What OpenQuestion holds

Textmetadata
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.