Evidence map›Paper›PMID 37668419›Full record

ArticleCurrent protocols2023

Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs).

Xuanzhi Zhan, Tamer S Kaoud, Kevin N Dalby, Eugenia V Gurevich, Vsevolod V Gurevich

Open access · greenAbstract read
In one paragraph

Article in Current protocols, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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 2 institutions in 1 country.

Xuanzhi ZhanDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee.
Tamer S KaoudDivision of Chemical Biology & Medicinal Chemistry, The University of Texas at Austin, Austin, Texas.
Kevin N DalbyDivision of Chemical Biology & Medicinal Chemistry, The University of Texas at Austin, Austin, Texas.
Eugenia V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee.
Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee.
Vanderbilt University · USThe University of Texas at Austin · US

Funding

STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
Targeted Engineering of Designer Arrestins to Regulate Cell SignalingR35GM122491 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2017 to 2021
$2.6M
Mechanism and Specificity of MAP KinasesR01GM059802 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI DALBY, KEVIN N · 2001 to 2011
$2.3M
Signaling regulation in the striatum in Parkinson's diseaseR01NS065868 · NINDS · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2009 to 2013
$1.7M
The role of receptor desensitization machinery in psychostimulant addictionR21DA030103 · NIDA · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2011 to 2012
$390k
NEI NIH HHS R01 EY011500NIDA NIH HHS R21 DA030103NIGMS NIH HHS R01 GM059802NIGMS NIH HHS R35 GM122491NINDS NIH HHS R01 NS065868
6 · The paper itself

Abstract

Only 1 out of 4 mammalian arrestin subtypes, arrestin-3, facilitates the activation of c-Jun N-terminal kinase (JNK) family kinases. Here, we describe two different sets of protocols used for elucidating the mechanisms involved. One is based on reconstitution of signaling modules from the following purified proteins: arrestin-3, MKK4, MKK7, JNK1, JNK2, and JNK3. The main advantage of this method is that it unambiguously establishes which effects are direct because only intended purified proteins are present in these assays. The key drawback is that the upstream-most kinases of these cascades, ASK1 or other MAP3Ks, are not available in purified form, limiting reconstitution to incomplete two-kinase modules. The other approach is used for analyzing the effects of arrestin-3 on JNK activation in intact cells. In this case, signaling modules include ASK1 and/or other MAP3Ks. However, as every cell expresses thousands of different proteins, their possible effects on the readout cannot be excluded. Nonetheless, the combination of in vitro reconstitution from purified proteins and cell-based assays makes it possible to elucidate the mechanisms of arrestin-3-dependent activation of JNK family kinases. © 2023 Wiley Periodicals LLC. Basic Protocol 1: Construction of arrestin-3-scaffolded MKK4/7-JNK1/2/3 signaling modules in vitro using purified proteins Alternate Protocol 1: Characterization of arrestin-3-mediated JNK1/2 activation by MKK4/7 by measurement of JNK1/2 phosphorylation using immunoblotting with anti-phospho-JNK antibody Support Protocol 1: Expression, purification, and activation of GST-MKK4 Support Protocol 2: Expression, purification, and activation of GST-MKK7-His

Indexed as

JNK Mitogen-Activated Protein KinasesProtein Processing, Post-TranslationalAnimalsArrestinsbeta-Arrestin 1beta-Arrestin 2MammalsMAP Kinase Kinase 4PhosphorylationArrestinsbeta-Arrestin 1beta-Arrestin 2JNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4activationarrestinbiphasic dependencec-Jun N-terminal kinase (JNK)scaffold

Identifiers

PMID37668419
PMCPMC10624153
OpenAlexW4386438867

What OpenQuestion holds

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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.