Evidence map›Paper›PMID 26868142›Full record

ArticleScientific reports2016

Peptide mini-scaffold facilitates JNK3 activation in cells.

Xuanzhi Zhan, Henriette Stoy, Tamer S Kaoud, Nicole A Perry, Qiuyan Chen, Alejandro Perez, Sylvia Els-Heindl, Jack V Slagis, Tina M Iverson, Annette G Beck-Sickinger and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Arrestins as Possible Drug Targets.Biomolecules & therapeutics · 2025
    Review
  4. Article
  5. Article
  6. GPCR-dependent and -independent arrestin signaling.Trends in pharmacological sciences · 2024
    Review
  7. Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024
    Review
  8. Pharmacological reviews · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Short Arrestin-3-Derived Peptides Activate JNK3 in Cells.International journal of molecular sciences · 2022
    Article
  13. Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins.International journal of molecular sciences · 2022
    Review
  14. The Two Non-Visual Arrestins Engage ERK2 Differently.Journal of molecular biology · 2022
    Article
  15. Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Targeting arrestin interactions with its partners for therapeutic purposes.Advances in protein chemistry and structural biology · 2020
    Review
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 5 institutions in 3 countries.

Xuanzhi ZhanDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Henriette StoyDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Tamer S KaoudFaculty of Pharmacy, Minia University, Minia, Egypt.
Nicole A PerryDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Qiuyan ChenDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Alejandro PerezDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Sylvia Els-HeindlUniversität Leipzig, Faculty of Biosciences, Pharmacy and Psychology, Institute of Biochemistry, Brüderstrasse 34, 04103 Leipzig, Germany.
Jack V SlagisDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Tina M IversonDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Annette G Beck-SickingerUniversität Leipzig, Faculty of Biosciences, Pharmacy and Psychology, Institute of Biochemistry, Brüderstrasse 34, 04103 Leipzig, Germany.
Eugenia V GurevichDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Kevin N DalbyDivision of Medicinal Chemistry, The University of Texas at Austin, Austin, Texas 78712, USA.
Vsevolod V GurevichDepartments of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Vanderbilt University · USLeipzig University · DEMinia University · EGThe University of Texas at Austin · USUniversity of Tübingen · DE

Funding

STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Mechanism and Specificity of MAP KinasesR01GM059802 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI DALBY, KEVIN N · 2001 to 2011
$2.3M
Arrestin interactions with non-receptor binding partnersR01GM077561 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2007 to 2015
$2.3M
Signaling regulation in the striatum in Parkinson's diseaseR01NS065868 · NINDS · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2009 to 2013
$1.7M
Conformational regulation of arrestin-mediated signalingR01GM081756 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2008 to 2011
$1.5M
Stabilization of Membrane Protein Signaling ComplexesR01GM095633 · NIGMS · VANDERBILT UNIVERSITY · PI IVERSON, T M · 2010 to 2013
$1.2M
Regulation of GPCR signaling with receptor-specific arrestinsR01GM109955 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2015 to 2017
$1.1M
Novel Therapeutics for Translation Control in Breast CancerR21CA167505 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI DALBY, KEVIN N, OZPOLAT, BULENT · 2012 to 2013
$369k
NCI NIH HHS CA167505NCI NIH HHS R21 CA167505NEI NIH HHS EY011500NEI NIH HHS R01 EY011500NIGMS NIH HHS GM059802NIGMS NIH HHS GM077561NIGMS NIH HHS GM081756NIGMS NIH HHS GM095633NIGMS NIH HHS R01 GM059802NIGMS NIH HHS R01 GM077561NIGMS NIH HHS R01 GM081756NIGMS NIH HHS R01 GM095633NIGMS NIH HHS R01 GM109955NIGMS NIH HHS T32 GM008320NINDS NIH HHS NS065868NINDS NIH HHS R01 NS065868
6 · The paper itself

Abstract

Three-kinase mitogen-activated protein kinase (MAPK) signaling cascades are present in virtually all eukaryotic cells. MAPK cascades are organized by scaffold proteins, which assemble cognate kinases into productive signaling complexes. Arrestin-3 facilitates JNK activation in cells, and a short 25-residue arrestin-3 peptide was identified as the critical JNK3-binding element. Here we demonstrate that this peptide also binds MKK4, MKK7, and ASK1, which are upstream JNK3-activating kinases. This peptide is sufficient to enhance JNK3 activity in cells. A homologous arrestin-2 peptide, which differs only in four positions, binds MKK4, but not MKK7 or JNK3, and is ineffective in cells at enhancing activation of JNK3. The arrestin-3 peptide is the smallest MAPK scaffold known. This peptide or its mimics can regulate MAPKs, affecting cellular decisions to live or die.

Indexed as

Enzyme ActivatorsPeptidesAnimalsbeta-Arrestin 1beta-Arrestin 2Chlorocebus aethiopsCOS CellsEnzyme ActivationHumansMitogen-Activated Protein Kinase 10beta-Arrestin 1beta-Arrestin 2Enzyme ActivatorsMitogen-Activated Protein Kinase 10Peptides

Identifiers

PMID26868142
PMCPMC4751492
OpenAlexW2295526222

What OpenQuestion holds

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LicenceCC BY
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.