Evidence map›Paper›PMID 27466283›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2016

JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships.

András Zeke, Mariya Misheva, Attila Reményi, Marie A Bogoyevitch

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 290 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
290citing papers in PubMed, 4 pooled it
15.5field-weighted citation impact, top 1% 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

290 citing papers in PubMed, 4 syntheses or guidelines pooled it, 514 citations in OpenAlex.

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  15. The hidden players: LncRNA-Encoded micropeptides in cancer hallmarks.Cellular and molecular life sciences : CMLS · 2026
    Review
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230 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

András ZekeLendulet Protein Interaction Group, Institute of Enzymology, Research Center for Natural Sciences Hungarian Academy of Sciences, Budapest, Hungary.
Mariya MishevaCell Signaling Research Laboratories and Bio21 Institute, Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria, Australia.
Attila ReményiLendulet Protein Interaction Group, Institute of Enzymology, Research Center for Natural Sciences Hungarian Academy of Sciences, Budapest, Hungary marieb@unimelb.edu.au remenyi.attila@ttk.mta.hu.
Marie A BogoyevitchCell Signaling Research Laboratories and Bio21 Institute, Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria, Australia marieb@unimelb.edu.au remenyi.attila@ttk.mta.hu.
University of Melbourne · AUHungarian Academy of Sciences · HUInstitute of Molecular Life Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The c-Jun N-terminal kinases (JNKs), as members of the mitogen-activated protein kinase (MAPK) family, mediate eukaryotic cell responses to a wide range of abiotic and biotic stress insults. JNKs also regulate important physiological processes, including neuronal functions, immunological actions, and embryonic development, via their impact on gene expression, cytoskeletal protein dynamics, and cell death/survival pathways. Although the JNK pathway has been under study for >20 years, its complexity is still perplexing, with multiple protein partners of JNKs underlying the diversity of actions. Here we review the current knowledge of JNK structure and isoforms as well as the partnerships of JNKs with a range of intracellular proteins. Many of these proteins are direct substrates of the JNKs. We analyzed almost 100 of these target proteins in detail within a framework of their classification based on their regulation by JNKs. Examples of these JNK substrates include a diverse assortment of nuclear transcription factors (Jun, ATF2, Myc, Elk1), cytoplasmic proteins involved in cytoskeleton regulation (DCX, Tau, WDR62) or vesicular transport (JIP1, JIP3), cell membrane receptors (BMPR2), and mitochondrial proteins (Mcl1, Bim). In addition, because upstream signaling components impact JNK activity, we critically assessed the involvement of signaling scaffolds and the roles of feedback mechanisms in the JNK pathway. Despite a clarification of many regulatory events in JNK-dependent signaling during the past decade, many other structural and mechanistic insights are just beginning to be revealed. These advances open new opportunities to understand the role of JNK signaling in diverse physiological and pathophysiological states.

Indexed as

AnimalsEukaryotic CellsHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Signaling SystemPhosphorylationProtein IsoformsJNK Mitogen-Activated Protein KinasesProtein Isoforms

Identifiers

PMID27466283
PMCPMC4981676
OpenAlexW2497333816

What Socratic 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 Socratic graph.