Evidence map›Paper›PMID 37988460›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases.

Jaylissa Torres Robles, Hua Jane Lou, Guangda Shi, Pauline Lining Pan, Benjamin E Turk

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Fuzziness in enzymatic catalysis.Current opinion in structural biology · 2025
    Review
  3. Article
  4. Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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 1 institution in 1 country.

Jaylissa Torres RoblesDepartment of Chemistry, Yale University, New Haven, CT 06520.
Hua Jane LouDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520.
Guangda ShiDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520.
Pauline Lining PanDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520.
Benjamin E TurkDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520.ORCID 0000-0001-9275-4069
Yale University · US

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Mechanisms of selective signaling in MAP kinase phosphorylation networksR01GM135331 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E · 2020 to 2023
$1.4M
High Performance Computing Instrumentation for the Yale Center for Genome AnalysisS10OD030363 · OD · YALE UNIVERSITY · PI MANE, SHRIKANT M · 2022 to 2022
$1.2M
NCATS NIH HHS UL1 TR001863NIGMS NIH HHS R01 GM135331NIH HHS S10 OD030363
6 · The paper itself

Abstract

Mitogen-activated protein kinase (MAPK) cascades are essential for eukaryotic cells to integrate and respond to diverse stimuli. Maintaining specificity in signaling through MAPK networks is key to coupling distinct inputs to appropriate cellular responses. Docking sites-short linear motifs found in MAPK substrates, regulators, and scaffolds-can promote signaling specificity through selective interactions, but how they do so remains unresolved. Here, we screened a proteomic library for sequences interacting with the MAPKs extracellular signal-regulated kinase 2 (ERK2) and p38α, identifying selective and promiscuous docking motifs. Sequences specific for p38α had high net charge and lysine content, and selective binding depended on a pair of acidic residues unique to the p38α docking interface. Finally, we validated a set of full-length proteins harboring docking sites selected in our screens to be authentic MAPK interactors and substrates. This study identifies features that help define MAPK signaling networks and explains how specific docking motifs promote signaling integrity.

Indexed as

Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesBinding SitesPhosphorylationProtein BindingProteomicsSignal TransductionMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinaseskinase docking interactionsMAP kinaseshort linear motifsignal transductionsubstrate specificity

Identifiers

PMID37988460
PMCPMC10691213
OpenAlexW4388857666

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.