Evidence map›Paper›PMID 40737028›Full record

ArticleThe Biochemical journal2025

Structural insights and biophysical characterization of p90RSK2:ERK2 complex.

Evan Kazuo Kobori, Hoang Phuong My Nguyen, Jian Wu, Katherine Chen, Rodeon Malinovski, Susan Taylor

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Biochemical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    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

6 authors.

Evan Kazuo Kobori *Department of Chemistry and Biochemistry, University of California, San Diego, CA, U.S.A.
Hoang Phuong My Nguyen *Department of Chemistry and Biochemistry, University of California, San Diego, CA, U.S.A.ORCID 0000-0002-1614-7424
Jian WuDepartment of Pharmacology, University of California, San Diego, CA, U.S.A.ORCID 0000-0002-8031-9462
Katherine ChenDepartment of Chemistry and Biochemistry, University of California, San Diego, CA, U.S.A.
Rodeon MalinovskiDepartment of Chemistry and Biochemistry, University of California, San Diego, CA, U.S.A.
Susan TaylorDepartment of Chemistry and Biochemistry, University of California, San Diego, CA, U.S.A.ORCID 0000-0002-7702-6108

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
Lessons Learned from PKA: Assembly of Dynamic Macromolecular SwitchesR35GM130389 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SUSAN S. TAYLOR · 2019 to 2026
$5.7M
Cellular and Molecular Pharmacology Training ProgramT32GM153123 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JOAN HELLER BROWN, Tracy M Handel · 2024 to 2026
$1.3M
Chemical Biology Interfaces at UC San DiegoT32GM112584 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2015 to 2019
$729k
Fletcher Jones Foundation Dissertation Year FellowshipNIGMS NIH HHS R35 GM130389NIGMS NIH HHS T32 GM008326NIGMS NIH HHS T32 GM112584NIGMS NIH HHS T32 GM153123NIH Office of the Director R35-GM130389
6 · The paper itself

Abstract

Kinase domains are often flanked by flexible tails and intrinsically disordered regions (IDRs) that contain conserved motifs. The co-ordinated action and interplay of IDRs and folded kinase domains is necessary for the proper function of kinases and kinase complexes. Characterization of full-length kinases and complexes is often challenging due to the flexible nature of flanking IDRs, yet necessary to fully understand their function and regulation. The p90 ribosomal S6 kinase (RSK) family is a unique kinase family with two distinct, functional kinase domains (NTK and CTK) flanked by flexible tails and a linker. RSK2 forms a stable complex with its activating kinase, ERK2, and here, we use multiple complementary techniques, hydrogen-deuterium exchange mass spectrometry, cryoelectron microscopy (cryo-EM), and AlphaFold (AF) modeling to study the full-length RSK2:ERK2 complex. We find that broadly, ERK2 is more solvent protected than the NTK/CTK. The NTK N-lobe has quite high deuterium uptake, and analysis of published NTK crystal structures suggests that the NTK N-lobe is dynamic and can adopt a wide range of conformations. The cryo-EM reveals that the RSK2:ERK2 complex adopts a compact shape, and this is consistent with the AF model of the complex, which hints at a possible additional interface between the NTK and ERK2. Collectively, our approach demonstrates that employing multiple complementary techniques can provide insight into the structure and biophysical characteristics of this challenging-to-study kinase complex.

Indexed as

Mitogen-Activated Protein Kinase 1Ribosomal Protein S6 Kinases, 90-kDaCryoelectron MicroscopyHumansModels, MolecularProtein BindingProtein ConformationProtein DomainsMAPK1 protein, humanMitogen-Activated Protein Kinase 1ribosomal protein S6 kinase, 90kDa, polypeptide 3Ribosomal Protein S6 Kinases, 90-kDaAlphaFold modelingcryogenic electron microscopyERKhydrogen–deuterium exchange mass spectrometrykinasep90RSK

Identifiers

PMID40737028
PMCPMC12614931

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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.