Evidence map›Paper›PMID 32585314›Full record

ArticleJournal of structural biology2020

Recognition of physiological phosphorylation sites by p21-activated kinase 4.

Ashwin K Chetty, Joel A Sexton, Byung Hak Ha, Benjamin E Turk, Titus J Boggon

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Rho family GTPase signaling through type II p21-activated kinases.Cellular and molecular life sciences : CMLS · 2022
    Review
  4. Article
  5. Review
  6. 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

5 authors at 2 institutions in 1 country.

Ashwin K ChettyYale College, New Haven, CT 06520, USA; Department of Molecular Biophysics and Biochemistry, Yale University, 333 Cedar Street, New Haven, CT 06520, USA.
Joel A SextonDepartment of Pharmacology, Yale University, 333 Cedar Street, New Haven, CT 06520, USA.
Byung Hak HaDepartment of Pharmacology, Yale University, 333 Cedar Street, New Haven, CT 06520, USA.
Benjamin E TurkDepartment of Pharmacology, Yale University, 333 Cedar Street, New Haven, CT 06520, USA; Yale Cancer Center, Yale University, 333 Cedar Street, New Haven, CT 06520, USA.
Titus J BoggonDepartment of Molecular Biophysics and Biochemistry, Yale University, 333 Cedar Street, New Haven, CT 06520, USA; Department of Pharmacology, Yale University, 333 Cedar Street, New Haven, CT 06520, USA; Yale Cancer Center, Yale University, 333 Cedar Street, New Haven, CT 06520, USA. Electronic address: titus.boggon@yale.edu.
Yale University · USYale Cancer Center · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
INSTITUTIONAL NATIONAL RESEARCH SERVICE AWARDT32GM007324 · NIGMS · YALE UNIVERSITY · PI BENNETT, ANTON M · 1987 to 2022
$6.2M
Structure-directed investigations into the regulation of Ste20 kinasesR01GM102262 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2012 to 2025
$4.2M
Dual-specificity phosphatase action in muscle diseaseR01AR080152 · NIAMS · YALE UNIVERSITY · PI Anton M Bennett · 2022 to 2026
$2.5M
Upgrade of a home source macromolecular X-ray diffraction system.S10OD018007 · OD · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2014 to 2014
$460k
NIAMS NIH HHS R01 AR080152NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM102262NIGMS NIH HHS T32 GM007324NIH HHS S10 OD018007
6 · The paper itself

Abstract

Many serine/threonine protein kinases discriminate between serine and threonine substrates as a filter to control signaling output. Among these, the p21-activated kinase (PAK) group strongly favors phosphorylation of Ser over Thr residues. PAK4, a group II PAK, almost exclusively phosphorylates its substrates on serine residues. The only well documented exception is LIM domain kinase 1 (LIMK1), which is phosphorylated on an activation loop threonine (Thr508) to promote its catalytic activity. To understand the molecular and kinetic basis for PAK4 substrate selectivity we compared its mode of recognition of LIMK1 (Thr508) with that of a known serine substrate, β-catenin (Ser675). We determined X-ray crystal structures of PAK4 in complex with synthetic peptides corresponding to its phosphorylation sites in LIMK1 and β-catenin to 1.9 Å and 2.2 Å resolution, respectively. We found that the PAK4 DFG + 1 residue, a key determinant of phosphoacceptor preference, adopts a sub-optimal orientation when bound to LIMK1 compared to β-catenin. In peptide kinase activity assays, we find that phosphoacceptor identity impacts catalytic efficiency but does not affect the K

Indexed as

beta CateninCatalytic DomainCrystallography, X-RayHumansLim KinasesMutationp21-Activated KinasesPeptide FragmentsPhosphorylationSerineThreoninebeta CateninCTNNB1 protein, humanLIMK1 protein, humanLim Kinasesp21-Activated KinasesPAK4 protein, humanPeptide FragmentsSerineThreonineCrystallographyKinaseLIM domain kinaseSte20 kinaseSubstrate specificityβ-Catenin

Identifiers

PMID32585314
PMCPMC7395882
OpenAlexW3037980589

What OpenQuestion holds

Textmetadata
LicenceTDM
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.