Evidence map›Paper›PMID 29295922›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

CDC42 binds PAK4 via an extended GTPase-effector interface.

Byung Hak Ha, Titus J Boggon

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed, 26 citations in OpenAlex.

  1. A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Rho family GTPase signaling through type II p21-activated kinases.Cellular and molecular life sciences : CMLS · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
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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

2 authors at 1 institution in 1 country.

Byung Hak HaDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06520.
Titus J BoggonDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06520; Titus.Boggon@yale.edu.
Yale University · US

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structure-directed investigations into the regulation of Ste20 kinasesR01GM102262 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2012 to 2025
$4.2M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
A Simultaneous SAXS/WAXS Detector System for Solving Biological StructuresS10OD012331 · OD · STATE UNIVERSITY NEW YORK STONY BROOK · PI ALLAIRE, MARC · 2012 to 2012
$1.1M
Upgrade of a home source macromolecular X-ray diffraction system.S10OD018007 · OD · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2014 to 2014
$460k
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM102262NIH HHS S10 OD012331NIH HHS S10 OD018007
6 · The paper itself

Abstract

The p21-activated kinase (PAK) group of serine/threonine kinases are downstream effectors of RHO GTPases and play important roles in regulation of the actin cytoskeleton, cell growth, survival, polarity, and development. Here we probe the interaction of the type II PAK, PAK4, with RHO GTPases. Using solution scattering we find that the full-length PAK4 heterodimer with CDC42 adopts primarily a compact organization. X-ray crystallography reveals the molecular nature of the interaction between PAK4 and CDC42 and shows that in addition to the canonical PAK4 CDC42/RAC interactive binding (CRIB) domain binding to CDC42 there are unexpected contacts involving the PAK4 kinase C-lobe, CDC42, and the PAK4 polybasic region. These additional interactions modulate kinase activity and increase the binding affinity of CDC42 for full-length PAK4 compared with the CRIB domain alone. We therefore show that the interaction of CDC42 with PAK4 can influence kinase activity in a previously unappreciated manner.

Indexed as

Amino Acid SequenceBinding Sitescdc42 GTP-Binding ProteinCrystallography, X-RayHumansModels, MolecularMolecular Sequence Datap21-Activated KinasesProtein BindingProtein Domainscdc42 GTP-Binding Proteinp21-Activated KinasesPAK4 protein, humancrystal structureprotein kinaseprotein–protein interactionsignal transductionsmall GTPase

Identifiers

PMID29295922
PMCPMC5776996
OpenAlexW2782230450

What OpenQuestion 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 OpenQuestion graph.