Evidence map›Paper›PMID 18423203›Full record

ArticleCell2008

CASK Functions as a Mg2+-independent neurexin kinase.

Konark Mukherjee, Manu Sharma, Henning Urlaub, Gleb P Bourenkov, Reinhard Jahn, Thomas C Südhof, Markus C Wahl

Open access · greenAbstract read
In one paragraph

Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.

0numbers the graph read from it
0cells of the map it votes in
149citing papers in PubMed
9.5field-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

149 citing papers in PubMed, 275 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. CASK hypomorph mice display cone photoreceptor dysfunction.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Postsynaptic receptors regulate presynaptic transmitter stability through transsynaptic bridges.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Calcium/Calmodulin-Dependent Serine Protein Kinase (Animals : an open access journal from MDPI · 2023
    Article
  18. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  19. Article
  20. PK1 fromOpen biology · 2023
    Article

89 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Konark MukherjeeDepartment of Neuroscience, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390-9111, USA. konark.mukherjee@utsouthwestern.edu
Manu Sharma
Henning Urlaub
Gleb P Bourenkov
Reinhard Jahn
Thomas C Südhof
Markus C Wahl
Max Planck Institute for Biophysical Chemistry · DEThe University of Texas Southwestern Medical Center · USDeutsches Elektronen-Synchrotron DESY · DE

Funding

FUNCTION OF NEUREXINSR37MH052804 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI SUDHOF, THOMAS C. · 2000 to 2019
$9.3M
NIMH NIH HHS R37 MH052804NIMH NIH HHS R37 MH52804-08
6 · The paper itself

Abstract

CASK is a unique MAGUK protein that contains an N-terminal CaM-kinase domain besides the typical MAGUK domains. The CASK CaM-kinase domain is presumed to be a catalytically inactive pseudokinase because it lacks the canonical DFG motif required for Mg2+ binding that is thought to be indispensable for kinase activity. Here we show, however, that CASK functions as an active protein kinase even without Mg2+ binding. High-resolution crystal structures reveal that the CASK CaM-kinase domain adopts a constitutively active conformation that binds ATP and catalyzes phosphotransfer without Mg2+. The CASK CaM-kinase domain phosphorylates itself and at least one physiological interactor, the synaptic protein neurexin-1, to which CASK is recruited via its PDZ domain. Thus, our data indicate that CASK combines the scaffolding activity of MAGUKs with an unusual kinase activity that phosphorylates substrates recuited by the scaffolding activity. Moreover, our study suggests that other pseudokinases (10% of the kinome) could also be catalytically active.

Indexed as

AnimalsCell LineCells, CulturedCrystallography, X-RayGlycoproteinsGuanylate KinasesHumansMagnesiumMiceModels, MolecularNeuronsNeuropeptidesNucleotidesProtein BindingProtein Structure, TertiaryRatsCASK kinasesGlycoproteinsGuanylate KinasesMagnesiumneurexophilinNeuropeptidesNucleotides

Identifiers

PMID18423203
PMCPMC3640377
OpenAlexW2099387330

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.