Evidence map›Paper›PMID 23141066›Full record

ArticleNeuron2012

Regulation of DLK-1 kinase activity by calcium-mediated dissociation from an inhibitory isoform.

Dong Yan, Yishi Jin

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

71 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. An intraflagellar transport dependent negative feedback regulates the MAPKKK DLK-1 to protect cilia from degeneration.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. The MAP3Ks DLK and LZK Direct Diverse Responses to Axon Damage in Zebrafish Peripheral Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  11. Article
  12. A Critical Role for DLK and LZK in Axonal Repair in the Mammalian Spinal Cord.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. CaCold Spring Harbor perspectives in biology · 2019
    Review

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

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.

Dong YanNeurobiology Section, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093, USA.
Yishi Jin
University of California, San Diego · US

Funding

GABAERGIC NEURON DIFFERENTIATION IN C ELEGANSR01NS035546 · NINDS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI JIN, YISHI · 1996 to 2016
$5.3M
Development of a C. elegans model for axonal regenerationR01NS057317 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHISHOLM, ANDREW D · 2009 to 2013
$1.5M
Mechanisms of neural circuit formation in C. elegansR01NS094171 · NINDS · DUKE UNIVERSITY · PI YAN, DONG · 2015 to 2019
$1.5M
Regulation of the DLK-1 pathway in axon regenerationR00NS076646 · NINDS · DUKE UNIVERSITY · PI YAN, DONG · 2014 to 2016
$732k
Regulation of the DLK-1 pathway in axon regenerationK99NS076646 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI YAN, DONG · 2011 to 2012
$171k
Howard Hughes Medical InstituteNINDS NIH HHS K99 NS076646NINDS NIH HHS K99NS076646NINDS NIH HHS R00 NS076646NINDS NIH HHS R01 NS035546NINDS NIH HHS R01 NS057317NINDS NIH HHS R01 NS094171
6 · The paper itself

Abstract

MAPKKK dual leucine zipper-bearing kinases (DLKs) are regulators of synaptic development and axon regeneration. The mechanisms underlying their activation are not fully understood. Here, we show that C. elegans DLK-1 is activated by a Ca(2+)-dependent switch from inactive heteromeric to active homomeric protein complexes. We identify a DLK-1 isoform, DLK-1S, that shares identical kinase and leucine zipper domains with the previously described long isoform DLK-1L but acts to inhibit DLK-1 function by binding to DLK-1L. The switch between homo- or heteromeric DLK-1 complexes is influenced by Ca(2+) concentration. A conserved hexapeptide in the DLK-1L C terminus is essential for DLK-1 activity and is required for Ca(2+) regulation. The mammalian DLK-1 homolog MAP3K13 contains an identical C-terminal hexapeptide and can functionally complement dlk-1 mutants, suggesting that the DLK activation mechanism is conserved. The DLK activation mechanism is ideally suited for rapid and spatially controlled signal transduction in response to axonal injury and synaptic activity.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCalciumEnzyme ActivationHumansIsoenzymesMAP Kinase Kinase KinasesMutationNeural InhibitionCaenorhabditis elegans ProteinsCalciumDLK-1 protein, C elegansIsoenzymesMAP Kinase Kinase Kinases

Identifiers

PMID23141066
PMCPMC3508676
OpenAlexW2022903577

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.