Evidence map›Paper›PMID 20010694›Full record

ArticleThe EMBO journal2010

Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity.

Fernando Rodríguez-Castañeda, Mitcheell Maestre-Martínez, Nicolas Coudevylle, Kalina Dimova, Harald Junge, Noa Lipstein, Donghan Lee, Stefan Becker, Nils Brose, Olaf Jahn and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 77 citations in OpenAlex.

  1. A hydrophobic groove in secretagogin allows for alternate interactions with SNAP-25 and syntaxin-4 in endocrine tissues.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation.International journal of molecular sciences · 2023
    Review
  7. Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A.Protein science : a publication of the Protein Society · 2023
    Article
  8. Review
  9. Article
  10. The evolution of synaptic and cognitive capacity: Insights from the nervous system transcriptome ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Review
  12. Article
  13. Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

12 authors at 3 institutions in 1 country.

Fernando Rodríguez-CastañedaDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Mitcheell Maestre-Martínez
Nicolas Coudevylle
Kalina Dimova
Harald Junge
Noa Lipstein
Donghan Lee
Stefan Becker
Nils Brose
Olaf Jahn
Teresa Carlomagno
Christian Griesinger
Max Planck Institute for Biophysical Chemistry · DEMax Planck Institute of Experimental Medicine · DENanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103 · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ca(2+) signalling in neurons through calmodulin (CaM) has a prominent function in regulating synaptic vesicle trafficking, transport, and fusion. Importantly, Ca(2+)-CaM binds a conserved region in the priming proteins Munc13-1 and ubMunc13-2 and thus regulates synaptic neurotransmitter release in neurons in response to residual Ca(2+) signals. We solved the structure of Ca(2+)(4)-CaM in complex with the CaM-binding domain of Munc13-1, which features a novel 1-5-8-26 CaM-binding motif with two separated mobile structural modules, each involving a CaM domain. Photoaffinity labelling data reveal the same modular architecture in the complex with the ubMunc13-2 isoform. The N-module can be dissociated with EGTA to form the half-loaded Munc13/Ca(2+)(2)-CaM complex. The Ca(2+) regulation of these Munc13 isoforms can therefore be explained by the modular nature of the Munc13/Ca(2+)-CaM interactions, where the C-module provides a high-affinity interaction activated at nanomolar [Ca(2+)](i), whereas the N-module acts as a sensor at micromolar [Ca(2+)](i). This Ca(2+)/CaM-binding mode of Munc13 likely constitutes a key molecular correlate of the characteristic Ca(2+)-dependent modulation of short-term synaptic plasticity.

Indexed as

Neuronal PlasticityAmino Acid SequenceAnimalsCalciumCalmodulinHumansMammalsModels, BiologicalModels, MolecularMolecular ConformationMolecular Sequence DataMultiprotein ComplexesNerve Tissue ProteinsSequence Homology, Amino AcidStructure-Activity RelationshipSynapsesCalciumCalmodulinMultiprotein ComplexesNerve Tissue ProteinsUNC13B protein, human

Identifiers

PMID20010694
PMCPMC2830703
OpenAlexW2155341464

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.