Evidence map›Paper›PMID 11978810›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2002

Regulation of exocytosis through Ca2+/ATP-dependent binding of autophosphorylated Ca2+/calmodulin-activated protein kinase II to syntaxin 1A.

Akihiro Ohyama, Kohei Hosaka, Yoshiaki Komiya, Kimio Akagawa, Emiko Yamauchi, Hisaaki Taniguchi, Nobuyuki Sasagawa, Konosuke Kumakura, Sumiko Mochida, Takashi Yamauchi and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Eupafolin Suppresses P/Q-Type CaBiomolecules & therapeutics · 2021
    Article
  5. Article
  6. The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021
    Review
  7. Article
  8. Article
  9. Millisecond CaProceedings of the Japan Academy. Series B, Physical and biological sciences · 2017
    Review
  10. Activity-Dependent Phosphorylation by CaMKIIδ Alters the CaFrontiers in synaptic neuroscience · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Convergent Ca2+ and Zn2+ signaling regulates apoptotic Kv2.1 K+ currents.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  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

11 authors at 7 institutions in 1 country.

Akihiro OhyamaDepartment of Molecular and Cellular Neurobiology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan.
Kohei Hosaka
Yoshiaki Komiya
Kimio Akagawa
Emiko Yamauchi
Hisaaki Taniguchi
Nobuyuki Sasagawa
Konosuke Kumakura
Sumiko Mochida
Takashi Yamauchi
Michihiro Igarashi
Gunma University · JPLife Science Institute · JPFujita Health University · JPKyorin University · JPNiigata University · JPRIKEN · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syntaxin 1A/HPC-1 is a key component of the exocytotic molecular machinery, namely, the soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor mechanism. Although >10 syntaxin-binding proteins have been identified, they cannot completely explain the regulation of exocytosis. Thus, novel proteins may interact with syntaxin. Because exocytosis requires both Ca2+ and ATP, we searched for Ca2+/ATP-dependent syntaxin-binding proteins from the rat brain and discovered Ca2+/calmodulin-activated protein kinase II (CaMKII)-alpha. At Ca2+ concentrations of >10(-6) m, only autophosphorylated CaMKII bound to syntaxin. Bound CaMKII was released from syntaxin by EGTA or by phosphatase, indicating that the binding is reversible. CaMKII bound to the linker domain of syntaxin, unlike any other known syntaxin-binding proteins. CaMKII-syntaxin complexes were also detected in synaptosomes by immunoprecipitation, and when reconstituted in vitro, they recruited larger amounts of synaptotagmin and SNAP-25 than syntaxin alone. The microinjected CaMKII-binding domain of syntaxin specifically affected exocytosis in chromaffin cells and in neurons. These results indicate that the Ca2+/ATP-dependent binding of CaMKII to syntaxin is an important process in the regulation of exocytosis.

Indexed as

Calcium-Binding ProteinsVesicular Transport ProteinsAdenosine TriphosphateAnimalsAntigens, SurfaceBrain ChemistryCalciumCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2CatalysisCells, CulturedChelating AgentsChromaffin CellsExocytosisMacromolecular SubstancesMembrane GlycoproteinsAdenosine TriphosphateAntigens, SurfaceCalciumCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Chelating AgentsMacromolecular SubstancesMembrane GlycoproteinsMembrane ProteinsMunc18 ProteinsNerve Tissue ProteinsPeptide FragmentsPhosphoric Monoester HydrolasesSnap25 protein, ratSNARE ProteinsStx1a protein, ratSynaptosomal-Associated Protein 25SynaptotagminsSyntaxin 1Vesicular Transport Proteins

Identifiers

PMID11978810
PMCPMC6758377
OpenAlexW1507463132

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.