Evidence map›Paper›PMID 27154627›Full record

ArticleeLife2016

Distinct modes of endocytotic presynaptic membrane and protein uptake at the calyx of Held terminal of rats and mice.

Yuji Okamoto, Noa Lipstein, Yunfeng Hua, Kun-Han Lin, Nils Brose, Takeshi Sakaba, Mitsuharu Midorikawa

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Kinetics of transmitter release at the calyx of Held synapse.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018
    Review
  6. Article
  7. Article
  8. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Yuji OkamotoGraduate School of Brain Science, Doshisha University, Kyoto, Japan.
Noa LipsteinDepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Yunfeng HuaDepartment of Connectomics, Max Planck Institute of Brain Research, Frankfurt, Germany.
Kun-Han LinMax-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
Nils BroseDepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Takeshi SakabaGraduate School of Brain Science, Doshisha University, Kyoto, Japan.
Mitsuharu MidorikawaGraduate School of Brain Science, Doshisha University, Kyoto, Japan.ORCID 0000-0003-4818-6986
Doshisha University · JPMax Planck Institute of Experimental Medicine · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute for Brain Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurotransmitter is released at synapses by fusion of synaptic vesicles with the plasma membrane. To sustain synaptic transmission, compensatory retrieval of membranes and vesicular proteins is essential. We combined capacitance measurements and pH-imaging via pH-sensitive vesicular protein marker (anti-synaptotagmin2-cypHer5E), and compared the retrieval kinetics of membranes and vesicular proteins at the calyx of Held synapse. Membrane and Syt2 were retrieved with a similar time course when slow endocytosis was elicited. When fast endocytosis was elicited, Syt2 was still retrieved together with the membrane, but endocytosed organelle re-acidification was slowed down, which provides strong evidence for two distinct endocytotic pathways. Strikingly, CaM inhibitors or the inhibition of the Ca(2+)-calmodulin-Munc13-1 signaling pathway only impaired the uptake of Syt2 while leaving membrane retrieval intact, indicating different recycling mechanisms for membranes and vesicle proteins. Our data identify a novel mechanism of stimulus- and Ca(2+)-dependent regulation of coordinated endocytosis of synaptic membranes and vesicle proteins.

Indexed as

AnimalsCalmodulinCell MembraneEndocytosisExocytosisMiceNerve Tissue ProteinsNeurotransmitter AgentsPresynaptic TerminalsRatsSignal TransductionSynapsesSynaptic TransmissionSynaptic VesiclesSynaptotagmin IICalmodulinNerve Tissue ProteinsNeurotransmitter AgentsSynaptotagmin IISyt2 protein, mouseUnc13a protein, mouseelectrophysiologyendocytosisexocytosisimage analysismouseneuroscienceratsynaptic terminalstransgenic animals

Identifiers

PMID27154627
PMCPMC4927297
OpenAlexW2346743009

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.