Evidence map›Paper›PMID 39123091›Full record

ArticleCellular and molecular life sciences : CMLS2024

Non-canonical function of ADAM10 in presynaptic plasticity.

Julia Bär, Tomas Fanutza, Christopher C Reimann, Lisa Seipold, Maja Grohe, Janike Rabea Bolter, Flemming Delfs, Michael Bucher, Christine E Gee, Michaela Schweizer and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
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.

Julia BärAG Optobiology, Institute of Biology, Humboldt Universität Zu Berlin, 10115, Berlin, Germany.ORCID http://orcid.org/0000-0002-0954-2776
Tomas FanutzaAG Optobiology, Institute of Biology, Humboldt Universität Zu Berlin, 10115, Berlin, Germany.
Christopher C ReimannGuest Group, "Neuronal Protein Transport", Center for Molecular Neurobiology, University Medical Center Hamburg-Eppendorf, 20251, Hamburg, Germany.ORCID http://orcid.org/0000-0001-8080-0419
Lisa SeipoldBiochemisches Institut, Christian Albrechts-Universität Kiel, 24098, Kiel, Germany.
Maja GroheBiochemisches Institut, Christian Albrechts-Universität Kiel, 24098, Kiel, Germany.
Janike Rabea BolterAG Optobiology, Institute of Biology, Humboldt Universität Zu Berlin, 10115, Berlin, Germany.
Flemming DelfsGuest Group, "Neuronal Protein Transport", Center for Molecular Neurobiology, University Medical Center Hamburg-Eppendorf, 20251, Hamburg, Germany.
Michael BucherGuest Group, "Neuronal Protein Transport", Center for Molecular Neurobiology, University Medical Center Hamburg-Eppendorf, 20251, Hamburg, Germany.ORCID http://orcid.org/0000-0001-9296-121X
Christine E GeeDepartment of Synaptic Physiology, Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, 20251, Hamburg, Germany.ORCID http://orcid.org/0000-0003-0345-3665
Michaela SchweizerMorphology and Electron Microscopy, Center for Molecular Neurobiology, University Medical Center Hamburg-Eppendorf, ZMNH, 20251, Hamburg, Germany.
Paul SaftigBiochemisches Institut, Christian Albrechts-Universität Kiel, 24098, Kiel, Germany. psaftig@biochem.uni-kiel.de.ORCID http://orcid.org/0000-0003-2637-7052
Marina MikhaylovaAG Optobiology, Institute of Biology, Humboldt Universität Zu Berlin, 10115, Berlin, Germany. marina.mikhaylova@hu-berlin.de.ORCID http://orcid.org/0000-0001-7646-1346

Funding

Deutsche Forschungsgemeinschaft CRC1315 A10Deutsche Forschungsgemeinschaft CRC877 A3Deutsche Forschungsgemeinschaft CRC877 B12Deutsche Forschungsgemeinschaft EXC-2049-390688087Deutsche Forschungsgemeinschaft FOR2419 P2Deutsche Forschungsgemeinschaft FOR2419 P7Deutsche Forschungsgemeinschaft Z3
6 · The paper itself

Abstract

A Disintegrin And Metalloproteinase 10 (ADAM10) plays a pivotal role in shaping neuronal networks by orchestrating the activity of numerous membrane proteins through the shedding of their extracellular domains. Despite its significance in the brain, the specific cellular localization of ADAM10 remains not well understood due to a lack of appropriate tools. Here, using a specific ADAM10 antibody suitable for immunostainings, we observed that ADAM10 is localized to presynapses and especially enriched at presynaptic vesicles of mossy fiber (MF)-CA3 synapses in the hippocampus. These synapses undergo pronounced frequency facilitation of neurotransmitter release, a process that play critical roles in information transfer and neural computation. We demonstrate, that in conditional ADAM10 knockout mice the ability of MF synapses to undergo this type of synaptic plasticity is greatly reduced. The loss of facilitation depends on the cytosolic domain of ADAM10 and association with the calcium sensor synaptotagmin 7 rather than ADAM10's proteolytic activity. Our findings unveil a new role of ADAM10 in the regulation of synaptic vesicle exocytosis.

Indexed as

ADAM10 ProteinAmyloid Precursor Protein SecretasesMembrane ProteinsMice, KnockoutNeuronal PlasticitySynaptic VesiclesAnimalsExocytosisHippocampusMiceMice, Inbred C57BLMossy Fibers, HippocampalPresynaptic TerminalsSynapsesSynaptic TransmissionSynaptotagminsADAM10 ProteinAdam10 protein, mouseAmyloid Precursor Protein SecretasesMembrane ProteinsSynaptotagminsCA3Mossy fiber facilitationProteaseShort-term plasticityVesicle release

Identifiers

PMID39123091
PMCPMC11335265

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.