Evidence map›Paper›PMID 41521833›Full record

ArticleActa physiologica (Oxford, England)2026

The Calcium-Binding Protein S100A10 (p11) Is Required for Normal Motor Performance by Regulating Vesicle Dynamics at Excitatory Synapses.

Esther Vilches-Herrando, Guillermo Rodríguez-Bey, Rosendo G Hernández, Ángela Gento-Caro, Ángel M Pastor, Antonio Campos-Caro, David González-Forero, Bernardo Moreno-López

Abstract read
In one paragraph

Article in Acta physiologica (Oxford, England), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

8 authors.

Esther Vilches-HerrandoGRUpo de NEuroDEgeneración y NeurorREparación (GRUNEDERE), Área de Fisiología, Facultad de Medicina, Universidad de Cádiz, Cádiz, Spain.
Guillermo Rodríguez-BeyGRUpo de NEuroDEgeneración y NeurorREparación (GRUNEDERE), Área de Fisiología, Facultad de Medicina, Universidad de Cádiz, Cádiz, Spain.ORCID https://orcid.org/0000-0003-3597-0245
Rosendo G HernándezFacultad de Biología, Departamento de Fisiología, Universidad de Sevilla, Sevilla, Spain.
Ángela Gento-CaroGRUpo de NEuroDEgeneración y NeurorREparación (GRUNEDERE), Área de Fisiología, Facultad de Medicina, Universidad de Cádiz, Cádiz, Spain.
Ángel M PastorFacultad de Biología, Departamento de Fisiología, Universidad de Sevilla, Sevilla, Spain.
Antonio Campos-CaroInstituto de Investigación e Innovación Biomédica de Cádiz (INiBICA), Cádiz, Spain.
David González-ForeroGRUpo de NEuroDEgeneración y NeurorREparación (GRUNEDERE), Área de Fisiología, Facultad de Medicina, Universidad de Cádiz, Cádiz, Spain.
Bernardo Moreno-LópezGRUpo de NEuroDEgeneración y NeurorREparación (GRUNEDERE), Área de Fisiología, Facultad de Medicina, Universidad de Cádiz, Cádiz, Spain.ORCID https://orcid.org/0000-0003-2897-6227

Funding

Agencia Estatal de Investigación PID2019-110960GB-I00Agencia Estatal de Investigación PID2021-124300NB-I00Agencia Estatal de Investigación PID2023-152180NB-I00Agencia Estatal de Investigación RYC2021-033058-I
6 · The paper itself

Abstract

aimIdentifying interactors in sensorimotor processing and neurotransmission remains a current challenge for understanding neural information processing and brain function.

methodsTo evaluate the role of p11 in sensorimotor processing and excitatory synaptic neurotransmission, neuron-specific lentivirus-directed p11 silencing, small interfering RNA (siRNA

resultsp11 knockdown depressed baseline and chemoreceptor-modulated inspiratory-related activity in HMNs. Co-immunoprecipitation and PLA assays indicated that p11 interacts with Munc13-1, a presynaptic active zone (AZ) protein for vesicle priming, presumably at excitatory inputs in the hypoglossal nucleus. Interference with p11 resulted in Munc13-1 downregulation, reduction in AZ length, and increased vesicle accumulation at excitatory boutons on HMNs, without affecting the number of docked vesicles at the AZ. p11 knockdown robustly reduced the synaptic strength of excitatory neurotransmission incoming to HMNs by affecting both the synchronous and asynchronous phases of neurotransmitter release. The decrease in synaptic strength was concurrent with a reduction in the size of the "functional" pool of readily releasable (RRP) vesicles and with the slowing down of the vesicle recruitment rate to replenish RRP.

conclusionp11 is proposed as a relevant mediator in the neurotransmitter release by regulating vesicle dynamics at central excitatory synapses. Here, p11 is highlighted as a multifaceted factor involved in neurotransmission and synaptic plasticity and, therefore, central for neural information processing.

Indexed as

Hypoglossal NerveMotor NeuronsS100 ProteinsSynapsesSynaptic TransmissionSynaptic VesiclesAnimalsExcitatory Postsynaptic PotentialsNerve Tissue ProteinsRatsRats, Sprague-DawleyS100 Calcium Binding Protein A10Nerve Tissue ProteinsS100 Calcium Binding Protein A10S100 ProteinsUnc13a protein, ratmotor neuronneurotransmitter releasereadily releasable pool (RRP)replenishment rate of RRPS100A10synchronous and asynchronous release

Identifiers

PMID41521833
PMCPMC12793959

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.