Evidence map›Paper›PMID 40986063›Full record

ReviewCellular and molecular life sciences : CMLS2025

Bending the boundaries: the many facets of endophilin-As from membrane dynamics to disease.

Shiqiang Xu, Emilie Rigaux, Dorian Hène, Henri-François Renard, Louise Thines

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Shiqiang Xu *UNamur, Namur Research Institute in Life Sciences, Research Unit in Cell Biology, Rue de Bruxelles 61, B-5000, Namur, Belgium.ORCID http://orcid.org/0000-0002-0696-499X
Emilie Rigaux *UNamur, Namur Research Institute in Life Sciences, Research Unit in Cell Biology, Rue de Bruxelles 61, B-5000, Namur, Belgium.ORCID http://orcid.org/0000-0002-1943-1383
Dorian HèneUNamur, Namur Research Institute in Life Sciences, Research Unit in Cell Biology, Rue de Bruxelles 61, B-5000, Namur, Belgium.ORCID http://orcid.org/0009-0001-0498-9990
Henri-François RenardUNamur, Namur Research Institute in Life Sciences, Research Unit in Cell Biology, Rue de Bruxelles 61, B-5000, Namur, Belgium. henri-francois.renard@unamur.be.ORCID http://orcid.org/0000-0002-2406-2519
Louise ThinesUNamur, Namur Research Institute in Life Sciences, Research Unit in Cell Biology, Rue de Bruxelles 61, B-5000, Namur, Belgium. louise.thines@unamur.be.ORCID http://orcid.org/0009-0003-4208-4580

Funding

Fondation Francqui - Stichting Collen-Francqui Start-Up GrantFondation Roi Baudouin (BE) Crédits supplémentaires de fonctionnement en oncologieFondation Universitaire de Belgique (BE) AS-0602Fonds De La Recherche Scientifique - FNRS CDR-J.0176.24Fonds De La Recherche Scientifique - FNRS MIS-F.4540.21Fonds De La Recherche Scientifique - FNRS PhD Research FellowshipFonds De La Recherche Scientifique - FNRS Postdoctoral Research FellowshipFonds Spéciaux de Recherche PhD fellowshipHORIZON EUROPE Marie Sklodowska-Curie Actions 101151524Namur Research Institute for Life Sciences, UNamur (BE) Projet de Recherche CollaboratifUniversité de Namur Doctoral assistant fellowship
6 · The paper itself

Abstract

The endophilin-A proteins (EndoAs) are Bin/Amphiphysin/Rvs (BAR) domain proteins with key roles in both clathrin-mediated (CME) and clathrin-independent endocytosis (CIE). Humans have three differentially expressed EndoAs, EndoA1, -A2, and -A3, encoded by the SH3GL2/1/3 genes, respectively. Their functions primarily arise from their N-terminal BAR domain, which senses and induces local membrane curvature, and C-terminal SH3 domain, which mediates interactions with various proline-rich domain-containing partners. Among others, EndoA-mediated endocytosis coordinates synaptic vesicle recycling, as well as internalization of cell adhesion molecules, ligand-stimulated receptors, and pathogens. Consequently, EndoAs influence key cellular processes like neurotransmission, signaling, cell adhesion, and infection. Importantly, EndoA dysregulation has been observed in several pathologies, notably neurodegeneration, cardiovascular diseases, and cancer. This review provides an overview of the function and regulation of the EndoA proteins in CME and CIE, and explores their lesser-characterized involvement in other processes such as autophagy. It further addresses how these functions contribute to physiological processes and the development of pathologies, with a particular focus on cancer pathophysiology. Together, it emphasizes non-redundant roles of EndoA proteins in various cellular processes and highlights the complex relationship between membrane trafficking and diseases.

Indexed as

Adaptor Proteins, Signal TransducingCell MembraneAcyltransferasesAnimalsAutophagyEndocytosisHumansAcyltransferasesAdaptor Proteins, Signal TransducingAutophagyBAR domainCancerCell adhesionEENEndocytosisEndophilin-A1/2/3MigrationNeurodegenerationProliferationReceptorSH3GL2/1/3SignalingTrafficking

Identifiers

PMID40986063
PMCPMC12457278

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.