Publicación:
Combined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosis

Vista sencilla de ítem
dc.contributor.authorMaestro, Armando
dc.contributor.authorZaccai, Nathan R.
dc.contributor.authorGonzález Martínez, Juan F.
dc.contributor.authorSánchez Puga, Pablo
dc.contributor.authorTajuelo Rodríguez, Javier
dc.contributor.authorRubio Álvarez, Miguel Ángel
dc.contributor.authorSanta María, Andreas
dc.contributor.authorCarrascosa Tejedor, Javier
dc.contributor.authorPereira, Daniel
dc.contributor.authorMontesinos Marín, Idelfonso
dc.contributor.authorGutfreund, Philipp
dc.contributor.authorCampbell, Richard
dc.contributor.authorKotar, Jurij
dc.contributor.authorKelly, Bernard T.
dc.contributor.authorCicuta, Pietro
dc.contributor.authorOwen, David J.
dc.date.accessioned2026-02-20T12:23:30Z
dc.date.available2026-02-20T12:23:30Z
dc.date.issued2025-08-12
dc.descriptionThe registered version of this article, first published in “Communications Biology 8 (2025), 1196", is available online at the publisher's website: Nature Research, https://doi.org/10.1038/s42003-025-08597-5
dc.descriptionLa versión registrada de este artículo, publicado por primera vez en “Communications Biology 8 (2025), 1196", está disponible en línea en el sitio web del editor: Nature Research, https://doi.org/10.1038/s42003-025-08597-5
dc.description.abstractClathrin-mediated endocytosis (CME), the main mechanism for swift, selective protein uptake in eukaryotic cells, initiates with adaptor protein AP2 recruitment to the plasma membrane (PM). AP2 recognizes PM-associated PtdIns(4,5)P2 and protein cargo for internalization. Nonetheless, many aspects of this process remain unclear due to their in vivo complexity. Here, a thermodynamic and time-resolved structural analysis of AP2 binding to different biomimetic PM was undertaken under physiological conditions using a combination of neutron reflectometry, interfacial tensiometry and rheology, and atomic force microscopy. The resultant in vitro data replicated previous in vivo observations, as well as yielded biophysical insights into normal and aborted CME. The presence of cargo may not be pivotal for the “activating” conformational change of AP2. However, the presence of cargo extends AP2’s residence time on the membrane surface, due to slower on- and off-rates, thereby tentatively giving sufficient time for CME to proceed fully. Moreover, upon interaction with AP2, phospholipid lateral diffusion decreases markedly, inducing a gel phase attributed to creating a percolated network involving AP2 on the membrane, which could potentially serve as a mechanism for modulating subsequent clathrin binding. The subsequent clathrin polymerization at the membrane is dependent on the AP2’s clathrin binding sequence.en
dc.description.provenanceMade available in DSpace on 2026-02-20T12:23:30Z (GMT). No. of bitstreams: 1 Combined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosis. Javier Tajuelo.pdf: 2811283 bytes, checksum: cfe4d65d03dbd7bc25d1a8e57707c43c (MD5) Previous issue date: 2025-08-12en
dc.description.versionversión publicada
dc.identifier.citationMaestro, A., Zaccai, N.R., Gonzalez-Martinez, J.F. et al., (2025). Combined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosis. Commun Biol 8, 1196. https://doi.org/10.1038/s42003-025-08597-5
dc.identifier.doihttps://doi.org/10.1038/s42003-025-08597-5
dc.identifier.eissn2399-3642
dc.identifier.urihttps://hdl.handle.net/20.500.14468/31876
dc.journal.titleCommunications Biology
dc.journal.volume8
dc.language.isoen
dc.page.final13
dc.page.initial1
dc.publisherNature Research
dc.relation.centerFacultad de Ciencias
dc.relation.departmentFísica Interdisciplinar
dc.relation.researchgroupGrupo de investigación de materia blanda y fluidos
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject2406 Biofísica
dc.titleCombined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosisen
dc.typeartículoes
dc.typejournal articleen
dspace.entity.typePublication
relation.isAuthorOfPublicationf6b576e9-92f7-414e-bc62-6ef2e5eddedd
relation.isAuthorOfPublication283ce738-b7b4-4df7-a7d7-4903d7d0eba6
relation.isAuthorOfPublication.latestForDiscoveryf6b576e9-92f7-414e-bc62-6ef2e5eddedd
Archivos
Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
Combined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosis. Javier Tajuelo.pdf
Tamaño:
2.68 MB
Formato:
Adobe Portable Document Format
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
license.txt
Tamaño:
3.62 KB
Formato:
Item-specific license agreed to upon submission
Descripción:
Descargar
Colecciones
Artículos y papers