Alternative molecular mechanisms for force transmission at adherens junctions via β-catenin-vinculin interaction

Simple item page
dc.article.number5608
dc.catalogadorjlo
dc.contributor.authorMorales-Camilo, Nicole
dc.contributor.authorLiu, Jingzhun
dc.contributor.authorRamírez Contador, Manuel José
dc.contributor.authorCanales Salgado, Patricio Andrés
dc.contributor.authorAlegría Fuentes, Juan José
dc.contributor.authorLiu, Xuyao
dc.contributor.authorOng, Ting Ong
dc.contributor.authorBarrera Rojas, Nelson Patricio
dc.contributor.authorFierro Huerta, Angélica María
dc.contributor.authorToyama, Yusuke
dc.contributor.authorGoult, Benjamin
dc.contributor.authorWang, Yilin
dc.contributor.authorMeng, Yue
dc.contributor.authorNishimura, Ryosuke
dc.contributor.authorFong-Ngern, Kedsarin
dc.contributor.authorLow, Christine Siok Lan
dc.contributor.authorKanchanawong, Pakorn
dc.contributor.authorYan, Jie
dc.contributor.authorRavasio, Andrea
dc.contributor.authorBertocchi, Cristina
dc.date.accessioned2024-08-22T15:09:04Z
dc.date.available2024-08-22T15:09:04Z
dc.date.issued2024
dc.description.abstractForce transmission through adherens junctions (AJs) is crucial for multicellular organization, wound healing and tissue regeneration. Recent studies shed light on the molecular mechanisms of mechanotransduction at the AJs. However, the canonical model fails to explain force transmission when essential proteins of the mechanotransduction module are mutated or missing. Here, we demonstrate that, in absence of α-catenin, β-catenin can directly and functionally interact with vinculin in its open conformation, bearing physiological forces. Furthermore, we found that β-catenin can prevent vinculin autoinhibition in the presence of α-catenin by occupying vinculin´s head-tail interaction site, thus preserving force transmission capability. Taken together, our findings suggest a multi-step force transmission process at AJs, where α-catenin and β-catenin can alternatively and cooperatively interact with vinculin. This can explain the graded responses needed to maintain tissue mechanical homeostasis and, importantly, unveils a force-bearing mechanism involving β-catenin and extended vinculin that can potentially explain the underlying process enabling collective invasion of metastatic cells lacking α-catenin.
dc.description.funderMinistry of Education
dc.description.funderNational University of Singapore
dc.description.funderPontificia Universidad Catolica de Chile
dc.description.funderMechanobiology Institute at National University of Singapore
dc.description.funderANID
dc.description.funderFondecyt
dc.description.funderSingapore Ministry of Education
dc.description.funderSingapore Ministry of Education
dc.description.funderSingapore National Research Foundation
dc.description.funderSingapore National Research Foundation
dc.description.funderSingapore National Research Foundation-Israel Science Foundation
dc.fechaingreso.objetodigital2024-08-22
dc.format.extent19 páginas
dc.fuente.origenSCOPUS
dc.identifier.doi10.1038/s41467-024-49850-5
dc.identifier.issn2041-1723
dc.identifier.scopusidSCOPUS_ID:85197526905
dc.identifier.urihttps://doi.org/10.1038/S41467-024-49850-5
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/87600
dc.information.autorucFacultad de Ciencias Biológicas; Ramírez Contador, Manuel José; S/I; 234221
dc.information.autorucInstituto de Ingeniería Biológica y Médica; Canales Salgado, Patricio Andrés; S/I; 1009434
dc.information.autorucFacultad de Ciencias Biológicas; Alegría Fuentes, Juan José; S/I; 1152994
dc.information.autorucFacultad de Ciencias Biológicas; Barrera Rojas, Nelson Patricio; 0000-0001-7825-1406; 4086
dc.information.autorucEscuela de Química; Fierro Huerta, Angélica María; 0000-0002-6507-4188; 218137
dc.language.isoen
dc.nota.accesocontenido completo
dc.revistaNature Communications
dc.rightsacceso abierto
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.subject.ods03 Good health and well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAlternative molecular mechanisms for force transmission at adherens junctions via β-catenin-vinculin interaction
dc.typeartículo
dc.volumen15
sipa.codpersvinculados234221
sipa.codpersvinculados1009434
sipa.codpersvinculados1152994
sipa.codpersvinculados4086
sipa.codpersvinculados218137
sipa.trazabilidadSCOPUS;2024-07-21
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
s41467-024-49850-5 (1).pdf
Size:
4.16 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Artículos de revistas