Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncb3456
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dc.titleNanoscale architecture of cadherin-based cell adhesions
dc.contributor.authorBertocchi, Cristina
dc.contributor.authorWang, Yilin
dc.contributor.authorRavasio, Andrea
dc.contributor.authorHara, Yusuke
dc.contributor.authorWu, Yao
dc.contributor.authorSailov, Talgat
dc.contributor.authorBaird, Michelle A
dc.contributor.authorDavidson, Michael W
dc.contributor.authorZaidel-Bar, Ronen
dc.contributor.authorToyama, Yusuke
dc.contributor.authorLadoux, Benoit
dc.contributor.authorMege, Rene-Marc
dc.contributor.authorKanchanawong, Pakorn
dc.date.accessioned2021-07-13T09:13:58Z
dc.date.available2021-07-13T09:13:58Z
dc.date.issued2017-01-01
dc.identifier.citationBertocchi, Cristina, Wang, Yilin, Ravasio, Andrea, Hara, Yusuke, Wu, Yao, Sailov, Talgat, Baird, Michelle A, Davidson, Michael W, Zaidel-Bar, Ronen, Toyama, Yusuke, Ladoux, Benoit, Mege, Rene-Marc, Kanchanawong, Pakorn (2017-01-01). Nanoscale architecture of cadherin-based cell adhesions. NATURE CELL BIOLOGY 19 (1) : 28-37. ScholarBank@NUS Repository. https://doi.org/10.1038/ncb3456
dc.identifier.issn14657392
dc.identifier.issn14764679
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/194056
dc.description.abstractMulticellularity in animals requires dynamic maintenance of cell-cell contacts. Intercellularly ligated cadherins recruit numerous proteins to form supramolecular complexes that connect with the actin cytoskeleton and support force transmission. However, the molecular organization within such structures remains unknown. Here we mapped protein organization in cadherin-based adhesions by super-resolution microscopy, revealing a multi-compartment nanoscale architecture, with the plasma-membrane-proximal cadherin-catenin compartment segregated from the actin cytoskeletal compartment, bridged by an interface zone containing vinculin. Vinculin position is determined by α-catenin, and following activation, vinculin can extend â 1/430 nm to bridge the cadherin-catenin and actin compartments, while modulating the nanoscale positions of the actin regulators zyxin and VASP. Vinculin conformational activation requires tension and tyrosine phosphorylation, regulated by Abl kinase and PTP1B phosphatase. Such modular architecture provides a structural framework for mechanical and biochemical signal integration by vinculin, which may differentially engage cadherin-catenin complexes with the actomyosin machinery to regulate cell adhesions.
dc.language.isoen
dc.publisherNATURE PUBLISHING GROUP
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectCell Biology
dc.subjectALPHA-CATENIN
dc.subjectVINCULIN
dc.subjectACTIN
dc.subjectMICROSCOPY
dc.subjectTENSION
dc.subjectCOMPLEX
dc.subjectBINDING
dc.subjectCONTRACTILITY
dc.subjectORGANIZATION
dc.subjectASSOCIATION
dc.typeArticle
dc.date.updated2021-07-13T08:19:18Z
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentDEPT OF BIOMEDICAL ENGINEERING
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.1038/ncb3456
dc.description.sourcetitleNATURE CELL BIOLOGY
dc.description.volume19
dc.description.issue1
dc.description.page28-37
dc.published.statePublished
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