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Molecular Insights into the Mechanism and Dynamics of Paxillin Binding to Focal Adhesions by Fluorescence Imaging Approaches

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Defense Thèse de doctorat : Univ. Genève, 2020 - Sc. Vie - Bioméd. 74 - 2020/09/28
Abstract Paxillin is a focal adhesion (FA) adapter protein that controls integrin-signaling. However, its binding mechanism to this complex is not understood. This study shows that compromising paxillin interactions with FAs causes rapid adhesion sliding, which could be rescued by inducing mechanical coupling of paxillin to integrins via bimolecular fluorescence complementation. While confirming the previously proposed FA-targeting function of the paxillin LIM domains, this work demonstrates specific contributions of each LIM domain to FA binding, which have been revealed by combining difference fluorescnce imaging approaches such as live cell imaging, photoactivation, FRAP, FA-isolation and bimolecular fluorescence complementation.
Keywords BiFCDynamicsFocal adhesionsIntegrinsLIM domainsPalmitoylationPaxillinPhotoactivationPlasma membraneTalin
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URN: urn:nbn:ch:unige-1471751
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Research group Migration cellulaire (645)
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FNS: 166384
FNS: 185261
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RIPAMONTI, Marta. Molecular Insights into the Mechanism and Dynamics of Paxillin Binding to Focal Adhesions by Fluorescence Imaging Approaches. Université de Genève. Thèse, 2020. doi: 10.13097/archive-ouverte/unige:147175 https://archive-ouverte.unige.ch/unige:147175

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Deposited on : 2021-01-13

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