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Doctoral thesis
Open access
English

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

ContributorsRipamonti, Marta
Defense date2020-09-28
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.

eng
Keywords
  • BiFC
  • Dynamics
  • Focal adhesions
  • Integrins
  • LIM domains
  • Palmitoylation
  • Paxillin
  • Photoactivation
  • Plasma membrane
  • Talin
Funding
  • Swiss National Science Foundation - 166384
  • Swiss National Science Foundation - 185261
Citation (ISO format)
RIPAMONTI, Marta. Molecular Insights into the Mechanism and Dynamics of Paxillin Binding to Focal Adhesions by Fluorescence Imaging Approaches. 2020. doi: 10.13097/archive-ouverte/unige:147175
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Creation01/09/2021 11:37:00 AM
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