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Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells

As adhesion molecules, integrins connect a cell to its environment and transduce signals across the membrane. Their different functional states correspond to distinct conformations. Using a biomembrane force probe, we observed real-time reversible switches between bent and extended conformations of... Full description

Journal Title: The Journal of cell biology 29 October 2012, Vol.199(3), pp.497-512
Main Author: Chen, Wei
Other Authors: Lou, Jizhong , Evans, Evan A , Zhu, Cheng
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1540-8140 ; PMID: 23109670 Version:1 ; DOI: 10.1083/jcb.201201091
Link: http://pubmed.gov/23109670
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recordid: medline23109670
title: Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells
format: Article
creator:
  • Chen, Wei
  • Lou, Jizhong
  • Evans, Evan A
  • Zhu, Cheng
subjects:
  • Cell Adhesion -- Physiology
  • Cell Membrane -- Metabolism
  • Intercellular Adhesion Molecule-1 -- Metabolism
  • Lymphocyte Function-Associated Antigen-1 -- Chemistry
ispartof: The Journal of cell biology, 29 October 2012, Vol.199(3), pp.497-512
description: As adhesion molecules, integrins connect a cell to its environment and transduce signals across the membrane. Their different functional states correspond to distinct conformations. Using a biomembrane force probe, we observed real-time reversible switches between bent and extended conformations of a single integrin, α(L)β(2), on the surface of a living cell by measuring its nanometer-scale headpiece displacements, bending and unbending frequencies, and molecular stiffness changes. We determined the stabilities of these conformations, their dynamic equilibrium, speeds and rates of conformational changes, and the impact of divalent cations and tensile forces. We quantified how initial and subsequent conformations of α(L)β(2) regulate the force-dependent kinetics of dissociation from intercellular adhesion molecule 1. Our findings provide new insights into how integrins function as nanomachines to precisely control cell adhesion and signaling.
language: eng
source:
identifier: E-ISSN: 1540-8140 ; PMID: 23109670 Version:1 ; DOI: 10.1083/jcb.201201091
fulltext: fulltext
issn:
  • 15408140
  • 1540-8140
url: Link


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subjectCell Adhesion -- Physiology ; Cell Membrane -- Metabolism ; Intercellular Adhesion Molecule-1 -- Metabolism ; Lymphocyte Function-Associated Antigen-1 -- Chemistry
descriptionAs adhesion molecules, integrins connect a cell to its environment and transduce signals across the membrane. Their different functional states correspond to distinct conformations. Using a biomembrane force probe, we observed real-time reversible switches between bent and extended conformations of a single integrin, α(L)β(2), on the surface of a living cell by measuring its nanometer-scale headpiece displacements, bending and unbending frequencies, and molecular stiffness changes. We determined the stabilities of these conformations, their dynamic equilibrium, speeds and rates of conformational changes, and the impact of divalent cations and tensile forces. We quantified how initial and subsequent conformations of α(L)β(2) regulate the force-dependent kinetics of dissociation from intercellular adhesion molecule 1. Our findings provide new insights into how integrins function as nanomachines to precisely control cell adhesion and signaling.
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abstractAs adhesion molecules, integrins connect a cell to its environment and transduce signals across the membrane. Their different functional states correspond to distinct conformations. Using a biomembrane force probe, we observed real-time reversible switches between bent and extended conformations of a single integrin, α(L)β(2), on the surface of a living cell by measuring its nanometer-scale headpiece displacements, bending and unbending frequencies, and molecular stiffness changes. We determined the stabilities of these conformations, their dynamic equilibrium, speeds and rates of conformational changes, and the impact of divalent cations and tensile forces. We quantified how initial and subsequent conformations of α(L)β(2) regulate the force-dependent kinetics of dissociation from intercellular adhesion molecule 1. Our findings provide new insights into how integrins function as nanomachines to precisely control cell adhesion and signaling.
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