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Ligand binding regulates the directed movement of β1 integrins on fibroblasts

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Abstract

TO enable cells to crawl, adhesion receptors such as integrins must bind to extracellular molecules and simultaneously interact with force-generating components of the cytoskeleton1,2. We show here that the binding of extracellular ligand in living cells induces the attachment of β1 integrins to the retrograde-moving cytoskeleton. Unliganded integrins are not associated with the rearward-moving cytoskeleton: gold particles attached to β1 integrin by a monoclonal antibody diffuse in the membrane. However, addition of soluble RGD peptide (single-letter amino-acid code) or the use of fibronectin-coated gold particles causes the attachment of integrins to the rearward-moving cytoskeleton. Deletion of the β1 cytoplasmic tail blocks cytoskeletal attachment. The directed movement of integrins in response to ligand indicates that ligand binding is the critical step in regulating organized receptor movement on the cell surface and the migration of adherent cells.

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Authors and Affiliations

  1. Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Dan P. Felsenfeld, Daniel Choquet & Michael P. Sheetz

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  1. Dan P. Felsenfeld
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  2. Daniel Choquet
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  3. Michael P. Sheetz
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Felsenfeld, D., Choquet, D. & Sheetz, M. Ligand binding regulates the directed movement of β1 integrins on fibroblasts. Nature 383, 438–440 (1996). https://doi.org/10.1038/383438a0

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  • DOI: https://doi.org/10.1038/383438a0

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