Ligand binding regulates the directed movement of β1 integrins on fibroblasts

Dan P. Felsenfeld, Daniel Choquet, Michael P. Sheetz
Nature. 1996-10-01; 383(6599): 438-440
DOI: 10.1038/383438a0

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1. Nature. 1996 Oct 3;383(6599):438-40.

Ligand binding regulates the directed movement of beta1 integrins on fibroblasts.

Felsenfeld DP(1), Choquet D, Sheetz MP.

Author information:
(1)Department of Cell Biology, Duke University Medical Center, Durham, North
Carolina 27710, USA.

Comment in
Nature. 1996 Oct 3;383(6599):390-1.

To enable cells to crawl, adhesion receptors such as integrins must bind to
extracellular molecules and simultaneously interact with force-generating
components of the cytoskeleton. We show here that the binding of extracellular
ligand in living cells induces the attachment of beta1 integrins to the
retrograde-moving cytoskeleton. Unliganded integrins are not associated with the
rearward-moving cytoskeleton: gold particles attached to beta1 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 beta1 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.

DOI: 10.1038/383438a0
PMID: 8837776 [Indexed for MEDLINE]

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