Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation

Françoise Coussen, Daniel Choquet, Michael Sheetz, Harold P. Erickson

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10, on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.

Original languageEnglish (US)
Pages (from-to)2581-2590
Number of pages10
JournalJournal of Cell Science
Volume115
Issue number12
StatePublished - Jun 15 2002
Externally publishedYes

Fingerprint

Actin Cytoskeleton
Cell Adhesion
Integrins
Actins
Fibronectins
Fluorescence Microscopy
Ligands

Keywords

  • Cell adhesion
  • Dimerization
  • Fibronectin
  • Mutivalent
  • Oligomer
  • Signalling

ASJC Scopus subject areas

  • Cell Biology

Cite this

Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation. / Coussen, Françoise; Choquet, Daniel; Sheetz, Michael; Erickson, Harold P.

In: Journal of Cell Science, Vol. 115, No. 12, 15.06.2002, p. 2581-2590.

Research output: Contribution to journalArticle

Coussen, Françoise ; Choquet, Daniel ; Sheetz, Michael ; Erickson, Harold P. / Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation. In: Journal of Cell Science. 2002 ; Vol. 115, No. 12. pp. 2581-2590.
@article{6f0a3a1e4a6a4bd4bc8319ee1dc47142,
title = "Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation",
abstract = "Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10, on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.",
keywords = "Cell adhesion, Dimerization, Fibronectin, Mutivalent, Oligomer, Signalling",
author = "Fran{\cc}oise Coussen and Daniel Choquet and Michael Sheetz and Erickson, {Harold P.}",
year = "2002",
month = "6",
day = "15",
language = "English (US)",
volume = "115",
pages = "2581--2590",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "12",

}

TY - JOUR

T1 - Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation

AU - Coussen, Françoise

AU - Choquet, Daniel

AU - Sheetz, Michael

AU - Erickson, Harold P.

PY - 2002/6/15

Y1 - 2002/6/15

N2 - Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10, on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.

AB - Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10, on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.

KW - Cell adhesion

KW - Dimerization

KW - Fibronectin

KW - Mutivalent

KW - Oligomer

KW - Signalling

UR - http://www.scopus.com/inward/record.url?scp=0037096170&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037096170&partnerID=8YFLogxK

M3 - Article

VL - 115

SP - 2581

EP - 2590

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 12

ER -