Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions

Marina E. Chicurel, Robert H. Singer, Christian J. Meyer, Donald E. Ingber

Research output: Contribution to journalArticle

287 Citations (Scopus)

Abstract

The extracellular matrix (ECM) activates signalling pathways that control cell behaviour by binding to cell-surface integrin receptors and inducing the formation of focal adhesion complexes (FACs). In addition to clustered integrins, FACs contain proteins that mechanically couple the integrins to the cytoskeleton and to immobilized signal-transducing molecules. Cell adhesion to the ECM also induces a rapid increase in the translation of preexisting messenger RNAs. Gene expression can be controlled locally by targeting mRNAs to specialized cytoskeletal domains. Here we investigate whether cell binding to the ECM promotes formation of a cytoskeletal microcompartment specialized for translational control at the site of integrin binding. High-resolution in situ hybridization revealed that mRNA and ribosomes rapidly and specifically localized to FACs that form when cells bind to ECM-coated microbeads. Relocation of these protein synthesis components to the FAC depended on the ability of integrins to mechanically couple the ECM to the contractile cytoskeleton and on associated tension- moulding of the actin lattice. Our results suggest a new type of gene regulation by integrins and by mechanical stress which may involve translation of mRNAs into proteins near the sites of signal reception.

Original languageEnglish (US)
Pages (from-to)730-733
Number of pages4
JournalNature
Volume392
Issue number6677
DOIs
StatePublished - Apr 16 1998

Fingerprint

Focal Adhesions
Ribosomes
Integrins
Extracellular Matrix
Messenger RNA
Cytoskeleton
Mechanical Stress
Proteins
Behavior Control
Aptitude
Cell Surface Receptors
Protein Biosynthesis
Microspheres
Cell Adhesion
In Situ Hybridization
Actins
Binding Sites
Gene Expression
Genes

ASJC Scopus subject areas

  • General

Cite this

Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions. / Chicurel, Marina E.; Singer, Robert H.; Meyer, Christian J.; Ingber, Donald E.

In: Nature, Vol. 392, No. 6677, 16.04.1998, p. 730-733.

Research output: Contribution to journalArticle

Chicurel, Marina E. ; Singer, Robert H. ; Meyer, Christian J. ; Ingber, Donald E. / Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions. In: Nature. 1998 ; Vol. 392, No. 6677. pp. 730-733.
@article{fae2094f84e64f199f45332410a73a56,
title = "Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions",
abstract = "The extracellular matrix (ECM) activates signalling pathways that control cell behaviour by binding to cell-surface integrin receptors and inducing the formation of focal adhesion complexes (FACs). In addition to clustered integrins, FACs contain proteins that mechanically couple the integrins to the cytoskeleton and to immobilized signal-transducing molecules. Cell adhesion to the ECM also induces a rapid increase in the translation of preexisting messenger RNAs. Gene expression can be controlled locally by targeting mRNAs to specialized cytoskeletal domains. Here we investigate whether cell binding to the ECM promotes formation of a cytoskeletal microcompartment specialized for translational control at the site of integrin binding. High-resolution in situ hybridization revealed that mRNA and ribosomes rapidly and specifically localized to FACs that form when cells bind to ECM-coated microbeads. Relocation of these protein synthesis components to the FAC depended on the ability of integrins to mechanically couple the ECM to the contractile cytoskeleton and on associated tension- moulding of the actin lattice. Our results suggest a new type of gene regulation by integrins and by mechanical stress which may involve translation of mRNAs into proteins near the sites of signal reception.",
author = "Chicurel, {Marina E.} and Singer, {Robert H.} and Meyer, {Christian J.} and Ingber, {Donald E.}",
year = "1998",
month = "4",
day = "16",
doi = "10.1038/33719",
language = "English (US)",
volume = "392",
pages = "730--733",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6677",

}

TY - JOUR

T1 - Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions

AU - Chicurel, Marina E.

AU - Singer, Robert H.

AU - Meyer, Christian J.

AU - Ingber, Donald E.

PY - 1998/4/16

Y1 - 1998/4/16

N2 - The extracellular matrix (ECM) activates signalling pathways that control cell behaviour by binding to cell-surface integrin receptors and inducing the formation of focal adhesion complexes (FACs). In addition to clustered integrins, FACs contain proteins that mechanically couple the integrins to the cytoskeleton and to immobilized signal-transducing molecules. Cell adhesion to the ECM also induces a rapid increase in the translation of preexisting messenger RNAs. Gene expression can be controlled locally by targeting mRNAs to specialized cytoskeletal domains. Here we investigate whether cell binding to the ECM promotes formation of a cytoskeletal microcompartment specialized for translational control at the site of integrin binding. High-resolution in situ hybridization revealed that mRNA and ribosomes rapidly and specifically localized to FACs that form when cells bind to ECM-coated microbeads. Relocation of these protein synthesis components to the FAC depended on the ability of integrins to mechanically couple the ECM to the contractile cytoskeleton and on associated tension- moulding of the actin lattice. Our results suggest a new type of gene regulation by integrins and by mechanical stress which may involve translation of mRNAs into proteins near the sites of signal reception.

AB - The extracellular matrix (ECM) activates signalling pathways that control cell behaviour by binding to cell-surface integrin receptors and inducing the formation of focal adhesion complexes (FACs). In addition to clustered integrins, FACs contain proteins that mechanically couple the integrins to the cytoskeleton and to immobilized signal-transducing molecules. Cell adhesion to the ECM also induces a rapid increase in the translation of preexisting messenger RNAs. Gene expression can be controlled locally by targeting mRNAs to specialized cytoskeletal domains. Here we investigate whether cell binding to the ECM promotes formation of a cytoskeletal microcompartment specialized for translational control at the site of integrin binding. High-resolution in situ hybridization revealed that mRNA and ribosomes rapidly and specifically localized to FACs that form when cells bind to ECM-coated microbeads. Relocation of these protein synthesis components to the FAC depended on the ability of integrins to mechanically couple the ECM to the contractile cytoskeleton and on associated tension- moulding of the actin lattice. Our results suggest a new type of gene regulation by integrins and by mechanical stress which may involve translation of mRNAs into proteins near the sites of signal reception.

UR - http://www.scopus.com/inward/record.url?scp=0032537124&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032537124&partnerID=8YFLogxK

U2 - 10.1038/33719

DO - 10.1038/33719

M3 - Article

VL - 392

SP - 730

EP - 733

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6677

ER -