Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins

Paola Defilippi, Cristina Olivo, Guido Tarone, Patrizia Mancini, Maria Rosaria Torrisi, Alessandra Eva

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The Dbl oncogene is the putative exchange factor for two small GTP-binding proteins, RhoA and CDC42 which are involved in the polymerization of actin to produce stress fibers and filopodia, respectively. We report here that Dbl oncogene-transformed NIH3T3 cells show actin stress fibers only when cells are plated on fibronectin. Plating of cells on collagen I and IV as well as on poly-D-lysine and gelatin induces polymerization of actin to form filopodia, lamellipodia and membrane ruffles but not stress fibers. The putative collagen receptors, α1/β1 and α2/β1 integrins are expressed at reduced level in Dbl-transformed cells compared to untransformed NIH3T3 fibroblasts. Nevertheless, adhesion to collagens is not altered. Inhibitory monoclonal antibody to mouse integrin β1 subunit blocked adhesion of both Dbl-transformed and untransformed NIH3T3 cells, demonstrating that adhesion to collagen I and IV is mediated by the β1 family of integrins. Dbl product rapidly induces the depolymerization of actin stress fibers, rounding up of the cells, and formation of filopodia and lamellipodia when microinjected in NIH3T3 cells plated on gelatin. Thus, Dbl may exert its effect on actin cytoskeleton organization in response to extracellular proteins by altering integrin-mediated signalling pathways.

Original languageEnglish
Pages (from-to)1933-1943
Number of pages11
JournalOncogene
Volume14
Issue number16
Publication statusPublished - 1997

Fingerprint

Extracellular Matrix Proteins
Pseudopodia
Actin Cytoskeleton
Cell Adhesion
Polymerization
Stress Fibers
Fibroblasts
Integrins
Actins
Collagen
Gelatin
Oncogenes
rhoA GTP-Binding Protein
Collagen Receptors
Fibronectins
Lysine
Monoclonal Antibodies
Membranes
Proteins

Keywords

  • Dbl
  • Integrins
  • Stress fibers

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

Cite this

Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins. / Defilippi, Paola; Olivo, Cristina; Tarone, Guido; Mancini, Patrizia; Torrisi, Maria Rosaria; Eva, Alessandra.

In: Oncogene, Vol. 14, No. 16, 1997, p. 1933-1943.

Research output: Contribution to journalArticle

Defilippi, Paola ; Olivo, Cristina ; Tarone, Guido ; Mancini, Patrizia ; Torrisi, Maria Rosaria ; Eva, Alessandra. / Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins. In: Oncogene. 1997 ; Vol. 14, No. 16. pp. 1933-1943.
@article{090a602d00c74744bd265521bb4a8cc3,
title = "Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins",
abstract = "The Dbl oncogene is the putative exchange factor for two small GTP-binding proteins, RhoA and CDC42 which are involved in the polymerization of actin to produce stress fibers and filopodia, respectively. We report here that Dbl oncogene-transformed NIH3T3 cells show actin stress fibers only when cells are plated on fibronectin. Plating of cells on collagen I and IV as well as on poly-D-lysine and gelatin induces polymerization of actin to form filopodia, lamellipodia and membrane ruffles but not stress fibers. The putative collagen receptors, α1/β1 and α2/β1 integrins are expressed at reduced level in Dbl-transformed cells compared to untransformed NIH3T3 fibroblasts. Nevertheless, adhesion to collagens is not altered. Inhibitory monoclonal antibody to mouse integrin β1 subunit blocked adhesion of both Dbl-transformed and untransformed NIH3T3 cells, demonstrating that adhesion to collagen I and IV is mediated by the β1 family of integrins. Dbl product rapidly induces the depolymerization of actin stress fibers, rounding up of the cells, and formation of filopodia and lamellipodia when microinjected in NIH3T3 cells plated on gelatin. Thus, Dbl may exert its effect on actin cytoskeleton organization in response to extracellular proteins by altering integrin-mediated signalling pathways.",
keywords = "Dbl, Integrins, Stress fibers",
author = "Paola Defilippi and Cristina Olivo and Guido Tarone and Patrizia Mancini and Torrisi, {Maria Rosaria} and Alessandra Eva",
year = "1997",
language = "English",
volume = "14",
pages = "1933--1943",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "16",

}

TY - JOUR

T1 - Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins

AU - Defilippi, Paola

AU - Olivo, Cristina

AU - Tarone, Guido

AU - Mancini, Patrizia

AU - Torrisi, Maria Rosaria

AU - Eva, Alessandra

PY - 1997

Y1 - 1997

N2 - The Dbl oncogene is the putative exchange factor for two small GTP-binding proteins, RhoA and CDC42 which are involved in the polymerization of actin to produce stress fibers and filopodia, respectively. We report here that Dbl oncogene-transformed NIH3T3 cells show actin stress fibers only when cells are plated on fibronectin. Plating of cells on collagen I and IV as well as on poly-D-lysine and gelatin induces polymerization of actin to form filopodia, lamellipodia and membrane ruffles but not stress fibers. The putative collagen receptors, α1/β1 and α2/β1 integrins are expressed at reduced level in Dbl-transformed cells compared to untransformed NIH3T3 fibroblasts. Nevertheless, adhesion to collagens is not altered. Inhibitory monoclonal antibody to mouse integrin β1 subunit blocked adhesion of both Dbl-transformed and untransformed NIH3T3 cells, demonstrating that adhesion to collagen I and IV is mediated by the β1 family of integrins. Dbl product rapidly induces the depolymerization of actin stress fibers, rounding up of the cells, and formation of filopodia and lamellipodia when microinjected in NIH3T3 cells plated on gelatin. Thus, Dbl may exert its effect on actin cytoskeleton organization in response to extracellular proteins by altering integrin-mediated signalling pathways.

AB - The Dbl oncogene is the putative exchange factor for two small GTP-binding proteins, RhoA and CDC42 which are involved in the polymerization of actin to produce stress fibers and filopodia, respectively. We report here that Dbl oncogene-transformed NIH3T3 cells show actin stress fibers only when cells are plated on fibronectin. Plating of cells on collagen I and IV as well as on poly-D-lysine and gelatin induces polymerization of actin to form filopodia, lamellipodia and membrane ruffles but not stress fibers. The putative collagen receptors, α1/β1 and α2/β1 integrins are expressed at reduced level in Dbl-transformed cells compared to untransformed NIH3T3 fibroblasts. Nevertheless, adhesion to collagens is not altered. Inhibitory monoclonal antibody to mouse integrin β1 subunit blocked adhesion of both Dbl-transformed and untransformed NIH3T3 cells, demonstrating that adhesion to collagen I and IV is mediated by the β1 family of integrins. Dbl product rapidly induces the depolymerization of actin stress fibers, rounding up of the cells, and formation of filopodia and lamellipodia when microinjected in NIH3T3 cells plated on gelatin. Thus, Dbl may exert its effect on actin cytoskeleton organization in response to extracellular proteins by altering integrin-mediated signalling pathways.

KW - Dbl

KW - Integrins

KW - Stress fibers

UR - http://www.scopus.com/inward/record.url?scp=0030929154&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030929154&partnerID=8YFLogxK

M3 - Article

C2 - 9150360

AN - SCOPUS:0030929154

VL - 14

SP - 1933

EP - 1943

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 16

ER -