Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information

https://doi.org/10.1016/0955-0674(92)90100-QGet rights and content

Abstract

Adhesion receptors allow cells to interact with a dynamic and information-rich environment of extracellular matrix molecules. The integrin family of adhesion receptors transduces signals from the extracellular matrix that regulate growth, gene expression and differentiation, as well as cell shape, motility and cytoskeletal architecture. Recent data support the hypothesis that integrins transduce signals cooperatively with other classes of adhesion receptors or with growth factor receptors. Furthermore, the ability of integrins to interact with the cytoskeleton appears to be fundamental to their mechanism for signal transduction.

References (76)

  • S. Jaken et al.

    Association of Type 3 Protein Kinase C with Focal Contacts in Rat Embryo Fibroblasts

    J Cell Biol

    (1989)
  • M.M. Huang et al.

    Membrane Glycoprotein IV (CD36) Is Physically Associated with the Fyn, Lyn and Yes Protein-Tyrosine Kinases in Human Platelets

  • R. Talhouk et al.

    Coordinated Expression of Extracellular Matrix-Degrading Proteinases and their Inhibitors Regulates Mammary Epithelial Function during Involution

    J Cell Biol

    (1992)
  • A.H. Limper et al.

    Cell Surface Molecules that Bind Fibronectin's Matrix Assembly Domain

    J Biol Chem

    (1991)
  • R.P. Mecham

    Laminin Receptors

    Annu Rev Cell Biol

    (1991)
  • R.O. Hynes et al.

    Contact and Adhesive Specificities in the Associations, Migrations, and Targeting of Cells and Axons

    Cell

    (1992)
  • P. Kiefer et al.

    The Int-2/Fgf-3 Oncogene Product Is Secreted and Associates with Extracellular Matrix:Implications for Cell Transformation

    Mol Cell Biol

    (1991)
  • E.W. Raines et al.

    The Extracellular Glycoprotein SPARC Interacts with Platelet-Derived Growth Factor (PDGF)-AB and -BB and Inhibits the Binding of PDGF to Its Receptors

  • P. Santala et al.

    Regulation of Integrin-type Cell Adhesion Receptors by Cytokines

    J Biol Chem

    (1991)
  • A. Yamada et al.

    Activation of Human CD4 T-Lymphocytes. Interaction of Fibronectin with VLA-5 Receptor on CD4 Cells Induces the AP-1 Transcription Factor

    J Immunol

    (1991)
  • A. Shaw et al.

    Coordinate Interactions of Protein Tyrosine Kinases and Protein Tyrosine Phosphatases in T-cell Receptor-mediated Signalling

    Curr Opin Cell Biol

    (1991)
  • Y. Shimizu et al.

    Lymphocyte Interactions with Extracellular Matrix

    FASEB J

    (1991)
  • J.D. Esko

    Genetic Analysis of Proteoglycan Structure, Function and Metabolism

    Curr Opin Cell Biol

    (1991)
  • K.M. Yamada

    Adhesive Recognition Sequences

    J Biol Chem

    (1991)
  • M.J. Elices et al.

    Receptor Functions for the Integrin VLA-3: Fibronectin, Collagen, and Laminin Binding Are Differentially Influenced by Arg-Gly-Asp Peptide and by Divalent Cations

    J Cell Biol

    (1991)
  • W.E. Pullman et al.

    Cloning and Characterization of a Gene That Regulates Cell Adhesion

    Nature

    (1992)
  • A. Woods et al.

    Protein Kinase C Involvement in Focal Adhesion Formation

    J Cell Sci

    (1992)
  • D. Muir et al.

    Stromelysin Generates a Fibronectin Fragment That Inhibits Schwann Cell Proliferation

    J Cell Biol

    (1992)
  • Z. Werb et al.

    Signal Transduction through the Fibronectin Receptor Induces Collagenase and Stromelysin Gene Expression

    J Cell Biol

    (1989)
  • C.H. Damsky et al.

    Signal Transduction via the Fibronectin Receptor: Do Integrins Regulate Matrix Remodeling?

    Matrix

    (1992)
  • F. Grinnell et al.

    Degradation of Fibronectin and Vitronectin in Chronic Wound Fluid: Analysis by Cell Blotting, Immunoblotting, and Cell Adhesion Assays

    J Invest Dermatol

    (1992)
  • R. Chiquet-Ehrismann et al.

    Tenascin Variants: Differential Binding to Fibronectin and Distinct Distribution in Cell Cultures and Tissues

    Cell Regul

    (1991)
  • E.H. Sage et al.

    Extracellular Proteins That Modulate Cell-Matrix Interactions

    J Biol Chem

    (1991)
  • J.E. Murphy-Ullrich et al.

    Focal Adhesion Integrity Is Downregulated by the Alternatively Spliced Domain of Human Tenascin

    J Cell Biol

    (1991)
  • G. Schmidt et al.

    Interaction of the Small Proteoglycan Decorin with Fibronectin — Involvement of the Sequence NKISK of the Core Protein

    Biochem J

    (1991)
  • C.E. Turner et al.

    Transmembrane Molecular Assemblies in Cell-Extracellular Matrix Interactions

    Curr Opin Cell Biol

    (1991)
  • F.M. Pavalko et al.

    Disruption of the Actin Cytoskeleton after Microinjection of Proteolytic Fragments of α-Actinin

    J Cell Biol

    (1991)
  • A.A. Reszka et al.

    Identification of Amino Acid Sequences in the Integrin β1 Cytoplasmic Domain Implicated in Cytoskeletal Association

    J Cell Biol

    (1992)
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