Adhesion in cell migration

https://doi.org/10.1016/0955-0674(95)80112-XGet rights and content

Abstract

Adhesive interactions play a central role in cell migration. The regulation of these interactions requires the coordination of a multiplicity of signals, both spatially and temporally. The role of the integrin family has received considerable recent attention. Progress has been made in the elucidation of the mechanisms by which growth factors and other motogenic factors stimulate migration. Major advances have also been made in understanding the mechanisms by which the formation and breakdown of adhesive complexes are regulated, including the participation of members of the rho family. Despite these advances, many important questions remain, and the field seems well positioned to answer them.

References (136)

  • P Tremble et al.

    SPARC: a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway

    J Cell Biol

    (1993)
  • JE Murphy-Ullrich et al.

    Thrombospondin modulates focal adhesions in endothelial cells

    J Cell Biol

    (1989)
  • P Chen et al.

    Cell movement elicited by epidermal growth factor receptor requires kinase and autophosphorylation but is separable from mitogenesis

    J Cell Biol

    (1994)
  • S Wennstrom et al.

    Membrane ruffling and chemotaxis transduced by the PDGF β-receptor require the binding site for phosphatidylinositol 3′ kinase

    Oncogene

    (1994)
  • J-L Duband et al.

    Neural crest cell locomotion induced by antibodies to β1 integrins

    J Cell Sci

    (1991)
  • F Balzac et al.

    Expression of β1b integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility

    J Cell Biol

    (1994)
  • CE Schmidt et al.

    Integrin cytoskeletal interactions in migrating fibroblasts are dynamic, asymmetric, and regulated

    J Cell Biol

    (1993)
  • AJ Ridley et al.

    Rho family GTPase activating proteins p190bcr and rhoGAP show distinct specificities in vitro and in vivo

    EMBO J

    (1993)
  • AJ Ridley et al.

    Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase

    EMBO J

    (1994)
  • MJ Seckl et al.

    Guanosine 5'-3-O-(Thio)-triphosphate stimulates tyrosine phosphorylation of p125FAK and paxillin in permeabilized Swiss 3T3 cells: role of p21rho

    J Biol Chem

    (1995)
  • J Zhang et al.

    Activation of platelet phosphatidylinositide 3—kinase requires the small GTP-binding protein Rho

    J Biol Chem

    (1993)
  • M Bronner-Fraser

    Neural crest cell formation and migration in the developing embryo

    FASEB J

    (1994)
  • PA Appeddu et al.

    Molecular analysis of cell surface β1,4 galactosyltransferase function during cell migration

    Proc Natl Acad Sci USA

    (1994)
  • TP Stossel

    On the crawling of animal cells

    Science

    (1993)
  • RL Juliano et al.

    Signal transduction from the extracellular matrix

    J Cell Biol

    (1993)
  • MA Schwartz et al.

    Integrating with integrins

    Mol Cell Biol

    (1994)
  • EA Clark et al.

    Integrins and signal transduction pathways: the road taken

    Science

    (1995)
  • CY Wu et al.

    The role of α4β1 integrin in cell motility and fibronectin matrix assembly

    J Cell Sci

    (1995)
  • BMC Chan et al.

    In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells

    Science

    (1990)
  • R Fassler et al.

    Lack of β1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts

    J Cell Biol

    (1995)
  • REB Seftor et al.

    Role of the αvβ3 integrin in human melanoma cell invasion

    Proc Nat Acad Sci USA

    (1992)
  • PC Brooks et al.

    Requirement of vascular integrin αvβ3 for angiogenesis

    Science

    (1994)
  • TA Springer

    Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration

    Annu Rev Physiol

    (1995)
  • A Beauvais et al.

    Changes in the fibronectin-specific integrin expression pattern modify the migratory behavior of sarcoma S180 cells in vitro and in the embryonic environment

    J Cell Biol

    (1995)
  • JR Dunlevy et al.

    Controlled induction of focal adhesion disassembly and migration in primary fibroblasts

    J Cell Sci

    (1993)
  • CE Turner et al.

    Transmembrane molecular assemblies in cell—extracellular matrix interactions

    Curr Opin Cell Biol

    (1991)
    SH Lo et al.

    Focal adhesion as a signal transduction organelle

    Cancer Metastasis Rev

    (1994)
  • A Horwitz et al.

    Interaction of plasma membrane fibronectin receptor with talin — a transmembrane linkage

    Nature

    (1986)
  • C Otey et al.

    An interaction between α-actinin and the β1 integrin subunit in vitro

    J Cell Biol

    (1990)
  • JM Lewis et al.

    Mapping in vivo associations of cytoplasmic proteins with integrin β1 cytoplasmic domain mutants

    J Cell Sci

    (1995)
  • JLR Fernandez et al.

    Overexpression of vinculin suppresses cell motility in Balb/C 3T3 cells

    Cell Motil Cytoskeleton

    (1992)
  • JLR Fernandez et al.

    Suppression of vinculin expression by antisense transfection confers changes in cell morphology, motility, and anchorage dependent growth of 3T3 cells

    J Cell Biol

    (1993)
  • U Gluck et al.

    Modulation of alpha actinin levels affects cell motility and confers tumorigenicity on 3T3 cells

    J Cell Sci

    (1994)
  • GH Nuckolls et al.

    Microinjection of antibodies against talin inhibits the spreading and migration of fibroblasts

    J Cell Sci

    (1992)
  • S Miyamoto et al.

    Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function

    Science

    (1995)
  • NS Bartfield et al.

    The αvβ3 integrin associates with a 190 kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor

    J Biol Chem

    (1993)
  • J Ylanne et al.

    Localization of β1, β3, α5, αv and αIIb subunits of the integrin family in spreading human erytholeukemia cells

    Blood

    (1990)
  • EA Wayner et al.

    Integrins αvβ3 and αvβ5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface

    J Cell Biol

    (1991)
  • K Vuori et al.

    Association of insulin receptor substrate-1 with integrins

    Science

    (1994)
  • DD Schlaepfer et al.

    Integrin mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase

    Nature

    (1994)
  • M Manske et al.

    Growth factor-induced cell migration: biology and methods of analysis

    Int Rev Cytol

    (1994)
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