title: Signal co-operation between integrins and other receptor systems.
abstract: The multicellular nature of metazoans means that all cellular processes need to be tuned by adhesive interactions between cells and their local microenvironment. The spatial organization of cells within tissues requires sophisticated networks of extracellular signals to control their survival and proliferation, movements and positioning, and differentiated function. These cellular characteristics are mediated by multiple inputs from adhesion systems in combination with soluble and developmental signals. In the present review we explore how one class of adhesion receptor, the integrins, co-operate with other types of receptor to control diverse aspects of cell fate. In particular we discuss: (i) how beta3 and beta1 integrins work together with growth factors to control angiogenesis; (ii) how alpha6beta4 integrin co-operates with receptor tyrosine kinases in normal epithelial function and cancer; (iii) the interplay between beta1 integrins and EGF (epidermal growth factor) receptor; (iv) signal integration connecting integrins and cytokine receptors for interleukins, prolactin and interferons; and (v) how integrins and syndecans co-operate in cell migration.
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, U.K. cstreuli@manchester.ac.uk
authors.forename: Charles H
authors.initials: CH
authors.lastname: Streuli
authors.forename: Nasreen
authors.initials: N
authors.lastname: Akhtar
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000502:physiology*; D002453:Cell Cycle / Q000502:physiology; D002465:Cell Movement / Q000502:physiology; D002470:Cell Survival / Q000502:physiology; D066246:ErbB Receptors / Q000502:physiology; D005109:Extracellular Matrix / Q000502:physiology; D018507:Gene Expression Regulation, Developmental / Q000502:physiology; D039161:Integrin alpha6beta4 / Q000502:physiology; D039302:Integrin alphaVbeta3 / Q000502:physiology; D019012:Integrin beta1 / Q000502:physiology; D039661:Integrin beta3 / Q000502:physiology; D016023:Integrins / Q000502:physiology*; D007372:Interferons / Q000502:physiology; D009361:Neoplasm Invasiveness / Q000503:physiopathology; D009375:Neoplasms, Glandular and Epithelial / Q000503:physiopathology; D018919:Neovascularization, Physiologic / Q000187:drug effects / Q000502:physiology; D011388:Prolactin / Q000502:physiology; D020794:Receptor Protein-Tyrosine Kinases / Q000502:physiology; D018121:Receptors, Cytokine / Q000502:physiology; D017978:Receptors, Growth Factor / Q000502:physiology*; D018123:Receptors, Interleukin / Q000502:physiology; D017479:Receptors, Platelet-Derived Growth Factor / Q000502:physiology; D019030:Receptors, Vitronectin / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D053667:Syndecans / Q000502:physiology
chemical_list: D039161:Integrin alpha6beta4; D039302:Integrin alphaVbeta3; D019012:Integrin beta1; D039661:Integrin beta3; D016023:Integrins; D018121:Receptors, Cytokine; D017978:Receptors, Growth Factor; D018123:Receptors, Interleukin; D019030:Receptors, Vitronectin; D053667:Syndecans; C094340:integrin alphavbeta1; D011388:Prolactin; D007372:Interferons; D066246:ErbB Receptors; D020794:Receptor Protein-Tyrosine Kinases; D017479:Receptors, Platelet-Derived Growth Factor