title: How integrins control mammary epithelial differentiation: a possible role for the ILK-PINCH-Parvin complex.
abstract: Differentiation into tissue-specific cell types occurs in response to numerous external signals. Integrins impart signals from the extracellular matrix microenvironment that are required for cell differentiation. However, the precise cytoplasmic transducers of these signals are yet to be understood properly. In lactating mammary epithelial cells, integrin-linked kinase has been identified as an indispensable integrin-signalling adaptor that enables the activation of Rac1, which is necessary for prolactin-induced milk protein expression. Here we use examples from various tissues to summarise possible mechanisms by which ILK and its binding partners PINCH and Parvin (ILK-PINCH-Parvin complex) could be required for Rac activation and mammary epithelial differentiation.
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences and Manchester Breast Centre, University of Manchester, Manchester, UK.
authors.forename: Nicholas
authors.initials: N
authors.lastname: Rooney
authors.forename: Charles H
authors.initials: CH
authors.lastname: Streuli
mesh_terms: D000185:Actinin / Q000378:metabolism*; D000818:Animals; D002454:Cell Differentiation; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004847:Epithelial Cells / Q000166:cytology* / Q000201:enzymology / Q000378:metabolism; D016023:Integrins / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000166:cytology*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D000099200:Scaffold Protein ILK
chemical_list: D000185:Actinin; D004268:DNA-Binding Proteins; D016023:Integrins; D017346:Protein Serine-Threonine Kinases; D000099200:Scaffold Protein ILK