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Journal of Cell Science, Vol 114, Issue 6 1137-1144, Copyright © 2001 by Company of Biologists
JOURNAL ARTICLES |
MD Henry, JS Satz, C Brakebusch, M Costell, E Gustafsson, R Fassler and KP Campbell
Howard Hughes Medical Institute, University of Iowa College of Medicine, Department of Physiology and Biophysics and Department of Neurology, Iowa City, IA 52242, USA. kevin-campbell@uiowa.edu
Dystroglycan (DG) is a cell surface receptor for several extracellular matrix (ECM) molecules including laminins, agrin and perlecan. Recent data indicate that DG function is required for the formation of basement membranes in early development and the organization of laminin on the cell surface. Here we show that DG-mediated laminin clustering on mouse embryonic stem (ES) cells is a dynamic process in which clusters are consolidated over time into increasingly more complex structures. Utilizing various null-mutant ES cell lines, we define roles for other molecules in this process. In (&bgr;)1 integrin-deficient ES cells, laminin-1 binds to the cell surface, but fails to organize into more morphologically complex structures. This result indicates that (&bgr;)1 integrin function is required after DG function in the cell surface-mediated laminin assembly process. In perlecan-deficient ES cells, the formation of complex laminin-1 structures is defective, implicating perlecan in the laminin matrix assembly process. Moreover, laminin and perlecan reciprocally modulate the organization of the other on the cell surface. Taken together, the data support a model whereby DG serves as a receptor essential for the initial binding of laminin on the cell surface, whereas (&bgr;)1 integrins and perlecan are required for laminin matrix assembly processes after it binds to the cell.
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