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. 1999 May 3;145(3):619–631. doi: 10.1083/jcb.145.3.619

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Laminin polymerization induces a selective reorganization of cell surface receptors and components of the cortical cytoskeleton. Myotubes were incubated with 10 μg/ml laminin-1 for 4 h, followed by double indirect immunofluorescence to visualize sets of bound laminin and various sarcolemmal proteins: Lm, laminin; α7, α7 integrin subunit; β1, β1 integrin subunit; DG, dystroglycan; vinc, vinculin; DN, dystrophin; α-act, α-actinin. Merged images of paired sets are shown to the far left in yellow. Sarcolemmal proteins in myotubes treated with BSA or with nonpolymerizing (AEBSF-treated) laminin are shown in the bottom two rows of images. In the presence of laminin that can polymerize, receptors and cytoskeletal proteins reorganize into a similar polygonal pattern, colocalizing with each other and with laminin. Bar, 5 μm; insets are twice the magnification.