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Integrins are cell-surface adhesion molecules that link extracellular matrix components to the actin cytoskeleton and regulate numerous biologic processes such as spreading and migration. Lipid rafts, microdomains enriched in sphingolipids and cholesterol, are one class of cellular compartment responsible for the organization of protein-protein interactions, including integrin-mediated cell-cell adhesion. The lipid raft association of alpha 3 beta 1 and alpha 6 beta 1 integrins was investigated in a model system of chick embryo fibroblasts using detergent-resistant cell fractions. Like beta 1 integrins, alpha 3 and alpha 6 integrins partitioned preferentially into detergent-insoluble fractions, and most of the detergent-resistant alpha 3 beta 1 was lipid raft-associated. Both alpha 6 beta 1 and alpha 3 beta 1 are expressed as a heterodimer, and in initial attempts to evaluate protein-protein associations in this system, beta 1 integrins were not detected. However, anti-alpha 6 antibodies specifically cross-reacted with alpha 6 beta 1 in cytoskeletal fractions, suggesting that beta 1 integrins are localized within lipid rafts. These findings suggest that integrins are distributed into distinct populations of lipid rafts that may be associated with cytoskeletal components in the detergent-soluble and detergent-insoluble cell fractions.Apple’s online music store has seen an increase of more than 100,000 people signing up in just four months.
In April, Apple Music had 2.8 million paying subscribers, with 5.8 million total users
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