Gamma-chain dependent recruitment of tyrosine kinases to membrane rafts by the human IgA receptor Fc alpha R

Abstract

We show that the human IgA receptor, Fc alpha R, redistributes to plasma membrane rafts after cross-linking and that tyrosine kinases are relocated to these sites following Fc alpha R capping. We demonstrate by confocal microscopy that Fc alpha R caps in membrane rafts by a gamma-chain-independent mechanism but that gamma-chain expression is necessary for Lyn redistribution. Immunoblotting of rafts isolated by sucrose density gradient centrifugation demonstrated recruitment of gamma-chain and phosphorylated tyrosine kinases Lyn and Bruton's tyrosine kinase to membrane rafts after Fc alpha R cross-linking. Time-dependent differences in Lyn phosphorylation and Bruton's tyrosine kinase distribution were observed between cells expressing Fc alpha R plus gamma-chain and cells expressing Fc alpha R only. This study defines early Fc alpha R-triggered membrane dynamics that take place before Fc alpha R internalization.