© The Rockefeller University Press,
0021-9525/1999//877 $5.00
The Journal of Cell Biology, Volume 145, Number 4,
, 1999 877-887
Critical Role for Cholesterol in Lyn-mediated Tyrosine Phosphorylation of Fc
RI and Their Association with Detergent-resistant Membranes
Erin D. Sheets,
David Holowka, and
Barbara Baird
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301
Tyrosine phosphorylation of the high affinity immunoglobulin (Ig)E receptor (Fc
RI) by the Src family kinase Lyn is the first known biochemical step that occurs during activation of mast cells and basophils after cross-linking of Fc
RI by antigen. The hypothesis that specialized regions in the plasma membrane, enriched in sphingolipids and cholesterol, facilitate the coupling of Lyn and Fc
RI was tested by investigating functional and structural effects of cholesterol depletion on Lyn/Fc
RI interactions. We find that cholesterol depletion with methyl-β-cyclodextrin substantially reduces stimulated tyrosine phosphorylation of Fc
RI and other proteins while enhancing more downstream events that lead to stimulated exocytosis. In parallel to its inhibition of tyrosine phosphorylation, cholesterol depletion disrupts the interactions of aggregated Fc
RI and Lyn on intact cells and also disrupts those interactions with detergent-resistant membranes that are isolated by sucrose gradient ultracentrifugation of lysed cells. Importantly, cholesterol repletion restores receptor phosphorylation together with the structural interactions. These results provide strong evidence that membrane structure, maintained by cholesterol, plays a critical role in the initiation of Fc
RI signaling.
Key Words: methyl-β-cyclodextrin immunoglobulin E receptor plasma membrane structure lipid domains signal transduction
Abbreviations used in this paper: BSA/BSS, BSA-containing buffered saline solution; DRM, detergent-resistant membrane; GPI, glycosylphosphatidylinositol; HRP, horseradish peroxidase; Lo, liquid-ordered; MβCD, methyl-β-cyclodextrin; TfR, transferrin receptor; TX-100, Triton X-100.
Address correspondence to Barbara Baird or David Holowka, Department of Chemistry & Chemical Biology, Baker Laboratory, Cornell University, Ithaca, NY 14853-1301. Tel.: (607) 255-4095 or (607) 255-6140. Fax: (607) 255-4137. E-mail: bab13{at}cornell.edu or dah24{at}cornell.edu

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