کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2828991 1162775 2009 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Roles for SH2 and SH3 domains in Lyn kinase association with activated FcεRI in RBL mast cells revealed by patterned surface analysis
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
Roles for SH2 and SH3 domains in Lyn kinase association with activated FcεRI in RBL mast cells revealed by patterned surface analysis
چکیده انگلیسی

In mast cells, antigen-mediated cross-linking of IgE bound to its high-affinity surface receptor, FcεRI, initiates a signaling cascade that culminates in degranulation and release of allergic mediators. Antigen-patterned surfaces, in which the antigen is deposited in micron-sized features on a silicon substrate, were used to examine the spatial relationship between clustered IgE–FcεRI complexes and Lyn, the signal-initiating tyrosine kinase. RBL mast cells expressing wild-type Lyn-EGFP showed co-redistribution of this protein with clustered IgE receptors on antigen-patterned surfaces, whereas Lyn-EGFP containing an inhibitory point mutation in its SH2 domain did not significantly accumulate with the patterned antigen, and Lyn-EGFP with an inhibitory point mutation in its SH3 domain exhibited reduced interactions. Our results using antigen-patterned surfaces and quantitative cross-correlation image analysis reveal that both the SH2 and SH3 domains contribute to interactions between Lyn kinase and cross-linked IgE receptors in stimulated mast cells.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 168, Issue 1, October 2009, Pages 161–167
نویسندگان
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