Identification of Fyn-binding proteins in MC/9 mast cells using mass spectrometry.
Identification of Fyn-binding proteins in MC/9 mast cells using mass spectrometry.
复制标题
使用质谱法鉴定 MC/9 肥大细胞中的 Fyn 结合蛋白。
DOI：
10.1016/j.bbrc.2003.08.132
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发表时间：
2003
影响因子：
3.1
通讯作者：
Metcalfe,DeanD
中科院分区：
文献类型：
--
作者：
Nahm,Dong-Ho;Tkaczyk,Christine;Fukuishi,Nobuyuki;Colucci-Guyon,Emma;Gilfillan,AlasdairM;Metcalfe,DeanD
Fyn is a Src kinase known to have an essential role in mast cell degranulation induced following aggregation of the high affinity IgE-receptor. Although Fyn possesses SH2 and SH3 protein binding domains, the molecules that interact with Fyn have not been characterized in mast cells. We thus analyzed Fyn-binding proteins in MC/9 mast cells to explore the Fyn-mediated signaling pathway. On mass spectrometric analysis of proteins binding to the SH2 and SH3 domains of Fyn, we identified six proteins that bind to Fyn including vimentin, pyruvate kinase, p62 ras-GAP associated phosphoprotein, SLP-76, HS-1, and FYB. Among these proteins, vimentin and pyruvate kinase have not been shown to bind to Fyn. After IgE-receptor mediated stimulation, binding of vimentin to Fyn was increased; and this interaction was via binding to the SH2, but not the SH3, domain of Fyn. Mast cells from vimentin-deficient mice showed enhanced mediator release and tyrosine phosphorylation of intracellular proteins including NTAL and LAT. The observation that vimentin and pyruvate kinase bind to Fyn provides additional insight into Fyn-mediated signaling pathways, and suggests a critical role for Fyn in mast cell degranulation in interacting with both cytosolic and structural proteins.
