期刊
JOURNAL OF IMMUNOLOGY
卷 180, 期 10, 页码 6518-6526出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.180.10.6518
关键词
-
类别
资金
- NHLBI NIH HHS [HL 069507, R01 HL069507] Funding Source: Medline
- NIAID NIH HHS [R01 AI067544-02, AI 50831, R56 AI067544, R01 AI050831, AI 67544, P01 AI 054456, T32 AI 60573, P01 AI054456, T32 AI060573, R01 AI067544] Funding Source: Medline
Ligation of the transmembrane protein T cell Ig and mucin domain (Tim)-1 can costimulate T cell activation. Agonistic Abs to Tim-1 are also capable of inducing T cell activation without additional stimuli. However, little is known about the biochemical mechanisms underlying T cell stimulation or costimulation through Tim-1. We show that a tyrosine in Tim-1 becomes phosphorylated in a lck-dependent manner, whereupon it can directly recruit p85 adaptor subunits of PI3K. This results in PI3K activation, which is required for Tim-1 function. We also provide genetic evidence that p85 expression is required for optimal Tim-1 function. Thus, we describe a pathway from Tim-1 tyrosine phosphorylation to the PI3K signaling pathway, which appears to be a major effector of Tim-1-mediated T cell activation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据