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T细胞抗原受体触发后脂筏蛋白质组广泛的时间调控性重组。

Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering.

作者信息

Bini Luca, Pacini Sonia, Liberatori Sabrina, Valensin Silvia, Pellegrini Michela, Raggiaschi Roberto, Pallini Vitaliano, Baldari Cosima T

机构信息

Department of Molecular Biology, University of Siena, Via Fiorentina 1, 53100 Siena, Italy.

出版信息

Biochem J. 2003 Jan 15;369(Pt 2):301-9. doi: 10.1042/BJ20020503.

DOI:10.1042/BJ20020503
PMID:12358599
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1223079/
Abstract

Signalling by immunoreceptors is orchestrated at specific plasma membrane microdomains, referred to as lipid rafts. Here we present a proteomics approach to the temporal analysis of protein association with lipid rafts following T-cell antigen receptor (TCR) triggering. We show that TCR engagement promotes the temporally regulated recruitment of proteins participating in the TCR signalling cascade to lipid rafts. Furthermore, TCR triggering results in profound modifications in the composition of lipid rafts involving a number of proteins associated either directly or indirectly with both plasma and intracellular membranes. Raft-associated proteins can be clustered according to their temporal profile of raft association. The data identify lipid rafts as highly dynamic structures and reveal a dramatic impact of surface TCR triggering not only on components of the TCR signalling machinery but also on proteins implicated in a number of diverse cellular processes.

摘要

免疫受体信号传导在特定的质膜微结构域(称为脂筏)中精心编排。在此,我们提出一种蛋白质组学方法,用于在T细胞抗原受体(TCR)触发后对与脂筏相关的蛋白质进行时间分析。我们表明,TCR的结合促进了参与TCR信号级联反应的蛋白质在时间上受到调控地募集到脂筏。此外,TCR触发导致脂筏组成发生深刻变化,涉及许多直接或间接与质膜和内膜相关的蛋白质。与脂筏相关的蛋白质可以根据它们与脂筏结合的时间特征进行聚类。这些数据将脂筏确定为高度动态的结构,并揭示了表面TCR触发不仅对TCR信号传导机制的成分有巨大影响,而且对涉及许多不同细胞过程的蛋白质也有巨大影响。

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TCR signal initiation machinery is pre-assembled and activated in a subset of membrane rafts.TCR信号起始机制在一部分膜筏中预先组装并被激活。
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