期刊
NATURE IMMUNOLOGY
卷 18, 期 1, 页码 86-95出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ni.3631
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资金
- Nomis Foundation
- Waitt Foundation
- James B. Pendleton Charitable Trust
- US National Institutes of Health [1DP2GM105455-01, T32 CA009370]
- Salk Institute Cancer Center core facilities (National Cancer Institute) [CA014195]
- Mass Spectrometry Core of the Salk Institute (National Cancer Institute Cancer Center Support Grants of the US National Institutes of Health) [P30 014195]
- Helmsley Center for Genomic Medicine
Cell-surface-receptor pathways amplify weak, rare and local stimuli to induce cellular responses. This task is accomplished despite signaling components that segregate into nanometer-scale membrane domains. Here we describe a 'catch-and-release' mechanism that amplified and dispersed stimuli by releasing activated kinases from receptors lacking intrinsic catalytic activity. Specifically, we discovered a cycle of recruitment, activation and release for Zap70 kinases at phosphorylated T cell antigen receptors (TCRs). This turned the TCR into a 'catalytic unit' that amplified antigenic stimuli. Zap70 released from the TCR remained at the membrane, translocated, and phosphorylated spatially distinct substrates. The mechanisms described here are based on widely used protein domains and post-translational modifications; therefore, many membrane-associated pathways might employ similar mechanisms for signal amplification and dispersion.
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