A tissue-specific atlas of mouse protein phosphorylation and expression.

A tissue-specific atlas of mouse protein phosphorylation and expression.
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DOI:
10.1016/j.cell.2010.12.001
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发表时间:
2010-12-23
期刊:
影响因子:
64.5
通讯作者:
Gygi SP
Gygi SP
中科院分区:
生物学1区
文献类型:
--
作者:
Huttlin EL;Jedrychowski MP;Elias JE;Goswami T;Rad R;Beausoleil SA;Villén J;Haas W;Sowa ME;Gygi SP

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虽然生物体中的大多数组织在遗传上是相同的,但每个组织的生物化学都被优化以实现其独特的生理作用,对人类健康和疾病产生重要影响。每个组织的独特生理学需要由专门的磷酸化依赖性细胞内信号协调的严格调控的基因和蛋白质表达。为了更好地了解磷酸化在维持组织间生理差异中的作用,我们对9种小鼠组织进行了蛋白质组学和磷酸化蛋白质组学表征。我们鉴定了12,039种蛋白质,其中包括6296种磷酸化蛋白,含有近36,000个磷酸化位点。比较蛋白质丰度和磷酸化水平揭示了每个组织内专门的、相互连接的磷酸化网络,同时表明许多蛋白质独立于其表达而受到磷酸化的调节。我们的数据表明,“典型的”磷蛋白广泛表达,但显示变量,往往组织特异性磷酸化,调整蛋白质活性的具体需要,每个组织。我们提供此数据集作为生物研究社区的在线资源。
Although most tissues in an organism are genetically identical, the biochemistry of each is optimized to fulfill its unique physiological roles, with important consequences for human health and disease. Each tissue’s unique physiology requires tightly regulated gene and protein expression coordinated by specialized, phosphorylation-dependent intracellular signaling. To better understand the role of phosphorylation in maintenance of physiological differences among tissues, we performed proteomic and phosphoproteomic characterizations of nine mouse tissues. We identified 12,039 proteins, including 6296 phosphoproteins harboring nearly 36,000 phosphorylation sites. Comparing protein abundances and phosphorylation levels revealed specialized, interconnected phosphorylation networks within each tissue while suggesting that many proteins are regulated by phosphorylation independently of their expression. Our data suggest that the ‘typical’ phosphoprotein is widely expressed, yet displays variable, often tissue-specific phosphorylation that tunes protein activity to the specific needs of each tissue. We offer this dataset as an online resource for the biological research community.
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