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泛素化在决定非Smad信号转导反应中的作用。

The Role of Ubiquitination to Determine Non-Smad Signaling Responses.

作者信息

Gudey Shyam Kumar, Landström Marene

机构信息

Department of Medical Biosciences, Umeå University, Pathology Building 6M, 2nd Floor, Umeå, 901 85, Sweden.

出版信息

Methods Mol Biol. 2016;1344:355-63. doi: 10.1007/978-1-4939-2966-5_23.

Abstract

Ubiquitination is a posttranslational modification of proteins which acts as a key regulator of their function as well as fate. We have recently reported transforming growth factor β (TGFβ)-induced activation of non-Smad signaling responses through a specific Lys63-linked polyubiquitination of TGFβ type I receptor and TGFβ-associated kinase 1 (TAK1) that are utilized to specify cellular responses in cancer cells. This chapter gives a brief introduction of the biological importance of ubiquitination of proteins, the methods we have used for detecting new partners in the TGFβ signaling pathway and for performing ubiquitination assays.

摘要

泛素化是蛋白质的一种翻译后修饰,它是蛋白质功能及其命运的关键调节因子。我们最近报道,转化生长因子β(TGFβ)通过TGFβ I型受体和TGFβ相关激酶1(TAK1)的特定赖氨酸63连接的多聚泛素化诱导非Smad信号反应的激活,这些反应被用于确定癌细胞中的细胞反应。本章简要介绍了蛋白质泛素化的生物学重要性,以及我们用于检测TGFβ信号通路中新伙伴和进行泛素化测定的方法。

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