The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II

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• 作者：Inken Lorenzen^a ; Juliane Lokau^a ; Stefan Dü ; sterhö ; ft^a ; Ahmad Trad^a ; Christoph Garbers^b ; Jü ; rgen Scheller^b ; Stefan Rose-John^a ; Joachim Grö ; tzinger^a ; ^{jgroetzinger@biochem.uni-kiel.de}
• 关键词：ADAM17 ; A Disintegrin And Metalloprotease 17 ; TNF-伪 ; Tumor Necrosis Factor-伪 ; IL-6R ; interleukin-6 receptor ; IL-1RII ; interleukin-1 receptor type II ; EGF ; Epidermal Growth Factor ; MPD ; membrane-proximal domain ; PMA ; phorbol 12-myristate 13-acetate ; GPI
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：24 April, 2012
• 卷：586
• 期：8
• 页码：1093-1100
• 文件大小：943 K

摘要

A great number of physiological processes are regulated by the release of ectodomains of membrane proteins. A Disintegrin And Metalloprotease 17 (ADAM17) is one of the important enzymes, which mediate this process called shedding. Today, more than 70 substrates of this transmembrane metalloprotease are known. This broad spectrum raises the question how ADAM17 recognizes its substrates specifically. Differently tagged ADAM17 deletion variants were used to demonstrate that exclusively the extracellular domains of ADAM17 are needed for interaction with two of its substrates, the IL-6R and the IL-1RII; whereas the transmembrane- and cytoplasmic-region are dispensable for this process. In the extracellular part solely the membrane-proximal domain of ADAM17 is mandatory for recognition of the two type-I transmembrane proteins, but not for the interaction with the type-II transmembrane molecule TNF-伪.

Structured summary of protein interactions

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