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首页> 外文期刊>Biochemistry >Extracellular Juxtamembrane Segment of ADAM17 Interacts with Membranes and Is Essential for Its Shedding Activity
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Extracellular Juxtamembrane Segment of ADAM17 Interacts with Membranes and Is Essential for Its Shedding Activity

机译：ADAM17的细胞外近膜节段与膜相互作用，并且是其脱落活性所必需的

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摘要

A wide variety of biological processes including differentiation, regeneration, and cancer progression are regulated by shedding of membrane-anchored proteins. One of the major sheddases is A Disintegrin And Metalloprotease-17 (ADAM17) whose extracellular region consists of a pro-, a catalytic, a disintegrin-, and a membrane-proximal domain (MPD) as well as a short juxtamembrane segment of 17 amino acid residues that has been named "Conserved ADAM-seventeeN Dynamic Interaction Sequence" (CANDIS). This segment is involved in substrate recognition. Key mediators of inflammation including interleukin-6 receptor (IL-6R) and tumor necrosis factor (TNF-alpha) are substrates of ADAM17. The shedding activity of ADAM17 is regulated by the conformation of the membrane-proximal domain preceding the CANDIS segment. Here, we show that CANDIS, besides being involved in substrate recognition, is able to interact with lipid bilayers in vitro and that this property could be involved in regulating ADAM17 shedding activity.
机译：各种各样的生物学过程，包括分化，再生和癌症进展，都通过膜锚定蛋白的脱落来调节。主要的棚底酶之一是Disintegrin and Metalloprotease-17（ADAM17），其胞外区域由一个前，催化，一个整合素和一个膜近端结构域（MPD）以及一个短的近17个氨基酸的近膜片段组成酸残基，已被命名为“保守的ADAM-seventeeN动态相互作用序列”（CANDIS）。该部分涉及底物识别。炎症的主要介质包括白介素6受体（IL-6R）和肿瘤坏死因子（TNF-α）是ADAM17的底物。 ADAM17的脱落活性受CANDIS片段之前的近膜结构域构象的调节。在这里，我们表明，CANDIS除参与底物识别外，还能够在体外与脂质双层相互作用，并且该特性可能与调节ADAM17脱落活性有关。

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