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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lokau, Juliane Garbers, Christoph Düsterhöft, Stefan Waetzig, Georg H. Scheller, Jürgen Lorenzen, Inken Höbel, Katharina Rose-john, Stefan Chalaris, Athena Oldefest, Mirja Grötzinger, Joachim |
| Description | Author Affiliation: Düsterhöft S ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Höbel K ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Oldefest M ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Lokau J ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Waetzig GH ( the CONARIS Research Institute AG, Schauenburgerstr. 116, 24118 Kiel, Germany, and.); Chalaris A ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Garbers C ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany, the Institute of Biochemistry and Molecular Biology II, Medical Faculty, Heinrich-Heine-University, Universitätsstr. 1, 40225 Düsseldorf, Germany.); Scheller J ( the Institute of Biochemistry and Molecular Biology II, Medical Faculty, Heinrich-Heine-University, Universitätsstr. 1, 40225 Düsseldorf, Germany.); Rose-John S ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Lorenzen I ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.); Grötzinger J ( From the Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany, jgroetzinger@biochem.uni-kiel.de.) |
| Abstract | A disintegrin and metalloprotease 17 (ADAM17) is a major sheddase involved in the regulation of a wide range of biological processes. Key substrates of ADAM17 are the IL-6 receptor (IL-6R) and TNF- . The extracellular region of ADAM17 consists of a prodomain, a catalytic domain, a disintegrin domain, and a membrane-proximal domain as well as a small stalk region. This study demonstrates that this juxtamembrane segment is highly conserved, -helical, and involved in IL-6R binding. This process is regulated by the structure of the preceding membrane-proximal domain, which acts as molecular switch of ADAM17 activity operated by a protein-disulfide isomerase. Hence, we have termed the conserved stalk region 'Conserved ADAM seventeen dynamic interaction sequence' (CANDIS). Finally, we identified the region in IL-6R that binds to CANDIS. In contrast to the type I transmembrane proteins, the IL-6R, and IL-1RII, CANDIS does not bind the type II transmembrane protein TNF- , demonstrating fundamental differences in the respective shedding by ADAM17. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 23 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-06-06 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | ADAM Proteins Metabolism Receptors, Interleukin-6 Chemistry Amino Acid Sequence Animals Binding Sites Circular Dichroism Conserved Sequence DNA Primers HEK293 Cells Molecular Sequence Data Polymerase Chain Reaction Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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