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dc.contributor.authorMatsuzaki, Tomoko
dc.contributor.authorKitayama, Hitoshi
dc.contributor.authorOmura, Akira
dc.contributor.authorNishimoto, Emi
dc.contributor.authorAlexander, David B.
dc.contributor.authorNoda, Makoto
dc.contributor.alternative松﨑, 朋子
dc.contributor.alternative北山, 仁志
dc.contributor.alternative野田, 亮
dc.date.accessioned2019-06-25T07:07:02Z-
dc.date.available2019-06-25T07:07:02Z-
dc.date.issued2018-10-04
dc.identifier.issn2046-6390
dc.identifier.urihttp://hdl.handle.net/2433/242230-
dc.description.abstractThe tumor suppressor protein RECK has been implicated in the regulation of matrix metalloproteinases (MMPs), NOTCH-signaling and WNT7-signaling. It remains unclear, however, how broad the spectrum of RECK targets extends. To find novel RECK binding partners, we took the unbiased approach of yeast two-hybrid screening. This approach detected ADAMTS10 as a RECK-interactor. ADAMTS10 has been characterized as a metalloproteinase involved in fibrillin-rich microfibril biogenesis, and its mutations have been implicated in the connective tissue disorder Weill-Marchesani syndrome. Experiments in vitro using recombinant proteins expressed in mammalian cells indicated that RECK indeed binds ADAMTS10 directly, that RECK protects ADAMTS10 from fragmentation following chemical activation and that ADAMTS10 interferes with the activity of RECK to inhibit MT1-MMP. In cultured cells, RECK increases the amount of ADAMTS10 associated with the cells. Hence, the present study has uncovered novel interactions between two molecules of known clinical importance, RECK and ADAMTS10.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherCompany of Biologists Ltd
dc.rights© 2018. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
dc.subjectRECK
dc.subjectADAMTS10
dc.subjectTumor suppressor
dc.subjectFibronectin
dc.subjectMT1-MMP
dc.subjectYeast two-hybrid assay
dc.titleThe RECK tumor-suppressor protein binds and stabilizes ADAMTS10
dc.type.niitypeJournal Article
dc.identifier.jtitleBiology Open
dc.identifier.volume7
dc.relation.doi10.1242/bio.033985
dc.textversionpublisher
dc.identifier.artnumbio033985
dc.addressDepartment of Molecular Oncology, Kyoto University Graduate School of Medicine
dc.addressDepartment of Molecular Oncology, Kyoto University Graduate School of Medicine
dc.addressDepartment of Molecular Oncology, Kyoto University Graduate School of Medicine
dc.addressDepartment of Molecular Oncology, Kyoto University Graduate School of Medicine
dc.addressDepartment of Molecular Toxicology, Nagoya City University
dc.addressDepartment of Molecular Oncology, Kyoto University Graduate School of Medicine
dc.identifier.pmid30287421
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