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The RECK tumor-suppressor protein binds and stabilizes ADAMTS10
Tomoko Matsuzaki1, Hitoshi Kitayama1, Akira Omura1
1Department of Molecular Oncology, Kyoto University Graduate School of Medicine, Yoshida-Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Biology Open
|October 6, 2018
Summary
This study identifies a new interaction between the tumor suppressor RECK and ADAMTS10, a metalloproteinase linked to connective tissue disorders. RECK directly binds ADAMTS10, influencing its stability and activity, and affecting cellular association.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- The tumor suppressor RECK regulates matrix metalloproteinases (MMPs) and signaling pathways like NOTCH and WNT7.
- The full range of RECK's molecular targets and functions remains incompletely understood.
Purpose of the Study:
- To identify novel binding partners of RECK using an unbiased screening approach.
- To characterize the functional interaction between RECK and its newly identified partner, ADAMTS10.
Main Methods:
- Yeast two-hybrid screening was employed to detect RECK-interacting proteins.
- In vitro experiments using recombinant proteins assessed direct binding and functional interplay.
- Cell-based assays were utilized to investigate RECK's effect on ADAMTS10 localization.
Main Results:
- Yeast two-hybrid screening identified ADAMTS10 as a RECK-binding protein.
- In vitro studies confirmed direct binding of RECK to ADAMTS10, with RECK protecting ADAMTS10 from fragmentation.
- ADAMTS10 was found to interfere with RECK's inhibition of MT1-MMP activity, and RECK enhanced cell-associated ADAMTS10 levels.
Conclusions:
- This study reveals a novel interaction between RECK and ADAMTS10, two proteins with established clinical relevance.
- The findings elucidate a new layer of regulation involving RECK and ADAMTS10, impacting metalloproteinase activity and cellular processes.
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