NDLI: MDA-9/syntenin interacts with ubiquitin via a novel ubiquitin-binding motif

Content Provider	Springer Nature Link
Author	Okumura, Fumihiko Yoshida, Koichi Liang, Fei Hatakeyama, Shigetsugu
Copyright Year	2011
Abstract	Ubiquitination appears to be involved in proteasome-dependent proteolysis and in the membrane trafficking system including endocytosis and exocytosis. In this study, we identified MDA-9/syntenin as a novel ubiquitin-binding protein by a yeast two-hybrid system using modified ubiquitin in which lysine 48 is substituted by arginine. It has been reported that MDA-9/syntenin is a membrane-associated protein and regulates a cellular process involving endocytosis and intracellular transport. We found that MDA-9/syntenin binds to ubiquitin by a non-covalent bond and is ubiquitinated covalently. MDA-9/syntenin has no ubiquitin-binding motifs that have so far been reported, suggesting that MDA-9/syntenin physically interacts with ubiquitin via a novel binding motif. MDA-9/syntenin is stable in the cell, suggesting that ubiquitin binding of MDA-9/syntenin or ubiquitination of MDA-9/syntenin is not related to proteolysis. Furthermore, we showed that overexpression of wild-type MDA-9/syntenin enhances formation of filopodia, whereas MDA-9/syntenin lacking the PDZ domain inhibits the formation of filopodia, suggesting that MDA-9/syntenin plays an important role via interaction with ubiquitin in the regulation of cancer metastasis and invasion.
Starting Page	163
Ending Page	172
Page Count	10
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	352
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Springer US
Publisher Date	2011-02-27
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Ubiquitin MDA-9/syntenin PDZ Membrane trafficking Proteolysis Oncology Cardiology Medical Biochemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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