Biosynthesis and secretion of mouse cysteine-rich with EGF-like domains 2 |
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Authors: | Oh-hashi Kentaro Kunieda Ryosuke Hirata Yoko Kiuchi Kazutoshi |
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Affiliation: | Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu, Japan. oohashi@gifu-u.ac.jp |
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Abstract: | In this study, we found that Cysteine-rich with EGF-like domains 2 (CRELD2), a novel endoplasmic reticulum stress-inducible protein, is not only localized in the ER-Golgi apparatus but also spontaneously secreted. Deletion of four C-terminal amino acids from mouse CRELD2 or addition of tag-peptides to its C-terminus dramatically enhanced CRELD2 secretion. Intra- and extra-cellular CRELD2 is differentially glycosylated and its spontaneous secretion was significantly prevented by overexpression of a dominant negative mutant Sar1 and treatment with brefeldin A. Overexpression of wild-type GRP78 remarkably enhanced the secretion of wild-type but not mutant CRELD2. Our results demonstrate both that CRELD2 is a novel secretory glycoprotein regulated by Sar1 and GRP78 and that the C-terminal of CRELD2 plays a crucial role in its secretion. |
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