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Publication : Biosynthesis and secretion of mouse cysteine-rich with EGF-like domains 2.

First Author  Oh-hashi K Year  2011
Journal  FEBS Lett Volume  585
Issue  15 Pages  2481-7
PubMed ID  21729698 Mgi Jnum  J:176035
Mgi Id  MGI:5288159 Doi  10.1016/j.febslet.2011.06.029
Citation  Oh-hashi K, et al. (2011) Biosynthesis and secretion of mouse cysteine-rich with EGF-like domains 2. FEBS Lett 585(15):2481-7
abstractText  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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