N-glycosylation of the Drosophila neural protein Chaoptin is essential for its stability, cell surface transport and adhesive activity
N-glycosylation of the Drosophila neural protein Chaoptin is essential for its stability, cell surface transport and adhesive activity
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DOI：
10.1016/j.febslet.2008.06.028
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发表时间：
2008-07-23
期刊：
影响因子：
3.5
通讯作者：
Goto, Satoshi
中科院分区：
文献类型：
--
作者：
Hirai-Fujita, Yu;Yamamoto-Hino, Miki;Goto, Satoshi
蛋白质的糖基化可以调节其在多种系统中的功能，包括免疫应答、神经元活动和发育。果蝇蛋白质Chaoptin（Chp）对于感光细胞的发育和维持是必不可少的。这种蛋白质是高度糖基化的，但这种糖基化的可能作用还不清楚。在这里，我们表明，突变引入约1/ 3的16个潜在的N-连接的糖基化位点内Chp的细胞粘附活性受损时，表达在果蝇S2细胞。2/ 3的糖基化位点的突变导致Chp蛋白丰度的显著降低。这些结果表明Chp的N连接糖基化对其稳定性和活性至关重要。(c)2008年欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
Glycosylation of proteins can modulate their function in a striking variety of systems, including immune responses, neuronal activities and development. The Drosophila protein, Chaoptin ( Chp), is essential for the development and maintenance of photoreceptor cells. This protein is heavily glycosylated, but the possible role of this glycosylation is not well- understood. Here we show that mutations introduced into about 1/ 3 of 16 potential N- linked glycosylation sites within Chp impaired its cell adhesive activities when expressed in Drosophila S2 cells. Mutation of 2/ 3 of the glycosylation sites resulted in a marked decrease in Chp protein abundance. These results suggest that Nlinked glycosylation of Chp is essential for its stability and activity. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.