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N ‐Glycosylation of the Drosophila neural protein Chaoptin is essential for its stability, cell surface transport and adhesive activity
Author(s) -
Hirai-Fujita Yu,
Yamamoto-Hino Miki,
Kanie Osamu,
Goto Satoshi
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.06.028
Subject(s) - glycosylation , n linked glycosylation , microbiology and biotechnology , function (biology) , mutation , biology , drosophila (subgenus) , glycoprotein , biochemistry , chemistry , gene , glycan
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 N ‐linked glycosylation of Chp is essential for its stability and activity.