N-Glycosylation of the Drosophila neural protein Chaoptin is essential for its stability, cell surface transport and adhesive activity.
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.
Hirai-Fujita
Yu
Y
Mitsubishi-Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo, Japan.
Yamamoto-Hino
Miki
M
Kanie
Osamu
O
Goto
Satoshi
S
D000818:Animals; D002448:Cell Adhesion; D002462:Cell Membrane / Q000378:metabolism*; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009154:Mutation; D021381:Protein Transport
D029721:Drosophila Proteins; D008562:Membrane Glycoproteins; C055093:chp protein, Drosophila