AI Article Synopsis
- Glycosylation of proteins, like in the case of the Drosophila protein Chaoptin (Chp), plays a crucial role in various biological systems and is important for photoreceptor cell development.
- Mutations in one-third of the potential N-linked glycosylation sites on Chp impaired its ability to adhere to cells when tested in a lab setting.
- Additionally, altering two-thirds of these glycosylation sites significantly reduced the levels of Chp protein, highlighting the importance of N-linked glycosylation for both the stability and function of Chp.
Article Abstract
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.
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