Mutations in Four Glycosyl Hydrolases Reveal a Highly Coordinated Pathway for Rhodopsin Biosynthesis and N-Glycan Trimming in

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As newly synthesized glycoproteins move through the secretory pathway, the asparagine-linked glycan (N-glycan) undergoes extensive modifications involving the sequential removal and addition of sugar residues. These modifications are critical for the proper assembly, quality control and transport of glycoproteins during biosynthesis. The importance of N-glycosylation is illustrated by a growing list of diseases that result from defects in the biosynthesis and processing of N-linked glycans. The major rhodopsin in the Drosophila (fruit fly) eye, Rh1, is highly unique among glycoproteins, as the N-glycan appears to be completely removed during Rh1 biosynthesis and maturation. However, much of the deglycosylation pathway for Rh1 remains unknown. To elucidate the key steps in Rh1 deglycosylation, we conducted a genetic dissection of glycoprotein processing in vivo. We have demonstrated that four glycosyl hydrolases play essential and unique roles in a highly coordinated pathway for N-glycan trimming during Rh1 biosynthesis. Our results reveal novel insights into the functions of glycosyl hydrolases in the secretory pathway and provide fundamental advances towards understanding N-glycosylation in vivo.

Vyšlo v časopise: Mutations in Four Glycosyl Hydrolases Reveal a Highly Coordinated Pathway for Rhodopsin Biosynthesis and N-Glycan Trimming in. PLoS Genet 10(5): e32767. doi:10.1371/journal.pgen.1004349
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004349

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