Work

Quantitative glycoproteomics identifies target N-glycoproteins of the Golgi-class I α-mannosidase SlMNSI1 that is important for tomato fruit development

Year: 2025

Type: article

Abstract: , respectively, on glycoprotein substrates. Analysis of the tomato fruit site-specific N-glycoproteome identified 3091 intact N-glycopeptides containing 873 N-glycosites and 158 N-glycans within 573 N-glycoproteins. Among these, 97 N-glycoproteins containing 127 N-glycosites were identified as candidate targets of SlMNSI1. Strikingly, SlMNSI1 itself is N-glycosylated at Asn288 and Asn334, and N-glycosylation is essential for Golgi localization and protein stability. Genetic complementation assays verified this in vivo: overexpression of wild-type SlMNSI1 fully restored normal fruit development in the mutant, whereas overexpression of a non-glycosylatable SlMNSI1 variant only partially complemented these phenotypes. Collectively, our findings reveal the critical role of SlMNSI1 and mannosidic N-glycans in fruit development.

Source: Plant Communications

DOI: 10.1016/j.xplc.2025.101537