Changes in cellular calcium levels are one of the earliest signalling events in plants exposed to pathogens or other exogenous factors. In a genetic screen, we identified an Arabidopsis thaliana 'changed calcium elevation 1' (cce1) mutant with attenuated calcium response to the bacterial flagellin flg22 peptide and several other elicitors. Whole genome re-sequencing revealed a mutation in ALG12 (Asparagine-Linked Glycosylation 12) that encodes the mannosyltransferase responsible for adding the eighth mannose residue in an α-1,6 linkage to the dolichol-PP-oligosaccharide N-glycosylation glycan tree precursors. While properly targeted to the plasma membrane, misglycosylation of several receptors in the cce1 background suggests that N-glycosylation is required for proper functioning of client proteins.

中文翻译：

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天冬酰胺连接糖基化 12 (ALG12) 的突变导致受体错误糖基化并减弱对多种微生物激发子的反应

细胞钙水平的变化是暴露于病原体或其他外源因素的植物中最早的信号事件之一。在遗传筛选中，我们鉴定了一种拟南芥'改变钙升高 1' (cce1) 突变体，其对细菌鞭毛蛋白 flg22 肽和其他几种诱导物的钙反应减弱。全基因组重测序揭示 ALG12（天冬酰胺连接糖基化 12）中的突变，该突变编码甘露糖基转移酶，负责将 α-1,6 连接中的第八个甘露糖残基添加到长醇-PP-寡糖 N-糖基化聚糖树前体。虽然正确靶向质膜，但 cce1 背景中几种受体的错误糖基化表明 N-糖基化是客户蛋白质正常运作所必需的。