FEBS Letters | |
A mutation in Asparagine-Linked Glycosylation 12 ( ALG12 ) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors | |
article | |
Fabian Trempel1  Lennart Eschen-Lippold1  Nicole Bauer1  Stefanie Ranf1  Lore Westphal1  Dierk Scheel1  Justin Lee1  | |
[1] Leibniz Institute of Plant Biochemistry | |
关键词: asparagine-linked glycosylation; calcium; membrane receptors; signalling; | |
DOI : 10.1002/1873-3468.13850 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 resequencing revealed a mutation in asparagine-linked glycosylation 12 that encodes the mannosyltransferase responsible for adding the eighth mannose residue in an a-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.
【 授权许可】
Unknown
【 预 览 】
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RO202105310000489ZK.pdf | 1599KB | download |