A mutation in Asparagine-Linked Glycosylation 12 ( ALG12 ) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors

FEBS Letters

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