A mutation in Asparagine‐Linked Glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors. Issue 15 (15th June 2020)

• Record Type: Journal Article
• Authors: Trempel, Fabian; Eschen‐Lippold, Lennart; Bauer, Nicole; Ranf, Stefanie; Westphal, Lore; Scheel, Dierk; Lee, Justin
• Is Part Of: FEBS letters. Volume 594:Issue 15(2020)
• Page Start: 2440
• Page End: 2451
• Publication Date: 2020-06-15
• Subjects: asparagine‐linked glycosylation -- calcium -- membrane receptors -- signalling; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13850
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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 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. Abstract :