Analysis for Protein Glycosylation of Pattern Recognition Receptors in Plants.
Recognition of molecules typical of microbes or aberrant cellular states, termed microbe- or danger-associated molecular patterns (MAMPs/DAMPs), respectively, provides an important step in plant and animal innate immunity. In plants, pattern recognition receptors (PRRs) identified to date are limited to membrane-associated proteins, of which the majority has an extracellular leucine-rich repeat (LRR) or lysine-motif (LysM) domain. These PRRs undergo quality control (QC) in the Endoplasmic Reticulum (ER) that is dependent on Asn (N)-linked glycosylation (Glc3Man9GlcNAc2 conjugation) of their extracellular domain. In Arabidopsis, genetic studies have revealed that a subset of these PRRs require an intact N-glycosylation pathway in the ER for their biogenesis and function. Here, we describe methods for immunoblot-based detection of protein glycosylation states in plants.
['Inokuchi|Takaakira|T|', 'Saijo|Yusuke|Y|']
D017360:Arabidopsis D029681:Arabidopsis Proteins D002462:Cell Membrane D004721:Endoplasmic Reticulum D006031:Glycosylation D015151:Immunoblotting D000072417:Protein Domains D051192:Receptors, Pattern Recognition
Pattern recognition receptors (PRRs) Endoplasmic Reticulum quality control (ERQC) Glycosidase treatment Immunoblot analysis N-linked glycosylation Plant immunity