Glycosylation is essential for all trees of life. N-glycosylation is one of the most common covalent protein modifications and influences a large variety of cellular processes including protein folding, quality control and protein-receptor interactions. Despite recent progress in understanding of N-glycan biosynthesis, our knowledge of N-glycan function on individual plant proteins is still very limited. In this respect, plant hormone receptors are an interesting group of proteins as several of these proteins are present at distinct sites in the secretory pathway or at the plasma membrane and have numerous potential N-glycosylation sites. Identifying and characterization of N-glycan structures on these proteins is essential to investigate the functional role of this abundant protein modification. Here, a straightforward immunoblot-based approach is presented that enables the analysis of N-glycosylation on endogenous hormone receptors like the brassinosteroid receptor BRI1.
Keywords: Brassinosteroid receptor; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; N-glycosylation; Secretory pathway.