ArticleMethods in molecular biology (Clifton, N.J.)2021
Mapping Plant Phosphoproteome with Improved Tandem MOAC and Label-Free Quantification.
Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Protein phosphorylation represents a fundamental and evolutionarily conserved type of posttranslational modification that regulates protein functions and cellular signal transmission. Due to the dynamic nature of protein phosphorylation processes in plant cells, large-scale studies of phosphoproteins face several challenges such as low stoichiometry in the modified peptides in a proteome, as well as heterogeneity of the phosphopeptides of a given protein. Here we describe an updated tandem MOAC combined phosphoprotein and phosphopeptide enrichment strategy, a scalable phosphoproteomics approach that allows identification of thousands of phophopeptides in plant materials in one LC-MS analysis. We implemented modifications to several steps of the original tandem MOAC procedure to increase the identification and quantification of phosphopeptides in a sample beginning with less amount of tissue and a smaller amount of extracted protein.
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