Categorization of Phosphorylation Site Behavior during the Diauxic Shift in Saccharomyces cerevisiae.

ABSTRACT: Protein phosphorylation has long been recognized as an essential regulator of protein activity, structure, complex formation, and subcellular localization among other cellular mechanisms. However, interpretation of the changes in protein phosphorylation is difficult. To address this difficulty, we measured protein and phosphorylation site changes across 11 points of a time course and developed a method for categorizing phosphorylation site behavior relative to protein level changes using the diauxic shift in yeast as a model and TMT11 sample multiplexing. We classified quantified proteins into behavioral categories that reflected differences in kinase activity, protein complex structure, and growth and metabolic pathway regulation across different phases of the diauxic shift. These data al

SUBMITTER: Gassaway BM 

PROVIDER: S-EPMC8210948 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature