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

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 also provide a valuable resource
for the study of fermentative versus respiratory growth and set a
new benchmark for temporal quantitative proteomics and phosphoproteomics
for the diauxic shift in Saccharomyces cerevisiae. Data are available via ProteomeXchange with identifier PXD022741.