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Towards a systematic map of the functional role of protein phosphorylation

Vieitez, C.; Busby, B. P.; Ochoa, D.; Mateus, A.; Galardini, M.; Jawed, A.; Memon, D.; Potel, C. M.; Vonesch, S. C.; Szu Tu, C.; Shahraz, M.; Stein, F.; Steinmetz, L. M.; Savitski, M. M.; Typas, A.; Beltrao, P.

2019-12-11 systems biology
10.1101/872770 bioRxiv
Show abstract

Phosphorylation is a critical post-translational modification involved in the regulation of almost all cellular processes. However, less than 5% of thousands of recently discovered phosphorylation sites have a known function. Here, we devised a chemical genetic approach to study the functional relevance of phosphorylation in S. cerevisiae. We generated 474 phospho-deficient mutants that, along with the gene deletion library, were screened for fitness in 102 conditions. Of these, 42% exhibited growth phenotypes, suggesting these phosphosites are likely functional. We inferred their function based on the similarity of their growth profiles with that of gene deletions, and validated a subset by thermal proteome profiling and lipidomics. While some phosphomutants showed loss-of-function phenotypes, a higher fraction exhibited phenotypes not seen in the corresponding gene deletion suggestive of a gain-of-function effect. For phosphosites conserved in humans, the severity of the yeast phenotypes is indicative of their human functional relevance. This study provides a roadmap for functionally characterizing phosphorylation in a systematic manner.

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