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Systematic investigation of protein phosphorylation in biomolecular condensates

ABSTRACT: We have adapted a recently developed quantitative proteomics based approach to measure protein solubility following a lysate centrifugation assay to determine the proportion of a protein in distinct subpopulations in a proteome-wide manner (Sridharan et al., 2019). Further, by combining the solubility measurements with phosphoproteomics (Potel et al., 2021), we have quantitatively mapped phosphorylation sites enriched in the different protein subpopulations.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sindhuja Sridharan

LAB HEAD: Mikhail M. Savitski

PROVIDER: PXD027769 | Pride | 2022-08-09

REPOSITORIES: Pride

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Systematic discovery of biomolecular condensate-specific protein phosphorylation.

Sridharan Sindhuja S Hernandez-Armendariz Alberto A Kurzawa Nils N Potel Clement M CM Memon Danish D Beltrao Pedro P Bantscheff Marcus M Huber Wolfgang W Cuylen-Haering Sara S Savitski Mikhail M MM

Nature chemical biology 20220721 10

Reversible protein phosphorylation is an important mechanism for regulating (dis)assembly of biomolecular condensates. However, condensate-specific phosphosites remain largely unknown, thereby limiting our understanding of the underlying mechanisms. Here, we combine solubility proteome profiling with phosphoproteomics to quantitatively map several hundred phosphosites enriched in either soluble or condensate-bound protein subpopulations, including a subset of phosphosites modulating protein-RNA ...[more]

PMID: 35864335

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