2022
DOI: 10.1038/s41589-022-01062-y
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Systematic discovery of biomolecular condensate-specific protein phosphorylation

Abstract: 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 interactions. W… Show more

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Cited by 62 publications
(44 citation statements)
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“…The localization of pyrophosphoproteins to the nucleolus was quite striking and raises the question whether pyrophosphorylation plays a general regulatory role in this biomolecular condensate. A recent study showed that phosphorylation of specific sites influenced partitioning of NPM1 (pSer125) and HNRNPA1 (Heterogeneous nuclear ribonucleoprotein A1, pSer6) to the nucleolus 64 . Interestingly, in our MS data both proteins were found to be pyrophosphorylated at these specific positions.…”
Section: Discussionmentioning
confidence: 99%
“…The localization of pyrophosphoproteins to the nucleolus was quite striking and raises the question whether pyrophosphorylation plays a general regulatory role in this biomolecular condensate. A recent study showed that phosphorylation of specific sites influenced partitioning of NPM1 (pSer125) and HNRNPA1 (Heterogeneous nuclear ribonucleoprotein A1, pSer6) to the nucleolus 64 . Interestingly, in our MS data both proteins were found to be pyrophosphorylated at these specific positions.…”
Section: Discussionmentioning
confidence: 99%
“…Temperature variation can result in markedly different PTM patterns shaped by temperature-sensitive PTM enzymes (Cai et al, 2018), including kinases (Haltenhof et al, 2020) and arginine methyltransferases (Hong et al, 2010). In fact, in vitro and in vivo evidence supports temperaturedependent changes in RNA-RBP condensation (Iserman et al, 2020;Molliex et al, 2015;Pullara et al, 2022;Riback et al, 2017) as a result of differential intermolecular interactions (Tauber et al, 2020), possibly linked to distinct PTM of the embedded RBPs (Hofweber and Dormann, 2019;Sridharan et al, 2022).…”
Section: Discussionmentioning
confidence: 99%
“…These regulatory factors could modulate the conformational space of one or more molecular community members, fine-tuning or dramatically changing the critical concentration for condensation. A recent proteomic study showed that phosphorylation is a major regulator of protein association with condensates ( Sridharan et al, 2022 ). Notably, one can intervene with indirect c-mods at multiple steps within a signaling cascade.…”
Section: C-mod Design Principlesmentioning
confidence: 99%