Simulating Mono-and Multi-Protein Phosphorylation within Nanoclusters
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arXiv
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| Format: | Preprint |
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2025
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| _version_ | 1866912704684359680 |
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| author | Destaing, Olivier Fourcade, Bertrand |
| author_facet | Destaing, Olivier Fourcade, Bertrand |
| contents | Protein nanoclustering is a characteristic feature of their activated state and is essential for forming numerous subcellular structures. The formation of these nanoclusters is highly dependent on a series of post-translational modifications, such as mono-and multi-phosphorylation and dephosphorylation of residues. We theoretically simulate how a protein can be either mono-or multi-phosphorylated on several residues in functional nanoclusters, depending on effective biophysical parameters (diffusion, dwell time, etc.). Moving beyond a binary view of phosphorylation, this approach highlights the interplay between mono-and multi-phosphorylation, the cooperative effects generally associated with multi-phosphorylation networks, and stresses the role of phosphatases in transforming graded phosphorylation signals into almost switch-like responses. The results are discussed in light of experiments that probe the distribution of phospho-residues. |
| format | Preprint |
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arxiv_https___arxiv_org_abs_2511_09295 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | Simulating Mono-and Multi-Protein Phosphorylation within Nanoclusters Destaing, Olivier Fourcade, Bertrand Biological Physics Subcellular Processes Protein nanoclustering is a characteristic feature of their activated state and is essential for forming numerous subcellular structures. The formation of these nanoclusters is highly dependent on a series of post-translational modifications, such as mono-and multi-phosphorylation and dephosphorylation of residues. We theoretically simulate how a protein can be either mono-or multi-phosphorylated on several residues in functional nanoclusters, depending on effective biophysical parameters (diffusion, dwell time, etc.). Moving beyond a binary view of phosphorylation, this approach highlights the interplay between mono-and multi-phosphorylation, the cooperative effects generally associated with multi-phosphorylation networks, and stresses the role of phosphatases in transforming graded phosphorylation signals into almost switch-like responses. The results are discussed in light of experiments that probe the distribution of phospho-residues. |
| title | Simulating Mono-and Multi-Protein Phosphorylation within Nanoclusters |
| topic | Biological Physics Subcellular Processes |
| url | https://arxiv.org/abs/2511.09295 |