The intrinsically disordered protein Tau is highly phosphorylated under pathological conditions, which, among others, results in Tau liquid–liquid phase separation (LLPS), followed by aggregation. The hub protein 14-3-3 regulates Tau protein solubility and prevents LLPS by binding with phosphorylated Tau residues pS214...
Maxime C. M. van den Oetelaar, Leandre M. Ravatt, Francisco Maqueda Zelaya et al.· RSC Chemical Biology· 0 citations
14-3-3 Proteins are hub proteins with an extensive interactome of phosphorylated client proteins, making them attractive targets for molecular glues (MGs) that stabilize specific 14-3-3/client protein complexes. However, selectively stabilizing individual 14-3-3 protein−protein interactions (PPIs) remains a key chall...
Marloes A. M. Pennings, G. Lauffer, Markella Konstantinidou et al.· Journal of Medicinal Chemist...· 0 citations
The tumor suppressor p53 is regulated by phosphorylation-dependent protein-protein interactions, including via binding to 14-3-3 adaptor proteins, which can tune p53 activity. Molecular glue (MG)-induced stabilization of 14-3-3/client interactions offers an attractive strategy to probe such networks, but cellular engag...
Diana C. Muñoz-Lasso, Yan Ni, Glenn Weber et al.· ACS Chemical Biology· 0 citations
A molecular glue-stabilizer and PROTAC strategies are combined to enable ubiquitination of the 14-3-3/estrogen receptor α complex, revealing cooperative linker-dependent activity and a structural basis for targeted E3 ligase recruitment.
Carlo J. A. Verhoef, Charlotte Crowe, M. Nakasone et al.· Nature Communications· 0 citations
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