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Intrinsically disordered proteins such as Tau protein, Amyloid beta and Alpha-synuclein drive neurodegeneration through misfolding and aggregation. 14-3-3 proteins emerge as key modulators of these processes by engaging client proteins in their monomeric and early assembly states. Multivalent, phosphorylation-dependent interactions reshape the conformational ensembles of these proteins. Strikingly, these interactions suppress amyloid fibril formation and redirect aggregation pathways. These results provide a mechanistic framework for understanding how protein–protein interactions regulate amyloid formation at the molecular level.
