Tau–amyloid precursor protein protein–protein interaction

The Tau–amyloid precursor protein (APP) protein-protein interaction is the direct molecular association between Tau, a cytoskeletal microtubule-associated protein, and APP, a transmembrane glycoprotein involved in amyloid-beta generation[1][3]. Both proteins are central to the pathology of Alzheimer’s disease: extracellular β-amyloid plaques result from APP cleavage, while intracellular neurofibrillary tangles consist of aggregated phosphorylated Tau[3][4]. Recent studies reveal that soluble Tau directly binds to the N-terminal region of APP, facilitating the internalization and propagation of Tau in neuronal cells and contributing to disease progression[3]. Inhibition or modulation of this interaction is being investigated as a novel therapeutic strategy, using peptides or small molecules designed to block or alter the Tau–APP interaction interface[1][3]. While the physiological function of the interaction remains incompletely characterized, its pathological role in neurodegeneration is a focus of ongoing drug discovery, with experimental evidence showing cognitive and pathological improvements by targeting this interface in preclinical models[1][3][4].

Other names

Tau–APP interactionTau–APP PPITau-APP bindingTau–amyloid precursor protein interface

Inhibition or modulation of Tau–APP binding to reduce pathological Tau uptake, aggregation, phosphorylation, or to interfere with downstream neurotoxic processes