Phosphorylated threonine 231–proline 232 motif in microtubule-associated protein tau, cis conformation (Phospho-Tau (Thr231-Pro232, cis))

The **cis conformation of the phosphorylated Thr231–Pro232 motif in microtubule-associated protein tau** is a specific post-translationally modified structural epitope of tau protein, arising when threonine at position 231 is phosphorylated and its adjacent peptide bond to proline 232 is in a cis conformation. Tau is an intrinsically disordered protein primarily responsible for stabilizing microtubules in neurons. Hyperphosphorylation at Thr231 is critical in disease as it induces structural changes that disrupt tau-tubulin interaction, promote a more aggregation-prone conformation, and facilitate the formation of neurofibrillary tangles characteristic of Alzheimer’s disease and other tauopathies[1][2]. The phosphorylation at this motif alters tau’s ability to promote microtubule assembly and is a recognized early event in tau pathology. The cis/trans isomerization of the peptide bond following phosphorylation is regulated in cells by prolyl isomerases, and the pathogenic cis conformation is believed to evade physiological degradation and drive neurotoxicity. CSF levels of phospho-tau (Thr231) are used as early biomarkers for Alzheimer’s disease[4]. While not a classical receptor, channel, or enzyme, the motif represents a promising frontier therapeutic target for neurodegenerative disease research.

Other names

Phospho-Tau Thr231-Pro232 (cis)Tau pThr231-Pro232 (cis)Cis-pT231-tau

Inhibition of phosphorylation or isomerization at this site may reduce pathological aggregation and neurotoxicity Therapeutic modulation of cis/trans isomerization to favor non-pathogenic states