Aside from glycogen synthase kinase 3(GSK3), p38, and ERK, Taucould be phosphorylated by JNK on various locations that are hyperphosphorylatedin paired helical fragments.30,35 Patients with AD haveshown incremented activity of JNK in neurofibrillary tangles in braintissue.36 In addition, JNK activity isenhanced in tangles in Tg2576/PS1P264L and traumatic brain injurymouse models, where JNK is colocalized with phosphorylated Tau.31,32 Noteworthy, D-JNKI-1, which is a JNK inhibitor peptide, reducesTau phosphorylation and subsequent aggregation.32 The gene discussed is MAPT; the disease is Alzheimer disease.