JNK is a protein kinase that can phosphorylate Ser63 and Ser73 at the amino terminal of c-Jun (a transcription regulator, a member of the leucine zipper family). It is a family of mitogen-activated protein kinase superfamily, including JNK1, JNK2, and JNK3. When Thr and Tyr in the activation motif Thr-Pro-Tyr are phosphorylated by JNKK1 and JNKK2, the activating enzyme can be activated. Phosphorylation of c-Jun and other proteins, thereby affecting the occurrence of cell apoptosis, inflammation and tumors.
JNK-mediated caspase-independent cell death plays an important role in tissue homeostasis during development. JNK signaling is a family of multifunctional signaling molecules that can be activated in response to a series of stress conditions and are effective inducers of cell death. More and more evidence collected in the AD model supports the involvement of JNK signaling in AD. It is reported that JNK can be activated by Aβ and induce the production of hyperphosphorylated Tau. In addition, inhibiting JNK with peptides can prevent cell loss in the AD model. Therefore, it is not only necessary to pay attention to the role of JNK in the pathogenesis of AD, but also to its potential as a therapeutic target and biomarker.
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