JNK3 Protein, Human (364a.a, His)

JNK3, a serine/threonine-protein kinase, is a key player in diverse neuronal processes, including proliferation, differentiation, migration, and programmed cell death. Activation of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway by extracellular stimuli, such as pro-inflammatory cytokines or physical stress, involves the phosphorylation and activation of JNK3 by dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7. Within this cascade, JNK3 phosphorylates critical transcription factors, particularly components of AP-1 like JUN and ATF2, thereby regulating AP-1 transcriptional activity. JNK3 plays pivotal roles in neuronal apoptosis by modulating signaling pathways, and it phosphorylates the neuronal microtubule regulator STMN2. Additionally, in the regulation of amyloid-beta precursor protein/APP signaling during neuronal differentiation, JNK3 phosphorylates APP. Furthermore, JNK3 contributes to neurite growth in spiral ganglion neurons and phosphorylates the CLOCK-BMAL1 heterodimer, influencing the photic regulation of the circadian clock. Notably, JNK3 phosphorylates JUND, and this phosphorylation is inhibited in the presence of MEN1.