DAPK3/ZIPK Protein, Human (sf9, GST)

DAPK3/ZIPK, a serine/threonine kinase, intricately regulates diverse cellular processes such as apoptosis, autophagy, transcription, translation, and actin cytoskeleton reorganization. It plays a crucial role in orchestrating both type I apoptotic and type II autophagic cell death signals, depending on the cellular context. DAPK3/ZIPK also governs smooth muscle contraction and is implicated in the regulation of starvation-induced autophagy. Its influence on myosin phosphorylation extends to both smooth muscle and non-muscle cells, where it directly phosphorylates MYL12B and MYL9 or inhibits smooth muscle myosin phosphatase (SMPP1M) via PPP1R12A phosphorylation. In non-muscle cells, it phosphorylates MYL12B, leading to actin cytoskeleton reorganization. Isoform 2, an alternative form of DAPK3/ZIPK, contributes to myosin, PPP1R12A, and MYL12B phosphorylation, inducing the condensation of actin stress fibers into thick bundles. Additionally, DAPK3/ZIPK plays a role in actin filament focal adhesion dynamics, and its function is modulated by RhoD. Moreover, it positively regulates canonical Wnt/beta-catenin signaling, interacts with NLK and TCF7L2, phosphorylates RPL13A upon interferon-gamma activation, enhancing its involvement in transcript-selective translation inhibition. DAPK3/ZIPK's diverse functions also extend to the regulation of cell cycle progression and cell proliferation, potentially acting as a tumor suppressor.