EIF2AK2 Protein, Human (Active, sf9, GST)

EIF2AK2 Protein, an interferon-induced dsRNA-dependent serine/threonine-protein kinase, stands at the forefront of the innate immune response to viral infections. Upon viral challenge, EIF2AK2 phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha), initiating the integrated stress response (ISR). This response acts as a potent antiviral strategy by converting EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to the shutdown of cellular and viral protein synthesis. Concurrently, ISR-specific mRNAs, such as the transcriptional activator ATF4, are preferentially translated, orchestrating a multifaceted defense mechanism. EIF2AK2's antiviral activity extends to a wide array of DNA and RNA viruses, including HCV, HBV, MV, and HHV-1. Beyond its role in antiviral defense, EIF2AK2 regulates signal transduction, apoptosis, cell proliferation, and differentiation. Its versatile kinase activity targets substrates like p53/TP53, PPP2R5A, DHX9, ILF3, IRS1, and the HHV-1 viral protein US11. Notably, EIF2AK2's impact extends to the modulation of various signaling pathways (p38 MAP kinase, NF-kappa-B, and insulin signaling) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of pro-inflammatory cytokines and IFNs. It acts as a versatile regulator, positively and negatively influencing the insulin signaling pathway and playing a role in the assembly and activation of inflammasomes. Moreover, EIF2AK2 contributes to the regulation of the cytoskeleton by binding to gelsolin (GSN), modulating its activity and impacting actin dynamics (By similarity).