DSRNA Dep Protein Kinase, also known as PKR (Protein Kinase R) or EIF2AK2, is a multifunctional protein kinase enzyme found in mammalian cells. It is primarily involved in the regulation of various cellular processes, particularly in response to viral infections or cellular stress.
DSRNA Dep Protein Kinase is a serine/threonine kinase that phosphorylates itself and other target proteins, including the eukaryotic initiation factor 2 alpha (eIF2α). Phosphorylation of eIF2α inhibits protein synthesis, an essential process for viral replication. By blocking protein synthesis, PKR restricts viral proliferation and replication, thereby promoting the immune response against viral infections.
Furthermore, DSRNA Dep Protein Kinase plays a crucial role in cellular stress responses, such as endoplasmic reticulum (ER) stress and oxidative stress. It acts as a sensor for these stressful conditions, triggering a cascade of downstream signaling events leading to apoptosis (programmed cell death) or autophagy (cell recycling). These cellular responses are essential for maintaining cellular homeostasis and eliminating damaged or infected cells.
Moreover, DSRNA Dep Protein Kinase also participates in various immune signaling pathways, including the regulation of interferon production and response. It is activated by double-stranded RNA (dsRNA), a byproduct of viral replication or during certain cellular processes. Once activated, PKR initiates a signaling cascade that triggers the immune response, resulting in the production of antiviral proteins and cytokines.
In summary, DSRNA Dep Protein Kinase, or PKR, is a versatile protein kinase involved in regulating various cellular processes, including protein synthesis, stress responses, apoptosis, autophagy, and immune signaling. It is a critical
