EIF2AK2: A Promising Drug Target and Biomarker for Interferon-Inducible Double Stranded RNA-Driven Processes

Target Name: EIF2AK2

NCBI ID: G5610

EIF2AK2

EIF2AK2: A Promising Drug Target and Biomarker for Interferon-Inducible Double Stranded RNA-Driven Processes

Abstract:

Interferon-inducible double stranded RNA (ISRNA) is a crucial regulator of gene expression and has been implicated in various diseases. EIF2AK2, a protein kinase thatocalizes with ISRNA, has been identified as a potential drug target or biomarker. This article summarizes the current understanding of EIF2AK2, its functions, and potential therapeutic applications.

Introduction:

Interferon-inducible double stranded RNA (ISRNA) is a small non-coding RNA molecule that plays a central role in regulating gene expression by controlling the translation of mRNAs into proteins. ISRNA has been shown to participate in various cellular processes, including cell growth, apoptosis, and immune response. ISRNA has also been implicated in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

EIF2AK2: A Protein Kinase That Binds to ISRNA

EIF2AK2 is a protein kinase that was identified as a potential drug target or biomarker due to its unique ability to interact with ISRNA. EIF2AK2 is a 21-kDa protein that contains a catalytic domain and a carboxy-terminal domain. The catalytic domain is responsible for the kinetic activity of EIF2AK2, while the carboxy-terminal domain is involved in the regulation of EIF2AK2's activity.

Several studies have shown that EIF2AK2 can interact with ISRNA in a variety of ways. For instance, EIF2AK2 has been shown to physically interact with ISRNA through its catalytic domain, leading to a stable complex that can be used for ISRNA-mediated signaling pathways (6 ). Additionally, EIF2AK2 has been shown to regulate the activity of ISRNA-mediated signaling pathways by phosphorylated ATP, which is thought to play a crucial role in the regulation of protein abundance and stability.

EIF2AK2's Interaction with ISRNA: Implications for ISRNA-Mediated Signaling

The interaction between EIF2AK2 and ISRNA has significant implications for ISRNA-mediated signaling pathways. ISRNA has also been shown to play a central role in regulating various cellular processes, including cell growth, apoptosis, and immune response. participate in various signaling pathways, including cell proliferation, angiogenesis, and neurodegenerative diseases. Therefore, the interaction between EIF2AK2 and ISRNA is of great interest for understanding the regulation of these processes.

EIF2AK2 has been shown to play a negative role in ISRNA-mediated signaling pathways. For instance, EIF2AK2 has been shown to inhibit the activity of ISRNA-mediated signaling pathways by phosphate phosphate ATP and leading to the dissociation of ISRNA from its cognate protein kinase( 10). This inhibition of ISRNA-mediated signaling pathways by EIF2AK2 has implications for the regulation of cellular processes, including cancer growth and the development of neurodegenerative diseases.

EIF2AK2 as a Potential Drug Target: Implications for Therapeutic Applications

The interaction between EIF2AK2 and ISRNA has significant implications for the development of therapeutic applications. By inhibiting the activity of ISRNA-mediated signaling pathways, EIF2AK2 may be a useful drug target for the treatment of various diseases.

One therapeutic potential application of EIF2AK2 is in the treatment of cancer. ISRNA has been shown to play a central role in the regulation of cancer cell growth and progression. By inhibiting the activity of ISRNA-mediated signaling pathways,

Protein Name: Eukaryotic Translation Initiation Factor 2 Alpha Kinase 2

Functions: IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19507191, PubMed:19189853, PubMed:21123651, PubMed:21072047, PubMed:22948139, PubMed:23229543, PubMed:22381929). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:20171114, PubMed:19840259, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:22214662, PubMed:19229320). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity)

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