TBK1: A Potential Drug Target for Many Diseases (G29110)

Target Name: TBK1

NCBI ID: G29110

TBK1: A Potential Drug Target for Many Diseases

TBK1 (Serine/threonine-protein kinase) is a protein that is expressed in a variety of tissues throughout the body, including the brain, heart, and kidneys. It plays a role in the regulation of cell growth, differentiation, and survival, and is known to be involved in the development and progression of many diseases, including cancer.

In recent years, researchers have been interested in identifying potential drug targets for TBK1, as this protein has been shown to be involved in the development of many diseases and is often overexpressed in cancer cells. In addition, TBK1 has also been shown to be involved in the regulation of cellular signaling pathways, and has been identified as a potential target for small molecules, antibodies, and other therapeutic agents.

One of the challenges in studying TBK1 is its complex structure and the fact that it is expressed in a variety of tissues, making it difficult to study its function in a specific context. However, researchers have been able to identify several key features of TBK1 that are involved in its function.

One of the most well-studied features of TBK1 is its catalytic activity, which is the process by which it adds a phosphate group to other proteins. This process is important for the regulation of cellular signaling pathways, and is involved in the development and progression of many diseases. Researchers have been able to use this activity to identify potential drug targets for TBK1.

Another key feature of TBK1 is its ability to interact with other proteins, including tyrosine kinases. This interaction is important for the regulation of cellular signaling pathways, and is involved in the development and progression of many diseases. Researchers have been able to use this interaction to identify potential drug targets for TBK1.

In addition to its catalytic activity and ability to interact with other proteins, TBK1 has also been shown to be involved in the regulation of cellular signaling pathways. This includes the regulation of the MAPK/ERK signaling pathway, which is involved in the development and progression of many diseases. Researchers have been able to use this feature to identify potential drug targets for TBK1.

Overall, TBK1 is a complex protein that is involved in the regulation of many cellular signaling pathways. As such, it is a potential drug target for the treatment of a variety of diseases. While further research is needed to fully understand its function and potential as a drug target, the studies that have been done so far suggest that TBK1 is a promising target for the development of new therapies.

Protein Name: TANK Binding Kinase 1

Functions: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:12692549, PubMed:14703513, PubMed:18583960, PubMed:12702806, PubMed:15367631, PubMed:10581243, PubMed:11839743, PubMed:15485837, PubMed:21138416, PubMed:25636800, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:26611359, PubMed:32404352). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:14703513, PubMed:18583960, PubMed:12702806, PubMed:15367631, PubMed:25636800). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (PubMed:12702806, PubMed:15367631, PubMed:25636800, PubMed:32972995). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (PubMed:23453971, PubMed:23453972, PubMed:23746807). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800, PubMed:30842653). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons (PubMed:25636800). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes (PubMed:21931631). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (PubMed:10783893, PubMed:15489227). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (PubMed:21617041). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (PubMed:27103069). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (PubMed:31709703). Phosphorylates and activates AKT1 (PubMed:21464307). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C (PubMed:21270402). Phosphorylates Borna disease virus (BDV) P protein (PubMed:16155125). Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system (PubMed:22851595)

More Common Targets