Target Name: OPTN
NCBI ID: G10133
Other Name(s): optic neuropathy-inducing protein | HIP-7 | OPTN_HUMAN | TFIIIA-IntP | ALS12 | nemo-related protein | FIP2 | Optineurin, transcript variant 1 | Huntingtin yeast partner L | OPTN variant 1 | NEMO-related protein | Optineurin | tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains | GLC1E | Glaucoma 1, open angle, E (adult-onset) | OPTN variant 4 | huntingtin-interacting protein 7 | huntingtin-interacting protein L | E3-14.7K-interacting protein | optineurin | HYPL | NRP | Huntingtin-interacting protein 7 | OPTN variant 2 | Huntingtin interacting protein L | Transcription factor IIIA-interacting protein | transcription factor IIIA-interacting protein | huntingtin yeast partner L | TFIIIA-INTP | Huntingtin-interacting protein L | Nemo-related protein | Optic neuropathy-inducing protein | Tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains | HIP7 | Optineurin, transcript variant 2 | Optineurin, transcript variant 4 | FIP-2 | transcrption factor IIIA-interacting protein

OPTN: The Potential Drug Target and Biomarker

Optimized Protein-Protein Interaction Network (OPTN) is a protein-protein interaction network that has been identified as a potential drug target and biomarker in various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. OPTN is a highly interconnected network of proteins that are involved in various cellular processes, including cell signaling, protein-protein interactions, and intracellular signaling pathways.

The OPTN network was first identified by researchers using a computational approach, and it has been shown to play a crucial role in the regulation of various cellular processes, including cell proliferation, differentiation, and survival. The OPTN network is composed of a large number of proteins that are involved in different cellular functions, including but not limited to cell signaling pathways, DNA replication, gene expression, and protein-protein interactions.

One of the key features of the OPTN network is its flexibility. The network can be modified by adding or removing various proteins, and this modification can have a significant impact on the network's structure and function. This makes the OPTN network a potentially promising drug target, as researchers can target specific proteins and alter their behavior to improve the treatment of various diseases.

In cancer, OPTN has been shown to play a crucial role in the regulation of various cellular processes, including cell signaling, angiogenesis, and drug resistance. Many studies have shown that OPTN-mediated signaling pathways are involved in the development and progression of various types of cancer, including breast cancer, lung cancer, and colorectal cancer.

For example, research has shown that overexpression of the OPTN network can promote the growth and survival of various cancer cells, and that inhibition of OPTN signaling pathways can be an effective method of cancer treatment. Additionally, the OPTN network has been shown to play a role in drug resistance, as many cancer cells are able to survive in the presence of various chemotherapy drugs.

In neurodegenerative diseases, OPTN has been shown to be involved in the regulation of various cellular processes, including protein-protein interactions and intracellular signaling pathways. The OPTN network has been implicated in the development and progression of neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease.

For example, research has shown that OPTN-mediated signaling pathways are involved in the production of neurodegenerate proteins, including beta-amyloid plaques and neurofilaments. Additionally, the OPTN network has been shown to play a role in the regulation of neurotransmitter release and synaptic plasticity, which are important for the function of nerve cells.

In autoimmune diseases, OPTN has been shown to be involved in the regulation of various cellular processes, including immune cell function and inflammation. The OPTN network has been implicated in the development and regulation of autoimmune diseases, including rheumatoid arthritis, lupus, and multiple sclerosis.

For example, research has shown that OPTN-mediated signaling pathways are involved in the regulation of immune cell function, including the production and activation of T cells and B cells. Additionally, the OPTN network has been shown to play a role in the regulation of inflammation, as OPTN has been shown to be involved in the production of pro-inflammatory cytokines.

In conclusion, OPTN is a protein-protein interaction network that has been shown to play a crucial role in various cellular processes, including cell signaling, protein-protein interactions, and intracellular signaling pathways. The OPTN network is a potentially promising drug target and biomarker, and its research has the potential to lead to new treatments for a variety of diseases.

Protein Name: Optineurin

Functions: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment (PubMed:22854040). Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52

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