TPK: A Protein Potential Drug Target for Cancer and Neurodegenerative Diseases

Target Name: NTRK1

NCBI ID: G4914

NTRK1

TPK: A Protein Potential Drug Target for Cancer and Neurodegenerative Diseases

Tropomyosin-related kinase (TPK) is a protein that plays a critical role in cell signaling pathways. It is a key regulator of the myosin-associated protein complex (MAPC) and is involved in the regulation of muscle contractions. TPK has been identified as a potential drug target for the treatment of various diseases, including cancer, neurodegenerative diseases, and muscle-related conditions.

TPK is a protein that is expressed in various tissues, including muscle, heart, and brain. It is a 21-kDa protein that consists of two distinct domains: a catalytic domain and a regulatory domain. The catalytic domain is responsible for the catalytic activity of TPK, while the regulatory domain is involved in the regulation of TPK activity.

The catalytic domain of TPK is composed of a single catalytic center that is located at the center of the protein. This center contains a nucleotide-binding oligomerization (NBO) domain, which is responsible for the catalytic activity of TPK. The NBO domain is a unique feature that allows TPK to interact with nucleotides in a specific sequence. This interaction between TPK and nucleotides is critical for its catalytic activity.

The regulatory domain of TPK is composed of a nucleotide-binding oligomerization (NBO) domain and a protein-interaction domain. The NBO domain is responsible for interacting with nucleotides in a specific sequence, while the protein-interaction domain is responsible for interacting with other proteins.

TPK has been shown to play a critical role in the regulation of muscle contractions. It is involved in the regulation of myosin ATPase (M-ATPase), which is the protein that initiates muscle contractions. M-ATPase is a protein that is expressed in muscle cells and is involved in the regulation of muscle force production. TPK has been shown to regulate the activity of M-ATPase in a specific way, which is necessary for muscle contractions.

In addition to its role in muscle contractions, TPK has also been shown to play a critical role in the regulation of cancer cell proliferation. It is involved in the regulation of cell cycle progression and has been shown to be involved in the development of cancer. TPK has also been shown to play a critical role in the regulation of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease.

TPK has also been identified as a potential drug target for the treatment of various diseases. For example, TPK has been shown to be involved in the regulation of cancer cell migration and has been shown to be a potential therapeutic target for cancer. In addition, TPK has also been shown to be involved in the regulation of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease.

The catalytic domain of TPK is responsible for its catalytic activity, while the regulatory domain is involved in its regulation. The NBO domain is responsible for interacting with nucleotides in a specific sequence, while the protein-interaction domain is responsible for interacting with other proteins. TPK has been shown to play a critical role in the regulation of muscle contractions and has also been shown to play a critical role in the regulation of cancer cell proliferation and neurodegenerative diseases.

In conclusion, TPK is a protein that has been shown to play a critical role in various cell signaling pathways. It is a key regulator of the myosin-associated protein complex (MAPC) and is involved in the regulation of muscle contractions, cancer cell proliferation, and neurodegenerative diseases. As a result, TPK has been identified as a potential drug target for the treatment of various diseases, including cancer, neurodegenerative diseases, and muscle-related conditions. Further research is needed to fully understand the role of TPK in these diseases and to develop effective therapies.

Protein Name: Neurotrophic Receptor Tyrosine Kinase 1

Functions: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand (PubMed:1850821, PubMed:1849459, PubMed:1281417, PubMed:8325889, PubMed:15488758, PubMed:22649032, PubMed:17196528, PubMed:27445338). Can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival (By similarity). Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation (PubMed:1281417). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors

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•   general information;
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•   expression level;
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