Tetratricopeptide Repeat Domain 5: A Potential Drug Target Or Biomarker

Target Name: TTC5

NCBI ID: G91875

Tetratricopeptide Repeat Domain 5: A Potential Drug Target Or Biomarker

Tetratricopeptide repeat domain 5 (TTC5) is a protein that is found in various organisms, including humans. It is a repeat domain that is composed of four amino acids repeated units, which is a type of genetic repetition. This protein is of interest as a potential drug target or biomarker due to its unique structure and the involvement of various diseases.

The TTC5 protein is involved in various cellular processes in the body, including cell signaling, DNA replication, and protein synthesis. It is a key component of the microtubules, which are important for cell division and transport of organelles within the cell. TTC5 is also involved in the regulation of mitochondrial function and in the development of certain diseases, such as cancer.

One of the key functions of TTC5 is its role in cell signaling. It is involved in the regulation of the level of a protein called tyrosine, which is a key signaling molecule in many cellular processes. Tyrosine is a amino acid that can be modified to have a positive or negative charge, which can interact with various other molecules and trigger various cellular responses. TTC5 is involved in the regulation of tyrosine levels, which can affect the activity of many different cellular signaling pathways.

Another function of TTC5 is its role in DNA replication. TTC5 is a component of the machinery that is used to copy the DNA of a cell during cell division. It is involved in the regulation of the timing of DNA replication and is thought to play a key role in the development of certain diseases, such as cancer.

In addition to its role in cell signaling and DNA replication, TTC5 is also involved in the regulation of protein synthesis. It is a component of the machinery that is used to translate mRNA into a protein. TTC5 is thought to play a key role in the regulation of the level of a protein called synapse-associated protein 2 (SAP2), which is involved in the formation of synapses between neurons.

The TTC5 protein is also of interest as a potential drug target or biomarker due to its involvement in the development of certain diseases. One of the main focuses of cancer research is to develop drugs that can inhibit the activity of TTC5 and disrupt its role in cancer development. This is an important area of 鈥嬧?媟esearch because many cancer treatments currently involve drugs that inhibit cell signaling pathways, which can have unintended consequences, such as damage to other parts of the body.

In addition to its potential as a cancer treatment, TTC5 may also be a useful biomarker for some diseases. For example, TTC5 has been shown to be elevated in the blood of patients with certain types of cancer, which could be used as a diagnostic marker for these diseases. Additionally, TTC5 has been shown to be involved in the regulation of cellular processes that are involved in the development of certain diseases, such as Alzheimer's disease and Parkinson's disease.

Overall, TTC5 is a protein that is involved in various cellular processes in the body and has been shown to be involved in the development of several diseases. Its unique structure and the involvement of various diseases make it an interesting potential drug target or biomarker. Further research is needed to fully understand the role of TTC5 in these diseases and to develop effective treatments.

Protein Name: Tetratricopeptide Repeat Domain 5

Functions: Cofactor involved in the regulation of various cellular mechanisms such as actin regulation, autophagy, chromatin regulation and DNA repair (PubMed:18451878, PubMed:31727855). In non-stress conditions, interacts with cofactor JMY in the cytoplasm which prevents JMY's actin nucleation activity and ability to activate the Arp2/3 complex. Acts as a negative regulator of nutrient stress-induced autophagy by preventing JMY's interaction with MAP1LC3B, thereby preventing autophagosome formation (By similarity). Involves in tubulin autoregulation by promoting its degradation in response to excess soluble tubulin (PubMed:31727855). To do so, associates with the active ribosome near the ribosome exit tunnel and with nascent tubulin polypeptides early during their translation, triggering tubulin mRNA-targeted degradation (PubMed:31727855). Following DNA damage, phosphorylated by DNA damage responsive protein kinases ATM and CHEK2, leading to its nuclear accumulation and stability. Nuclear TTC5/STRAP promotes the assembly of a stress-responsive p53/TP53 coactivator complex, which includes the coactivators JMY and p300, thereby increasing p53/TP53-dependent transcription and apoptosis. Also recruits arginine methyltransferase PRMT5 to p53/TP53 when DNA is damaged, allowing PRMT5 to methylate p53/TP53. In DNA stress conditions, also prevents p53/TP53 degradation by E3 ubiquitin ligase MDM2 (By similarity). Upon heat-shock stress, forms a chromatin-associated complex with heat-shock factor 1 HSF1 and p300/EP300 to stimulate heat-shock-responsive transcription, thereby increasing cell survival (PubMed:18451878). Mitochondrial TTC5/STRAP interacts with ATP synthase subunit beta ATP5F1B which decreased ATP synthase activity and lowers mitochondrial ATP production, thereby regulating cellular respiration and mitochondrial-dependent apoptosis. Mitochondrial TTC5/STRAP also regulates p53/TP53-mediated apoptosis (By similarity)

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