TRPC4AP: A Potential Drug Target and Biomarker for Chronic Pain

Target Name: TRPC4AP

NCBI ID: G26133

TRPC4AP

TRPC4AP: A Potential Drug Target and Biomarker for Chronic Pain

Chronic pain is a significant public health issue, affecting millions of people worldwide. The World Health Organization (WHO) estimates that approximately 10% of the global population experiences chronic pain, with costs associated with such pain reaching $600 billion annually. Chronic pain can be caused by various conditions, including neuropathic pain, back pain, and rheumatoid arthritis, and its management is often challenging and expensive.

TRPC4AP, a G protein-coupled receptor (GPCR), is a potential drug target and biomarker for chronic pain. It is a transmembrane protein that plays an important role in the regulation of pain signaling. The TRPC4AP gene has not yet been fully characterized, but its functions in pain perception and regulation are well established.

The TRPC4AP Receptor

The TRPC4AP receptor is a GPCR that is expressed in various tissues and cells, including neurons, endothelial cells, and immune cells. It is a member of the TRPC family of GPCRs, which are characterized by the presence of a unique C-terminal hypervariable region (HVR). The TRPC4AP receptor is expressed in the central nervous system (CNS) and has been implicated in pain perception, neuropathic pain, and neuroinflammation.

TRPC4AP is a 12-amino acid protein that consists of an extracellular domain, a transmembrane region, and an intracellular domain. The extracellular domain is involved in the formation of TRPC4AP-GPCR interactions and may be involved in the regulation of TRPC4AP function. The transmembrane region is responsible for the delivery and retention of TRPC4AP in the cell membrane, while the intracellular domain is involved in the regulation of TRPC4AP signaling.

The TRPC4AP receptor is composed of two subunits, TRPC4AP1 and TRPC4AP2. TRPC4AP1 is the N-terminus subunit, while TRPC4AP2 is the C-terminus subunit. Both subunits contain a unique catalytic center that is responsible for the binding of agonists and the regulation of TRPC4AP signaling.

TRPC4AP Signaling

TRPC4AP is involved in pain signaling by modulating the activity of various neurotransmitter systems, including opioids, serotonins, and dopamine. Agonists that bind to TRPC4AP activate its intracellular domain and regulate the activity of multiple downstream signaling pathways.

The TRPC4AP receptor is activated by agonists that bind to the catalytic center of the subunit. This activated state causes an increase in the activity of several downstream signaling pathways, including the regulation of pain perception and the modulation of neurotransmitter systems.

TRPC4AP has been shown to play a role in the regulation of pain perception in various models of pain, including neuropathic pain and neuroinflammation. For example, TRPC4AP has been shown to modulate the activity of opioids and to influence the expression of genes involved in pain perception.

TRPC4AP as a Potential Drug Target

The TRPC4AP receptor is a potential drug target for chronic pain because of its involvement in pain signaling. Several TRPC4AP antagonists have been developed and are currently being tested in clinical trials. These antagonists have the potential to alleviate pain in various models of chronic pain, including neuropathic pain and neuroinflammation.

TRPC4AP has also been shown to be involved in the regulation of neuroinflammation, which is a significant contributor to chronic pain. Therefore, targeting TRPC4AP with small molecules or other therapeutic approaches may be an effective way to treat chronic pain.

TRPC4AP as a Biomarker

TRPC4AP has also been shown to be involved in the regulation of pain perception and neurotransmission. Therefore, it may be an attractive biomarker for the diagnosis and monitoring of chronic pain.

The expression and activity of TRPC4AP can be

Protein Name: Transient Receptor Potential Cation Channel Subfamily C Member 4 Associated Protein

Functions: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control (PubMed:20551172, PubMed:29779948). The DCX(TRPC4AP) complex specifically mediates the polyubiquitination and subsequent degradation of MYC as part of the DesCEND (destruction via C-end degrons) pathway (PubMed:20551172, PubMed:29779948). The DesCEND (destruction via C-end degrons) pathway recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(TRPC4AP) complex specifically recognizes proteins with an arginine at the minus 3 position (R-3 motif) at the C-terminus, such as MYC, leading to their ubiquitination and degradation (PubMed:29779948). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome (By similarity). Involved in JNK activation via its interaction with TRAF2 (By similarity). Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1 (By similarity)

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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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