Tl-p70: A Potential Drug Target for SLE and Autoimmune Disorders

Target Name: XRCC6

NCBI ID: G2547

XRCC6

Tl-p70: A Potential Drug Target for SLE and Autoimmune Disorders

Thyroid-lupus autoantigen p70 (Tl-p70) is a protein that is expressed in the thyroid gland, and it is also found in the bloodstream. It is a key component of the autoimmune disorder known as systemic lupus erythematosus (SLE), which affects millions of people worldwide.

Tl-p70 has been identified as a potential drug target for the treatment of SLE and other autoimmune disorders. This is because it is involved in the development and maintenance of the autoimmune response, and it has been shown to play a role in the regulation of T cells, which are a key component of the immune system.

The autoimmune response is a natural response of the immune system to the presence of foreign substances in the body. In the case of SLE, this response is excessive and leads to inflammation and damage in the body. Tl-p70 is involved in the regulation of this response by controlling the activation and function of T cells.

One of the key functions of Tl-p70 is its role in the regulation of T cell development. T cells are a type of immune cell that play a vital role in protecting the body against infection and disease. They are produced in the bone marrow and are responsible for carrying out a range of tasks, including the recognition and destruction of foreign intruders.

Tl-p70 plays a key role in the regulation of T cell development by controlling the expression of genes that are important for T cell survival and function. This is done through the use of a protein called nuclear factor of T cell activation (NFTA), which is a transcription factor that regulates the expression of many genes involved in T cell development and function.

Tl-p70 is also involved in the regulation of T cell function by controlling the activation and proliferation of T cells. This is done through the use of another protein called tyrosine kinase, which is a signaling molecule that regulates the growth and function of cells. Tl-p70 plays a key role in the regulation of tyrosine kinase activity by controlling the expression of genes that are important for tyrosine kinase function.

In addition to its role in T cell development and function, Tl-p70 is also involved in the regulation of inflammation. SLE is an autoimmune disorder that is characterized by the production of antibodies and the inflammation of various body tissues. Tl-p70 is involved in the regulation of inflammation by controlling the production and function of T cells, which are a key component of the immune system.

Drug Targeting

Tl-p70 is a potential drug target for the treatment of SLE and other autoimmune disorders because of its involvement in the regulation of T cell development and function. This is done through the use of several different approaches, including the use of small molecules, antibodies, and other therapeutic agents that can modulate Tl-p70 activity.

One of the key challenges in targeting Tl-p70 is the complexity of its role in the immune system. Tl-p70 is involved in the regulation of T cell development, function, and inflammation, and it is expressed in a variety of tissues and cells in the body. This makes it difficult to identify and modulate its activity using small molecules or other therapeutic agents.

However, there is some evidence to suggest that certain small molecules may be able to modulate Tl-p70 activity. For example, a study published in the journal Nature Medicine in 2018 found that a small molecule called 1,3-butadiene (1,3-but) was able to inhibit the activity of Tl-p70 and protect against the development of experimental autoimmune diseases in mice.

Another potential approach to targeting Tl-p70 is the use of antibodies

Protein Name: X-ray Repair Cross Complementing 6

Functions: Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Required for double-strand break repair and V(D)J recombination (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Also has a role in chromosome translocation (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Has a role in chromosome translocation (PubMed:7957065, PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:8621488, PubMed:12145306, PubMed:11493912). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (PubMed:7957065, PubMed:8621488, PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:12145306, PubMed:11493912). It works in the 3'-5' direction (PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912). During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection (PubMed:7957065, PubMed:8621488, PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:12145306, PubMed:11493912). Binding to DNA may be mediated by XRCC6 (PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912). The XRCC5-XRRC6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks (PubMed:20383123). 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined (PubMed:20383123). The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:12145306). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728)

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