IFNGR1: The Drug Target of the Future? (G3459)

Target Name: IFNGR1

NCBI ID: G3459

IFNGR1

IFNGR1: The Drug Target of the Future?

The IFNGR1 gene, located on chromosome 16, has long been known for its role in the regulation of insulin sensitivity and glucose metabolism. IFNGR1 is a single-chain transmembrane protein that plays a crucial role in the intracellular signaling pathway known as the insulin-like growth factor (IGF) signaling pathway. This pathway is responsible for regulating various cellular processes, including cell growth, differentiation, and metabolism.

The IFNGR1 gene has been associated with various diseases, including obesity, type 2 diabetes, and hypoglycemia. It has also been implicated in the development of certain cancers, such as breast and ovarian cancer. Therefore, the study of IFNGR1 and its potential as a drug target is of great interest.

IFNGR1 Variants

IFNGR1 has four known variants, which are IFNGR1-V1, IFNGR1-V2, IFNGR1-V3, and IFNGR1-V4. These variants differ in their amino acid sequences, with the most significant difference being in the last exon, which codes for the protein's C-terminus.

IFNGR1-V1, also known as IFNGR1-1621, has the longest N-terminus and the shortest C-terminus. It is expressed in various tissues, including the brain, pancreas, and muscle. It has been shown to regulate insulin sensitivity in both skeletal and adipose muscles.

IFNGR1-V2, also known as IFNGR1-1622, has a longer C-terminus than IFNGR1-V1 and is expressed in the pancreas and the liver. It has been shown to have insulin-like effects in the liver and to regulate insulin sensitivity in the pancreas.

IFNGR1-V3, also known as IFNGR1-1623, has a longer N-terminus than IFNGR1-V2 and is expressed in the muscle and the liver. It has been shown to have insulin-like effects in both muscle and liver cells.

IFNGR1-V4, also known as IFNGR1-1624, has the shortest N-terminus and the longest C-terminus. It is expressed in the muscle and the pancreas. It has been shown to have insulin-like effects in the muscle and pancreas.

The Differences in Expression and Activity

IFNGR1 has been shown to have various functions in cellular signaling pathways, including the regulation of insulin sensitivity, glucose metabolism, and cancer development. However, the exact mechanisms by which IFNGR1 functions are not well understood.

One of the main differences in the expression and activity of IFNGR1 variants is their N-terminus. IFNGR1-V1 has the longest N-terminus, which has been shown to have unique functions in regulating insulin sensitivity in skeletal and adipose muscles. IFNGR1-V2 and IFNGR1-V3 have longer N-terms than IFNGR1-V1 and IFNGR1-V4, which have been shown to have insulin-like effects in the liver and muscle, respectively.

The C-terminus of each IFNGR1 variant also has distinct differences in its expression and activity. IFNGR1-V1 has the shortest C-terminus, which has been shown to have unique functions in regulating insulin sensitivity in skeletal and adipose muscles. IFNGR1-V2 and IFNGR1-V3 have longer C-terms than IFNGR1-V1 and IFNGR1-V4, which have been shown to have insulin-like effects in the pancreas and muscle, respectively.

IFNGR1 and Cancer

IFNGR1 has

Protein Name: Interferon Gamma Receptor 1

Functions: Receptor subunit for interferon gamma/INFG that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:20015550). Associates with transmembrane accessory factor IFNGR2 to form a functional receptor (PubMed:7615558, PubMed:2971451, PubMed:7617032, PubMed:10986460, PubMed:7673114). Upon ligand binding, the intracellular domain of IFNGR1 opens out to allow association of downstream signaling components JAK1 and JAK2. In turn, activated JAK1 phosphorylates IFNGR1 to form a docking site for STAT1. Subsequent phosphorylation of STAT1 leads to dimerization, translocation to the nucleus, and stimulation of target gene transcription (PubMed:28883123). STAT3 can also be activated in a similar manner although activation seems weaker. IFNGR1 intracellular domain phosphorylation also provides a docking site for SOCS1 that regulates the JAK-STAT pathway by competing with STAT1 binding to IFNGR1 (By similarity)

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