RGS1 Human

RGS1 is located on the cytosolic side of the plasma membrane and contains a conserved 120 amino acid motif known as the RGS domain . This domain is essential for its function as a GTPase-activating protein (GAP). By binding to activated, GTP-bound G alpha subunits, RGS1 increases the rate of conversion of GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal .

RGS1 is involved in various biological processes, including the regulation of G protein-coupled receptor (GPCR) signaling cascades. It plays a significant role in signaling downstream of N-formylpeptide chemoattractant receptors and leukotriene receptors . Additionally, RGS1 inhibits B cell chemotaxis toward CXCL12, which is crucial for immune responses .

Mutations and dysregulation of the RGS1 gene have been associated with several diseases, including lymphoma and celiac disease . The gene is also linked to multiple sclerosis and type I diabetes, which are T cell-mediated pathologies . Elevated levels of RGS1 in T cells from the human gut have been observed in conditions of intestinal inflammation, suggesting its role in regulating T cell migration and immune responses in the gut .

Research on RGS1 has provided insights into its role in immune cell trafficking and tissue immunopathologies. Studies have shown that RGS1 expression is higher in T cells from the human gut compared to peripheral blood, and this expression can be exaggerated in inflammatory conditions . Understanding the function and regulation of RGS1 can help develop therapeutic strategies for diseases associated with its dysregulation.