About RGS / Regulator of G-Protein Signaling:
The Regulator of G-Protein Signaling (RGS) is a family of signaling proteins that regulate the activity of G protein-coupled receptors. The RGS proteins are known to be regulators of many processes, including neurotransmitter release, cell motility and proliferation, and differentiation. This blog post will go into detail about the structure, function, and interactions for this important regulator in mammalian cells!
Regulator of G-Protein Signaling is a protein that binds to and controls the activity of receptor systems. These proteins are involved in regulating cellular responses, including but not limited to cell motility, proliferation, differentiation, or death. Regulators may be constitutively associated with one type of signal transduction pathway (such as cAMP) or may bind and activate the receptors for a particular kind of signal (such as growth factors) either following phosphorylation on tyrosine residues by protein kinases.
Regulator of G-Protein Signaling Interactions
These proteins are found in the plasma membrane and regulate other protein interactions with GPCRs by slowing their activation or desensitization. For example, RGS-A regulates serotonin release from neurons which then modulates mood, sleep patterns, appetite - just to name a few! They also operate as molecular switches that control the duration of the GPCR signaling by slowing its deactivation process. These regulators bind G-proteins to either activate them (via guanine nucleotide release) or inhibit them (by interfering with GDP binding). One of the most well-characterized regulators is RGS11, which inhibits G-protein signaling by binding to the alpha subunit of a G-protein coupled receptor.
The structure of these proteins is often quite complex, with multiple domains that assist in carrying out their functions. Regulators are classified according to whether they regulate G-protein, cytokine, receptor tyrosine kinase, or phospholipid signal transduction.