Arrestin: Difference between revisions
m added biochem stub tag |
mNo edit summary |
||
| Line 1: | Line 1: | ||
The Arrestins are a family of proteins which regulate the activity of [[G-protein coupled receptors]] (GPCR) by binding to these proteins at serine or threonine residues which have been phosphorylated by [[G-protein coupled receptor kinases]] (GRKs). Different Arrestins can reduce the activity of their target receptor proteins in a variety of different ways. The simplest mechanism for an arrestin to inhibit the activation of its target is for it to bind to the intracellular domain of the GPCR in such a way that the binding site for the heterotrimeric G-protein is blocked, preventing extra cellular signals from activating the pathway. Another regulatory mechanism employed by certain arrestin family members is to link their target proteins to elements of the membrane internalization machinery which leads to the degradation of the receptor proteins within lysosomes. |
The Arrestins are a family of proteins which regulate the activity of [[G-protein coupled receptors]] (GPCR) by binding to these proteins at serine or threonine residues which have been phosphorylated by [[G-protein coupled receptor kinases]] (GRKs). Different Arrestins can reduce the activity of their target receptor proteins in a variety of different ways. The simplest mechanism for an arrestin to inhibit the activation of its target is for it to bind to the intracellular domain of the GPCR in such a way that the binding site for the heterotrimeric G-protein is blocked, preventing extra cellular signals from activating the pathway. Another regulatory mechanism employed by certain arrestin family members is to link their target proteins to elements of the membrane internalization machinery which leads to the degradation of the receptor proteins within lysosomes. |
||
The most well known family member is β-Arrestin which binds to sites on the β-Adrenergic receptor which are phosphorylated by the β-Adrenergic receptor kinase. |
The most well known family member is β-Arrestin which binds to sites on the [[β-Adrenergic receptor]] which are phosphorylated by the β-Adrenergic receptor kinase. |
||
(see [http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107941 OMIM]) |
(see [http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107941 OMIM]) |
||
Revision as of 18:48, 22 June 2006
The Arrestins are a family of proteins which regulate the activity of G-protein coupled receptors (GPCR) by binding to these proteins at serine or threonine residues which have been phosphorylated by G-protein coupled receptor kinases (GRKs). Different Arrestins can reduce the activity of their target receptor proteins in a variety of different ways. The simplest mechanism for an arrestin to inhibit the activation of its target is for it to bind to the intracellular domain of the GPCR in such a way that the binding site for the heterotrimeric G-protein is blocked, preventing extra cellular signals from activating the pathway. Another regulatory mechanism employed by certain arrestin family members is to link their target proteins to elements of the membrane internalization machinery which leads to the degradation of the receptor proteins within lysosomes.
The most well known family member is β-Arrestin which binds to sites on the β-Adrenergic receptor which are phosphorylated by the β-Adrenergic receptor kinase.
(see OMIM)
.svg){kind=small} | This biochemistry article is a stub. You can help Wikipedia by expanding it. |