| Description | Rapid regulation of G-protein-coupled receptors (GPCRs) involves agonist- promoted receptor phosphorylation by GPCR kinases (GRKs) [ ]. This process is followed by arrestin binding and transient receptor internalisation. It has been shown that beta-adrenergic receptor kinase (beta ARK-1 or GRK2) follows a similar pattern of internalisation upon agonist activation of beta(2)-adrenergic receptors (beta(2)AR) and that beta ARK expression levels modulate receptor sequestration []. Such studies indicate a functional relationship between receptor phosphorylation and sequestration, showing that beta ARK not only translocates from the cytoplasm to the plasma membrane in response to receptor occupancy, but also shares endocytic mechanisms with the beta(2)AR []. These results suggest a role for beta ARK in the sequestration process, or involvement of receptor internalisation in the intracellular trafficking of the kinase []. | Name | GPCR kinase |
| Short Name | GPCR_kinase | Type | Family |
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