GRK6are

GRK6are refers to the AU-rich element (ARE) in the 3' untranslated region of the GRK6 mRNA. GRK6 stands for G protein-coupled receptor kinase 6, an enzyme involved in phosphorylation of activated GPCRs to promote desensitization and internalization. The GRK6 ARE is a cis-regulatory element characterized by multiple AUUUA motifs within a uridine-rich context that can recruit ARE-binding proteins.

Binding proteins like tristetraprolin, HuR, and AUF1 interact with the GRK6 ARE, influencing mRNA stability and translation. Depending on the cell type and signaling state, the GRK6 ARE can promote mRNA decay or, in some contexts, stabilization and enhanced translation.

Regulation and mechanism: Signaling pathways such as p38 MAPK modulate ARE function by phosphorylating binding proteins, altering their affinity and recruiting decay or stabilizing complexes.

Biological significance: By modulating GRK6 mRNA stability, GRK6 ARE contributes to dynamic control of GRK6 protein levels in tissues including brain and immune cells, affecting GPCR signaling and receptor sensitivity.

Discovery and status: The GRK6 ARE has been described in molecular studies using reporter assays and RNA-binding protein experiments as part of the broader field of post-transcriptional regulation of GRK genes. See also GRK family, AU-rich element, mRNA stability.