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- W1557524937 abstract "G protein-coupled receptor kinases (GRK), such as the beta-adrenergic receptor kinase (beta ARK) and rhodopsin kinase, specifically phosphorylate the activated form of G protein-coupled receptors. To identify additional members of the GRK family, we screened a human heart cDNA library by low stringency hybridization using the catalytic domains of two beta ARK isoforms. Here we report the isolation of a cDNA that encodes a 576-amino-acid protein kinase, termed GRK6, that has significant homology with GRK5 (70.1% amino acid identity), IT11 (68.5%), rhodopsin kinase (47.1%), and beta ARK (37.4%). RNA blot analysis of GRK6 with selected human tissues reveals two distinct mRNAs of 3 and 2.4 kilobases with a distribution very similar to that of beta ARK (i.e. brain, skeletal muscle > pancreas > heart, lung, kidney, placenta > liver). GRK6, overexpressed in Sf9 insect cells using the baculovirus system, was able to phosphorylate both the beta 2-adrenergic receptor and rhodopsin in a stimulus-dependent fashion, although it was significantly less active then beta ARK on these substrates. These data extend the family of GRKs and suggest that GRK6 may have a substrate specificity quite distinct from beta ARK and rhodopsin kinase." @default.
- W1557524937 created "2016-06-24" @default.
- W1557524937 creator A5035941891 @default.
- W1557524937 creator A5056161061 @default.
- W1557524937 date "1993-09-01" @default.
- W1557524937 modified "2023-10-13" @default.
- W1557524937 title "Molecular cloning and expression of GRK6. A new member of the G protein-coupled receptor kinase family." @default.
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- W1557524937 doi "https://doi.org/10.1016/s0021-9258(19)36546-9" @default.
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