Molecular cloning of two rat GRK6 splice variants.

Details

Serval ID
serval:BIB_AD0903937922
Type
Article: article from journal or magazin.
Collection
Publications
Title
Molecular cloning of two rat GRK6 splice variants.
Journal
American Journal of Physiology. Cell Physiology
Author(s)
Firsov D., Elalouf J.M.
ISSN
0363-6143
ISSN-L
0363-6143
Publication state
Published
Issued date
1997
Volume
273
Number
3 Pt 1
Pages
C953-C961
Language
english
Abstract
Desensitization of G protein-coupled receptors is frequently triggered by G protein-coupled receptor kinases (GRKs) that preferentially phosphorylate agonist-occupied receptors. In this study, two GRK6 splice variants were cloned from the rat kidney. One isoform (GRK6a) encodes a 576-amino acid protein that is virtually identical (98% identity) to human GRK6. The second isoform is similar except for a 2-base pair insert that constitutes part of an intron interrupting the 3'-end coding region. This new isoform (GRK6b, 589 amino acids) has therefore a specific COOH-terminal region. A reverse transcription-polymerase chain reaction assay designed to discriminate GRK6 splice variants demonstrated that GRK6b mRNA is widely distributed and expressed at much higher levels than GRK6a mRNA in most peripheral tissues. In contrast, GRK6a predominates in brain. Functional studies, performed with cytosol extracts from transfected Chinese hamster ovary cells, indicated that GRK6a and GRK6b both phosphorylate light-activated rhodopsin as well as a synthetic peptide. The identification of GRK6b extends the family of GRKs. Further studies will be required to establish the tissue and subcellular distribution of this protein and to delineate its physiological role.
Keywords
Alternative Splicing, Amino Acid Sequence, Animals, Base Sequence, CHO Cells, Cloning, Molecular, Cricetinae, G-Protein-Coupled Receptor Kinase 4, G-Protein-Coupled Receptor Kinase 5, G-Protein-Coupled Receptor Kinases, GTP-Binding Proteins/metabolism, Genetic Variation, Humans, Kidney/metabolism, Male, Molecular Sequence Data, Organ Specificity, Polymerase Chain Reaction, Protein-Serine-Threonine Kinases, Rats, Receptor Protein-Tyrosine Kinases/biosynthesis, Receptor Protein-Tyrosine Kinases/chemistry, Recombinant Proteins/biosynthesis, Recombinant Proteins/chemistry, Sequence Alignment, Sequence Homology, Amino Acid, Transfection
Pubmed
Web of science
Create date
24/01/2008 12:32
Last modification date
20/08/2019 15:17
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