Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing

Caroline A Rivers, A Levy, J Hancock, SL Lightman, MR Norman

Research output: Contribution to journalArticle (Academic Journal)peer-review

110 Citations (Scopus)

Abstract

When the human glucocorticoid receptor (GR) was first sequenced, a predominant form (GR) and a minor variant (GRß) were identified (1). In the present communication, we describe a new variant of the glucocorticoid receptor (GR) in which, as a result of alternative splicing, three bases are retained from the intron separating exons 3 and 4. These three bases code for an additional amino acid (arginine) in the DNA binding domain of the receptor. Insertion of arginine at this site has previously been shown to decrease transcriptional activation by the GR to 48% that of GR (2). Analysis of cDNA from different tissues shows that the novel form is widely expressed at a relatively high level (between 3.8 and 8.7% of total GR).
Translated title of the contributionInsertion of an Amino Acid in the DNA-Binding Domain of the Glucocorticoid Receptor as a Result of Alternative Splicing
Original languageEnglish
Pages (from-to)4283 - 4286
Number of pages4
JournalJournal of Clinical Endocrinology and Metabolism
Volume84, 11
Publication statusPublished - 1999

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