Insulin regulates protein kinase CbetaII expression through enhanced exon inclusion in L6 skeletal muscle cells. A novel mechanism of insulin- and insulin-like growth factor-i-induced 5' splice site selection.

The Journal of Biological Chemistry
C E ChalfantDenise R Cooper

Abstract

The protein kinase Cbeta (PKCbeta) gene encodes two isoforms, PKCbetaI and PKCbetaII, as a result of alternative splicing. The unique mechanism that underlies insulin-induced alternative splicing of PKCbeta pre-mRNA was examined in L6 myotubes. Mature PKCbetaII mRNA and protein rapidly increased >3-fold following acute insulin treatment, while PKCbetaI mRNA and protein levels remained unchanged. Mature PKCbetaII mRNA resulted from inclusion of the PKCbetaII-specific exon rather than from selection of an alternative polyadenylation site. Increased PKCbetaII expression was also not likely accounted for by transcriptional activation of the gene or increased stabilization of the PKCbetaII mRNA, and suggest that PKCbetaII expression is regulated primarily at the level of alternative splicing. Insulin effects on exon inclusion were observed as early as 15 min after insulin treatment; by 20 min, a new 5'-splice site variant of PKCbetaII was also observed. After 30 min, the longer 5'-splice site variant became the predominate species through activation of a downstream 5' splice site. Similar results were obtained using IGF-I. Although the role of this new PKCbetaII mRNA species is presently unknown, inclusion of either PKCbetaII-specif...Continue Reading

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Citations

Dec 5, 2003·Biochimica Et Biophysica Acta·Rebeca Martínez-ContrerasJesús Valdés
Mar 23, 2000·Theriogenology·J D Murray
Mar 2, 2006·Genome Biology·Alistair R R ForrestSean M Grimmond
Jun 4, 2004·Human Molecular Genetics·Ilona RafalskaStefan Stamm
Oct 31, 2002·The Journal of Biological Chemistry·Niketa A PatelDenise R Cooper
Aug 17, 2004·The Biochemical Journal·Remko R BoschC G J Fred Sweep
Aug 13, 2005·Cellular Signalling·Miriam Horovitz-FriedSanford R Sampson

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