Identification and characterization of alternatively spliced murine Rgs11 isoforms: genomic structure and gene analysis
Giudice, A.; Gould, J.A.; Freeman, K.B.; Rastan, S.; Hertzog, P.; Kola, I.; Iannello, R.C.
Cytogenetics and Cell Genetics 94(3-4): 216-224
ISSN/ISBN: 0301-0171 PMID: 11856884 DOI: 10.1159/000048819
The RGS proteins comprise a large family of proteins which were recently identified as negative Regulators of G-protein Signaling. They have been shown to act as GTPase Activating Proteins (GAPs) towards the G(alpha) subunits of heterotrimeric G-proteins. In addition to this GAP activity, which has been shown to occur through the RGS domain, RGS proteins are likely to possess other functions due to the existence of other domains in these molecules (De Vries and Farquhar, 1999; Hepler, 1999). Here, we report the molecular characterization of the murine Rgs11 gene. The gene encodes a protein with high homology to human RGS11 (79.9%), containing conserved DEP (Dishevelled/EGL-10/Pleckstrin) and GGL (G protein gamma-like) domains. The gene is comprised of at least 13 exons, spanning 8-9 kb. Spliced transcript variants were identified which are co-expressed with 5A3, a transcript that contains the largest ORF. Expression of mouse Rgs11 was found to be restricted to specific tissues with a unique pattern of expression observed in brain.