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Identification of Novel Isoforms of Regulator of G‐Protein Signaling 6 (RGS6)
Author(s) -
Yang Jianqi,
Ibeawuchi StellaRita,
Huang Jie,
Stewart Adele,
Chen ChingKang Jason,
Fisher Rory A
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.587.2
Subject(s) - gene isoform , biology , knockout mouse , regulator of g protein signaling , microbiology and biotechnology , hek 293 cells , alternative splicing , receptor , genetics , gene , g protein , gtpase activating protein
RGS6 is a member of the RGS family of proteins that play critical roles in attenuating G protein‐coupled receptor signaling. In addition to a hallmark RGS domain that mediates inactivation of Gi/o subunits, certain RGS6 isoforms possess DEP and GGL domains implicated in their membrane anchoring and binding to Gβ5, respectively. Half of the 36 splice variants of RGS6 we identified in human brain encode DEP domain‐containing long isoforms of RGS6 (RGS6L). In this study, we generated a highly specific antibody against RGS6L isoforms. Using this antibody to evaluate expression of RGS6L in mouse tissues, we identified an immuno‐reactive band corresponding to the predicted molecular weight of RGS6L isoforms in numerous tissues including brain, cerebellum and spinal cord. Moreover, additional unique bands were present in brain, liver and kidney. The size of these other immuno‐reactive proteins could not be accounted for by any known RGS6L transcript. Both the predicted and unique RGS6L immuno‐reactive bands were present in lysates derived from wild‐type but not RGS6 knockout mice, suggesting that the unique bands represent novel isoforms of RGS6L. This is the first evidence that multiple and novel isoforms of RGS6L are present in various mouse tissues. The biological function of the novel isoforms of RGS6L are under investigation. (Supported by NIH GM075033, AHA 0750057Z).