{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T06:53:05Z","timestamp":1768978385957,"version":"3.49.0"},"reference-count":29,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,1,13]],"date-time":"2005-01-13T00:00:00Z","timestamp":1105574400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2005,2]]},"abstract":"<jats:p>Regulator of G protein signaling (RGS) proteins act as GTPase\u2010activating proteins (GAPs) for G\u03b1 subunits and negatively regulate G protein\u2010coupled receptor signaling. Using RGS5 gene\u2010specific RT\u2010PCR, we have identified a novel alternative splicing variant of RGS5 mRNA in human ocular tissues. The alternative splicing of RGS5 mRNA occurred at position +44 (GenBank <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"DDBJ\/EMBL\/GenBank\" xlink:href=\"NM_003617\">NM_003617<\/jats:ext-link>), spliced out 174\u2003bp (+44 to +218\u2003bp) of the coding region, and encoded an RGS5s protein with a 108 amino acid N\u2010terminal deletion. This study is the first to document alternative splicing of an <jats:italic>RGS5<\/jats:italic> gene. We therefore studied RGS5 and RGS5s mRNA distribution in human tissues. In the eye, RGS5s was found to be highly expressed in the ciliary body and trabecular meshwork. It was also expressed in the kidney, brain, spleen, skeletal muscle and small intestine, but was not detectable in the liver, lung, heart. RGS5s was not found in monkey and rat ocular tissues, indicating species specificity for the eye. Comparing the recombinant RGS5 and RGS5s expression in HEK293\/EBNA cells, RGS5s was present almost exclusively in the cytosolic fraction, whereas RGS5 was present in both membrane and cytosolic fractions. The data suggest that the N\u2010terminal of RGS5 may be important for protein translocation to the cell membrane. Both RGS5 and RGS5s antagonized the rapid phosphorylation of p44\/42 MAP kinase induced by G\u03b1i coupled cannibinoid receptor\u20101 activation. RGS5, but not RGS5s, inhibited the Ca<jats:sup>2+<\/jats:sup> signaling initiated by activation of G\u03b1q coupled angiotensin II receptors (AT1) and prostaglandin FP receptors. Cotransfection of RGS5s with RGS5 resulted in the blockade of RGS5 actions with respect to inhibition of the signal transduction initiated by activation of both AT1 and FP receptor, suggesting that RGS5s may contain functional domains that compete with RGS5 in the regulation of the G\u03b1q coupled AT1 and FP receptors. The unique expression pattern, cellular localization and functions of RGS5s suggest that RGS5s may play a critical role in the regulation of intracellular signaling pathways.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2004.04516.x","type":"journal-article","created":{"date-parts":[[2005,1,21]],"date-time":"2005-01-21T11:49:27Z","timestamp":1106308167000},"page":"791-799","source":"Crossref","is-referenced-by-count":22,"title":["Identification of a novel alternative splicing variant of RGS5 mRNA in human ocular tissues"],"prefix":"10.1111","volume":"272","author":[{"given":"Yanbin","family":"Liang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chen","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Victor M.","family":"Guzman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"William 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