Lanz et al. (1999) found that SRA was selective for steroid hormone receptors and mediated transactivation via their N-terminal activation function. The authors provided functional and mechanistic evidence that SRA acts as an RNA transcript; transfected SRA, unlike other steroid receptor coregulators, functioned in the presence of cycloheximide, and SRA mutants containing multiple translational stop signals retained their ability to activate steroid receptor-dependent gene expression. Biochemical fractionation showed that SRA exists in distinct ribonucleoprotein complexes, one of which contains steroid receptor coactivator-1 (602691). Lanz et al. (1999) suggested that SRA may act to confer functional specificity upon multiprotein complexes recruited by liganded receptors during transcriptional activation.
STEROIDS is an international research journal devoted to studies on all chemical and biological aspects of steroidal moieties. The journal focuses on both experimental and theoretical studies on the biology, chemistry, biosynthesis, metabolism, molecular biology, physiology and pharmacology of steroids and other molecules that target or regulate steroid receptors. Manuscripts presenting clinical research related to steroids, steroid drug development, comparative endocrinology of steroid hormones, investigations on the mechanism of steroid action and steroid chemistry are all appropriate for submission for peer review. STEROIDS publishes both original research and timely reviews. For details concerning the preparation of manuscripts see Instructions to Authors, which is published in each issue of the journal.
Sex hormone-binding globulin (SHBG) is thought to mainly function as a transporter and reservoir for the estradiol and testosterone sex hormones. However it has also been demonstrated that SHBG can bind to a cell surface receptor (SHBG-R). The SHBG-R has not been completely characterized. A subset of steroids are able to bind to the SHBG/SHBG-R complex resulting in an activation of adenylyl cyclase and synthesis of the cAMP second messenger.  Hence the SHBG/SHBG-R complex appears to act as a transmembrane steroid receptor that is capable of transmitting signals to the interior of cells.