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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.
The C-terminal AF-2 transactivation domain is highly conserved within the nuclear receptor superfamily 31 and is recognized by various transcriptional coactivators. 32 , 33 AF-2 is localized to the most C-terminal end of the E domain. A third transactivation domain called AF-2a or tau2 has been localized to the N-terminal region of the LBD of ERα 31 and GR. 34 Deletion experiments revealed a role for AF-2a and the DBD in targeting rat GR to the nuclear matrix, 35 an interconnected ribonuclear-protein network within the nucleus that is thought to play an important roles in transcription of active genes by stabilizing the assembly of the transcriptional machinery. 36