Steroid receptors are homodimers of zinc-finger proteins that reside within the nucleus (except for the glucocorticoid receptor which resides in the cytosol until it binds its ligand). Link to stereoscopic view of the glucocorticoid receptor bound to the promoter sequence of DNA.
In either case, binding triggers an allosteric change in the protein which, in turn, triggers the formation of a "second messenger" within the cell.
These are transmembrane proteins that wind 7 times back and forth through the plasma membrane.
Frizzled receptors, like GPCRs, are transmembrane proteins that wind 7 times back and forth through the plasma membrane. In mammals, when there is no hedgehog protein present, the patched receptors bind a second transmembrane protein called smoothened (Smo). Many of these other proteins are also tyrosine kinases (the human genome encodes 90 different tyrosine kinases) and in this way a cascade of expanding phosphorylations occurs within the cytosol. In May 2003, the US FDA approved a proteasome inhibitor, called bortezomib (Velcade®) for treatment of multiple myeloma, a cancer of plasma cells. T cells use a transmembrane dimeric protein as a receptor for a particular combination of an antigen fragment nestled in the cleft [View] of a histocompatibility molecule. Androgen receptor nuclear translocation is facilitated by the f-actin cross-linking protein filamin.

Relative potency of testosterone and dihydrotestosterone in preventing atrophy and apoptosis in the prostate of the castrated rat. Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins.
D-Aspartic Acid (D-AA) is a non-essential amino acid which support increased testosterone levels.
The most common protein target for NO seems to be guanylyl cyclase, the enzyme that generates the second messenger cyclic GMP (cGMP).
It differs from many of the other signaling pathways discussed here in that the ligands as well as their receptors are transmembrane proteins embedded in the plasma membrane of cells. There are many of them and often several versions within a family (such as the serrate and delta protein families).
This molecule fits into the active site of the ABL protein preventing ATP from binding there. Instead of activating the T cell, this turns on genes that convert the cell into a suppressive regulatory T cell (Treg) instead — Link.
A cytoskeletal protein Filamin-A (FlnA) interacts with the hinge, DBD and LBD of AR, facilitating AR translocation to the nucleus.
The cytochrome P450 enzyme, 5α-reductase, which converts testosterone to DHT, is highly expressed within the prostate and genital tissues.

AF-2 is the principal protein-protein interaction surface used by nuclear receptors to recruit LxxLL-motif containing coactivators. ARA70 protein has been found to be overexpressed in high grade prostate carcinomas, prostate cancer cell lines and xenografts, [63] whereas ARA70 mRNA expression was found to be decreased in prostate tumor tissue, [64] increased in response to hormone deprivation [65] or unchanged between normal and prostate cancer in the same tissue. Numerous immunohis-tochemical studies have shown that AR protein is expressed at high levels (compared to levels in untreated tumors), in most cases of CRPC. However, activation of mitogen-activated protein kinase (MAPK) and phosphatidylinositol-3 kinase (PI3K) pathways can also occur depending on the cell type. Large-scale epidemiological studies have suggested a correlation between elevated serum levels of IGF-1 and low levels of IGFBP-3 (Insulin-like growth factor-binding protein 3 , a serum protein that regulates the binding of free IGF-1 to the IGF receptor), and increased risk of developing prostate cancer. Kinase signal cascades are rapidly transduced and mediated through protein-protein interactions.
The activity of Src on AR transactivation is modulated, at least in part through its binding partner and associated scaffold protein, receptor for activated protein kinase C-1 (RACK1) [127]. Treatment of C4-2 cells with the Src inhibitor, protein phosphatase-2 in androgen free conditions results in decreased AR activation of reporter activities and reduced recruitment of AR to the PSA enhancer region.

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