Â“The identification of AR was immediately followed by the recognition that the receptor is a phosphoprotein and that phosphorylated AR is localized to the nucleus upon ligand stimulation. More extensive studies indicated that AR is synthesized as a single 110 kDa protein that is rapidly converted into a 112 kDa phosphoprotein in the absence of hormone, with constitutive phosphorylation at two Pro-directed serines (Ser650 and Ser94); and that androgens can further induce the expression of a 114 kDa isoform which is phosphorylated at additional residues and associated with AR nuclear activities. The distribution of these three isoforms can be attributed to the NTD, in particular the length of the outstanding polyglutamine (poly-Q) stretch and the phosphorylation at two adjacent Pro-directed serines (Ser81 and Ser94)Â”.
Journal of Steroids & Hormonal Science is an official journal of OMICS group international that publishes the articles related to androgen receptor phosphorylation. The peer review followed by Journal of Steroids & Hormonal Science is single blind peer review process. This sort of review process will enable the authors to make the required manipulations and improve the quality of their work as per the expertÂ’s opinion. The journal is publishing all the articles related to androgen receptors under a special issue entitled Androgen Receptors.
Last date updated on July, 2014