Previous structure prediction studies of LOX-PP using DISOPRED, GlobPlot and DisProt, and circular dichroism analysis have indicated that the propeptide assembles as an intrinsically disordered protein, suggesting that LOX-PP does not have defined domains. Here, we identified the CIN85 binding motif at aa 111 to 119. Thus, multiple proteins, mediating various biological activities, are able to interact with various regions of LOX-PP and these associations appear to regulate the activities of these interacting proteins. In addition, a single-nucleotide polymorphism G473A resulting in an Arg158Gln mutation has been shown to be associated with increased risk of estrogen receptor -alpha-negative invasive breast cancer in AfricanAmerican women, and subsequently with increased risk of breast cancer and ovarian cancer in Chinese women, and with gastric cancer. It is reasonable to assume that the SNP regulates the function of LOX-PP and might affect its interaction with an associating protein. In summary, here LOX-PP is shown to interact directly with CIN85 via 
an atypical ligand thereby reducing interaction of CIN85 with c-Cbl, and reducing the invasive phenotype of breast cancer cells. Steroid hormones, which are synthesized most prominently in the adrenal gland and gonads, play important roles in the regulation of carbohydrate, lipid and Tofacitinib protein metabolism and immune function, salt and water balance and blood pressure regulation and maintenance of secondary sex characteristics, reproductive functions and muscle and bone growth. Steroidogenesis or biosynthesis of steroid hormones represents a complex multistep and multienzymes process by which precursor cholesterol is converted to pregnenolone and subsequently metabolized into other biologically active steroids in a tissue specific manner. This process can be broadly divided into five major steps: 1) acquisition of cholesterol from exogenous and endogenous sources for storage in the form of cholesterol esters in lipid droplets, 2) mobilization of cholesterol from lipid droplet stored CEs, 3) transport of cholesterol to and from the outer mitochondrial membrane to the inner mitochondrial membrane, where cytochrome P450 side chain cleavage enzyme is localized, 4) P450scc catalyzed cleavage of a 6-carbon unit from the cholesterol side chain producing pregnenolone, the common precursor – for the synthesis of all of the other steroid hormones, and 5) efflux of pregnenolone from the mitochondria to the endoplasmic reticulum, where it is converted by ER enzymes into intermediate precursors, which further shuttle between mitochondria and ER for the tissue specific production of progestins, estrogens, androgens, glucocorticoids or mineralocorticoids. Adrenal and gonadal steroidogenesis is predominantly controlled by trophic hormones and is subject to both acute, and chronic regulation. Acute steroid synthesis that occurs over minutes in response to trophic hormone stimulation is controlled at the level of cholesterol delivery to the IMM for the first enzymatic step in the pathway, the conversion of cholesterol to pregnenolone by the P450scc. This rate limiting step, i.e., cholesterol transfer from OMM to IMM, is dependent upon the trophic hormone stimulated rapid induction of the steroidogenic acute regulatory protein. Although, the exact mechanism of action of StAR protein in mediating the cholesterol transfer across the mitochondrial membrane is not known, increasing evidence now suggests that StAR works in concert with several other SAR131675 VEGFR/PDGFR inhibitor proteins including peripheral benzodiazepine receptor /18-kDa transporter protein, voltage-dependent anion channel 1, phosphate carrier protein, cAMP-dependent protein kinase 1a and TSPO-associated acyl-coenzyme A binding domain containing 3 protein by forming a protein complex on the OMM.