For many decades, mitochondrion has been traditionally considered as the powerhouse of the cell. In addition to energy production, this intracellular organelle plays an important role in regulating programmed cell death (apoptosis), calcium homeostasis, thermogenesis, and stress response. All of these pleiotropic functions are mostly mediated by signaling pathways that pass through the mitochondrial membranes and matrix. Not surprisingly, members of the nuclear receptor family of transcription factors have been detected in mitochondrion following hormone-induced activation (1). A similar phenomenon seems to occur with members of the mammalian/mechanistic target of rapamycin complexes 1 and 2 (mTORC1 and mTORC2), indicating that subcellular compartmentalization of signaling proteins matters a lot (2). mTORC1 and mTORC2 are 2 distinct protein complexes that both consist of an intracellular serine-threonine kinase, named mTOR, which is activated by the PI3K-Akt pathway. mTORC1 is activated by several growth factors, including the epidermal growth factor (EGF) and the insulin-like growth factor 1/2, and plays a fundamental role in protein and lipid biosynthesis, ribosome biogenesis, as well as in the aging of organisms (2). On the other hand, mTORC2 is also activated by growth factors and participates in cell survival, cytoskeletal organization, metabolism, and cell migration (2). The protein members of both mTORC complexes have been detected in many subcellular compartments, including cytoplasm and nucleus, as well as in lysosomes, peroxisomes, and the Golgi apparatus. However, the mitochondrial localization of these proteins had not been clearly documented until recently (2). Independently of subcellular compartmentalization, Su et al demonstrated that the mTOR signaling cascade was overexpressed in the zona glomerulosa of patients with aldosterone-producing adenomas, indicating that mTOR inhibitors might be used to treat hyperaldosteronism (3). Soon after, De Martino and collaborators investigated the expression of the mTOR pathway in normal adrenal tissues, adrenal hyperplasia, adrenocortical adenomas, and adrenocortical carcinomas (4). They also studied the effects of sirolimus, a well-known mTOR inhibitor, on survival and cortisol secretion in a number of primary cultures of human adrenocortical tumors. Interestingly, the authors found that the mTOR pathway was activated in a subset of adrenocortical tumors and that certain cases of adrenocortical carcinomas were sirolimus-responsive (4), indicating that mTOR inhibitors might be further used to suppress adrenal steroid production. Furthermore, although angiotensin II (Ang II) had been shown to activate the mTOR pathway in esophageal carcinoma (2), a similar Ang II-induced activation of the mTOR signaling cascade had not been reported in adrenal cortex.