Reticulons (RTNs) are a group of membrane proteins localized on the ER and known to regulate ER structure and functions. Several studies have suggested that RTNs are involved in different important cellular functions such as changes in calcium homeostasis, ER-stress-mediated cell death, and autophagy. RTNs have been demonstrated to exert a cancer specific proapoptotic function via the interaction or the modulation of specific proteins. Reticulons have also been implicated in different signaling pathways which are at the basis of the pathogenesis of several neurodegenerative diseases. In this paper we discuss the accumulating evidence identifying RTN-1C protein as a promising target in the treatment of different pathologies such as cancer or neurodegenerative disorders. 1. Introduction Neuronal death occurs by necrosis or apoptosis, which differ morphologically and biochemically. Necrosis is the result of extreme perturbation of the cellular environment, as occurs in ischemic insults or trauma. In contrast apoptosis is dependent on intracellular pathways which lead to cellular commitment to a defined series of steps leading to cell suicide. Apoptosis is an important mechanism in normal cell turnover and in growth and development, as well as in aging. Alteration of this machinery results in the evolution of cancer and autoimmune or degenerative diseases. The process of neuronal apoptosis involves two principal pathways that converge on activation of caspases: the cell surface death receptor pathway and the mitochondrial pathway [1]. However, a role in the initiation of neuronal apoptotic cell death by other organelles, including endoplasmic reticulum (ER), is now well established [2]. Disruption of ER homeostasis interferes with protein folding and leads to the accumulation of unfolded and misfolded proteins in the ER lumen. This condition, designated “ER stress,” can be triggered by stimuli that perturb ER function, including depletion of Ca2+ stores, reduction of disulphide bonds, overexpression of certain proteins, and nutrient/glucose deprivation [3]. To maintain homeostasis, the ER mounts an unfolded protein response (UPR), as a self-protective mechanism, which results in transcriptional induction of UPR genes, translational attenuation of global protein synthesis, and ER-associated protein degradation (ERAD) [3]. However, if these adaptive responses are not sufficient to relieve the ER stress, the cell dies through apoptosis [3]. Interestingly, prolonged ER stress is at the basis of the pathogenesis of several neuronal disorders [4, 5]. In fact,
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