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Título: Redox dependence of endoplasmic reticulum (ER) Ca2+ signaling
Fecha de publicación: 2014
Editorial: F. Hernández y Juan F. Madrid. Universidad de Murcia: Departamento de Biología Celular e Histología
Cita bibliográfica: Histology and Histopathology, vol. 29, nº 5, (2014)
ISSN: 1699-5848
0213-3911
Materias relacionadas: CDU::6 - Ciencias aplicadas::61 - Medicina
Palabras clave: Endoplasmic Reticulum
Mitochondria
Mitochondria-associated membrane
Resumen: The endoplasmic reticulum (ER) is a multifunctional organelle that accommodates a large array of functions. Recent publications have shown that many of these functions are influenced by the ongoing oxidative folding of secretory and membrane proteins. Conversely, successful ER protein folding critically depends on the cellular redox state, but also the availability of Ca2+. These findings suggest the existence of regulatory mechanisms that steer ER Ca2+ homeostasis according to the cellular redox state. Indeed, accumulating evidence demonstrates that ER Ca2+ uptake and release by sarco-endoplasmic reticulum Ca2+ transport ATPases (SERCAs), stromal interaction molecule 1 (STIM1), Orai1, inositol 1,4,5-trisphosphate (IP3) receptors (IP3Rs) and ryanodine receptors (RyR) depends on redox modifications of these channels and pumps. In addition, ER chaperones and oxidoreductases moonlight as regulators of ER Ca2+ channels and pumps. Discrete redox conditions of channels, pumps and oxidoreductases exist that allow for opening and closing. Through these functions, redox regulation of ER Ca2+ influences signaling mechanisms governing cell growth and migration, apoptosis and mitochondrial energy production. Therefore, pharmacological intervention based on ER redox or on ER redox-sensitive chaperones and oxidoreductases is a promising strategy to influence all metabolic syndromes including cancer and neurodegeneration.
Autor/es principal/es: Raturi, Arun
Ortiz-Sandoval, Carolina
Simmen, Thomas
URI: http://hdl.handle.net/10201/68639
Tipo de documento: info:eu-repo/semantics/article
Número páginas / Extensión: 10
Derechos: info:eu-repo/semantics/openAccess
Aparece en las colecciones:Vol.29, nº 5 (2014)

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