Ilacqua Nicolò, Sánchez-Álvarez Miguel, Bachmann Magdalena, Costiniti Veronica, Del Pozo Miguel A, Giacomello Marta
Department of Biology, University of Padova, Padova, Italy.
Mechanoadaptation and Caveolae Biology Lab, Cell and Developmental Biology Area, Centro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.
Front Cell Dev Biol. 2017 Dec 12;5:107. doi: 10.3389/fcell.2017.00107. eCollection 2017.
Mitochondria-endoplasmic reticulum (ER) contacts (MERCs) are sites at which the outer mitochondria membrane and the Endoplasmic Reticulum surface run in parallel at a constant distance. The juxtaposition between these organelles determines several intracellular processes such as to name a few, Ca and lipid homeostasis or autophagy. These specific tasks can be exploited thanks to the enrichment (or re-localization) of dedicated proteins at these interfaces. Recent proteomic studies highlight the tissue specific composition of MERCs, but the overall mechanisms that control MERCs plasticity remains unclear. Understanding how proteins are targeted at these sites seems pivotal to clarify such contextual function of MERCs. This review aims to summarize the current knowledge on protein localization at MERCs and the possible contribution of the mislocalization of MERCs components to human disorders.
线粒体-内质网接触(MERC)是线粒体外膜与内质网表面以恒定距离平行排列的位点。这些细胞器之间的并置决定了几个细胞内过程,比如钙和脂质稳态或自噬等。由于这些界面处存在专门蛋白质的富集(或重新定位),这些特定任务得以实现。最近的蛋白质组学研究突出了MERC的组织特异性组成,但控制MERC可塑性的整体机制仍不清楚。了解蛋白质如何靶向这些位点似乎对于阐明MERC的这种背景功能至关重要。本综述旨在总结目前关于MERC处蛋白质定位的知识以及MERC组分定位错误对人类疾病可能产生的影响。