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. 2017 May 29;4:38. doi: 10.3389/fcvm.2017.00038

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Copyright © 2017 Cesselli, Aleksova, Sponga, Cervellin, Di Loreto, Tell and Beltrami.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Crosstalk between endoplasmic reticulum (ER) and mitochondria. In conditions of ER stress, PKR-like ER kinase (PERK) phosphorylates eIF2α which, in turn, reduces protein translation and promotes the expression of the transcription factor ATF4. This latter, subsequently promotes the transcription of Parkin, a protein that stimulates mitochondrial fission, mitochondrial autophagy, and the transfer of calcium from the ER to the mitochondria at the mitochondria-associated membranes (MAM). Furthermore, a kinase independent function of PERK promotes the tethering of the ER to mitochondria at the MAM and the oxidation of cardiolipin.