PerspectiveCell Biology

Mediating ER-mitochondrial cross-talk

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Science  03 Nov 2017:
Vol. 358, Issue 6363, pp. 591-592
DOI: 10.1126/science.aaq0141

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Cellular function and survival require the highly ordered subcellular localization of organelles. In particular, there is considerable interest in understanding the interconnectedness of the endoplasmic reticulum (ER) and mitochondria. The direct interaction of ER and mitochondrial membranes is referred to as tethering, typically defined as an interorganelle distance of less than 30 nm. Tethering has been implicated in numerous physiological processes, including lipid synthesis and transfer, coupling of Ca2+ transfer, autophagosome formation, inflammatory signaling, mitochondrial morphology, and mitochondrial DNA (mtDNA) synthesis and distribution (15). Although the functional relevance of ER-mitochondrial tethering is widely accepted, identification of the proteins that constitute these interconnected structures has remained elusive. On page 623 of this issue, Hirabayashi et al. (6) show that PDZ domain containing protein 8 (PDZD8) is required for the tethering of ER and mitochondrial membranes and is critical for Ca2+ transfer from ER to mitochondria.