期刊
SCIENCE
卷 358, 期 6363, 页码 623-629出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan6009
关键词
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资金
- NIH [NS089456, GM122589, GM45735, GM030518, S10 RR029300, 1S10OD016167]
- Fondation Roger De Spoelberch
- International Research Fellowship of the Japan Society for the Promotion of Science
- JST/PRESTO [JPMJPR16F7]
- NIH (National Cancer Institute) [P30 CA013696]
- Shared Instrumentation Grant [1S10OD14584]
- Simons Foundation [349247]
- New York Office of Science Technology and Academic Research (NYSTAR)
- NIH Intellectual and Developmental Disabilities Research Center grant from the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD) [U54 HD083092]
- [S10OD012351]
- [S10OD021764]
Interfaces between organelles are emerging as critical platforms for many biological responses in eukaryotic cells. In yeast, the ERMES complex is an endoplasmic reticulum (ER)-mitochondria tether composed of four proteins, three of which contain a SMP (synaptotagmin-like mitochondrial-lipid binding protein) domain. No functional ortholog for any ERMES protein has been identified in metazoans. Here, we identified PDZD8 as an ER protein present at ER-mitochondria contacts. The SMP domain of PDZD8 is functionally orthologous to the SMP domain found in yeast Mmm1. PDZD8 was necessary for the formation of ER-mitochondria contacts in mammalian cells. In neurons, PDZD8 was required for calcium ion (Ca2+) uptake by mitochondria after synaptically induced Ca2+-release from ER and thereby regulated cytoplasmic Ca2+ dynamics. Thus, PDZD8 represents a critical ER-mitochondria tethering protein in metazoans. We suggest that ER-mitochondria coupling is involved in the regulation of dendritic Ca2+ dynamics in mammalian neurons.
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