Polycystin 2 regulates mitochondrial Ca(2+) signaling, bioenergetics, and dynamics through mitofusin 2. Kuo, I. Y., Brill, A. L., Lemos, F. O., Jiang, J. Y., Falcone, J. L., Kimmerling, E. P., Cai, Y., Dong, K., Kaplan, D. L., Wallace, D. P., Hofer, A. M., & Ehrlich, B. E. Science signaling, May, 2019. doi abstract bibtex Mitochondria and the endoplasmic reticulum (ER) have an intimate functional relationship due to tethering proteins that bring their membranes in close (~30 nm) apposition. One function of this interorganellar junction is to increase the efficiency of Ca(2+) transfer into mitochondria, thus stimulating mitochondrial respiration. Here, we showed that the ER cation-permeant channel polycystin 2 (PC2) functions to reduce mitochondria-ER contacts. In cell culture models, PC2 knockdown led to a 50% increase in mitofusin 2 (MFN2) expression, an outer mitochondrial membrane GTPase. Live-cell super-resolution and electron microscopy analyses revealed enhanced MFN2-dependent tethering between the ER and mitochondria in PC2 knockdown cells. PC2 knockdown also led to increased
@article{kuo_polycystin_2019,
title = {Polycystin 2 regulates mitochondrial {Ca}(2+) signaling, bioenergetics, and dynamics through mitofusin 2.},
volume = {12},
copyright = {Copyright (c) 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.},
issn = {1937-9145 1945-0877},
doi = {10.1126/scisignal.aat7397},
abstract = {Mitochondria and the endoplasmic reticulum (ER) have an intimate functional relationship due to tethering proteins that bring their membranes in close ({\textasciitilde}30 nm) apposition. One function of this interorganellar junction is to increase the efficiency of Ca(2+) transfer into mitochondria, thus stimulating mitochondrial respiration. Here, we showed that the ER cation-permeant channel polycystin 2 (PC2) functions to reduce mitochondria-ER contacts. In cell culture models, PC2 knockdown led to a 50\% increase in mitofusin 2 (MFN2) expression, an outer mitochondrial membrane GTPase. Live-cell super-resolution and electron microscopy analyses revealed enhanced MFN2-dependent tethering between the ER and mitochondria in PC2 knockdown cells. PC2 knockdown also led to increased},
language = {eng},
number = {580},
journal = {Science signaling},
author = {Kuo, Ivana Y. and Brill, Allison L. and Lemos, Fernanda O. and Jiang, Jason Y. and Falcone, Jeffrey L. and Kimmerling, Erica P. and Cai, Yiqiang and Dong, Ke and Kaplan, David L. and Wallace, Darren P. and Hofer, Aldebaran M. and Ehrlich, Barbara E.},
month = may,
year = {2019},
pmid = {31064883},
}
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One function of this interorganellar junction is to increase the efficiency of Ca(2+) transfer into mitochondria, thus stimulating mitochondrial respiration. Here, we showed that the ER cation-permeant channel polycystin 2 (PC2) functions to reduce mitochondria-ER contacts. In cell culture models, PC2 knockdown led to a 50% increase in mitofusin 2 (MFN2) expression, an outer mitochondrial membrane GTPase. Live-cell super-resolution and electron microscopy analyses revealed enhanced MFN2-dependent tethering between the ER and mitochondria in PC2 knockdown cells. 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No claim to original U.S. Government Works.},\n\tissn = {1937-9145 1945-0877},\n\tdoi = {10.1126/scisignal.aat7397},\n\tabstract = {Mitochondria and the endoplasmic reticulum (ER) have an intimate functional relationship due to tethering proteins that bring their membranes in close ({\\textasciitilde}30 nm) apposition. One function of this interorganellar junction is to increase the efficiency of Ca(2+) transfer into mitochondria, thus stimulating mitochondrial respiration. Here, we showed that the ER cation-permeant channel polycystin 2 (PC2) functions to reduce mitochondria-ER contacts. In cell culture models, PC2 knockdown led to a 50\\% increase in mitofusin 2 (MFN2) expression, an outer mitochondrial membrane GTPase. Live-cell super-resolution and electron microscopy analyses revealed enhanced MFN2-dependent tethering between the ER and mitochondria in PC2 knockdown cells. 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