Journal
MOLECULAR CELL
Volume 39, Issue 1, Pages 121-132Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2010.06.029
Keywords
-
Categories
Funding
- Thomas Jefferson Pilot Research Award
- NIH [DK051526, RC2AA019416]
- Eunice Kennedy Shriver National Institute of Child Health and Human Development of the National Institutes of Health
- Hungarian Scientific Research Fund [OTKA NF-68563]
- Medical Research Council of Hungary [ETT 494/2009]
Ask authors/readers for more resources
The ER-mitochondrial junction provides a local calcium signaling domain that is critical for both matching energy production with demand and the control of apoptosis. Here, we visualize ER-mitochondrial contact sites and monitor the localized [Ca2+] changes ([Ca2+](ER-mt)) using drug-inducible fluorescent interorganelle linkers. We show that all mitochondria have contacts with the ER, but plasma membrane (PM)-mitochondrial contacts are less frequent because of interleaving ER stacks in both RBL-2H3 and H9c2 cells. Single mitochondria display discrete patches of ER contacts and show heterogeneity in the ER-mitochondrial Ca2+ transfer. Pericam-tagged linkers revealed IP3-induced ([Ca2+](ER-mt)) signals that exceeded 9 mu M and endured buffering bulk cytoplasmic [Ca2+] increases. Altering linker length to modify the space available for the Ca2+ transfer machinery had a biphasic effect on [Ca2+](ER-mt) signals. These studies provide direct evidence for the existence of high-Ca2+ microdomains between the ER and mitochondria and suggest an optimal gap width for efficient Ca2+ transfer.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available