Sigma-1 Receptor Chaperones at the ER- Mitochondrion Interface Regulate Ca2+ Signaling and Cell Survival
Teruo Hayashi,Tsung-Ping Su +1 more
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TLDR
The results reveal that the orchestrated ER chaperone machinery at MAM, by sensing ER Ca(2+) concentrations, regulates ER-mitochondrial interorganellar Ca( 2+) signaling and cell survival.About:
This article is published in Cell.The article was published on 2007-11-02 and is currently open access. It has received 1431 citations till now. The article focuses on the topics: Unfolded protein response & Endoplasmic reticulum.read more
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Physiology of Microglia
TL;DR: Current studies indicate that even in the normal brain, microglia have highly motile processes by which they scan their territorial domains, and microglial cells are considered the most susceptible sensors of brain pathology.
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Autophagosomes form at ER–mitochondria contact sites
Maho Hamasaki,Nobumichi Furuta,Atsushi Matsuda,Atsushi Matsuda,Akiko Nezu,Akitsugu Yamamoto,Naonobu Fujita,Hiroko Oomori,Takeshi Noda,Tokuko Haraguchi,Tokuko Haraguchi,Yasushi Hiraoka,Yasushi Hiraoka,Atsuo Amano,Tamotsu Yoshimori +14 more
TL;DR: It is shown that autophagosomes form at the ER–mitochondria contact site in mammalian cells, and new insight is provided into organelle biogenesis by demonstrating that the ER-resident SNARE protein syntaxin 17 (STX17) binds ATG14 and recruits it to the ER—mitochondia contact site.
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Mitochondria as sensors and regulators of calcium signalling
TL;DR: During the past two decades calcium (Ca2+) accumulation in energized mitochondria has emerged as a biological process of utmost physiological relevance, opening new perspectives for investigation and molecular intervention.
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An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Benoît Kornmann,Erin Currie,Sean R. Collins,Maya Schuldiner,Jodi Nunnari,Jonathan S. Weissman,Peter Walter +6 more
TL;DR: In this article, the authors identified the Mmm1/Mdm10/mdm12/mdr34 complex as a molecular tether between the endoplasmic reticulum (ER) and mitochondria.
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Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
TL;DR: The evidence linking calcium homeostasis to the regulation of apoptotic, and more recently autophagic cell death is reviewed, as well as the discussion of mitochondria as a critical, although not unique checkpoint, and the molecular and functional elucidation of ER/mitochondria contacts.
References
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The mammalian unfolded protein response
TL;DR: In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure as mentioned in this paper.
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The mitochondrial calcium uniporter is a highly selective ion channel
TL;DR: By patch-clamping the inner mitochondrial membrane, it is concluded that the properties of the current mediated by this novel channel are those of the MCU, enabling high Ca2+ selectivity despite relatively low cytoplasmic Ca 2+ concentrations.
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Orchestrating the unfolded protein response in health and disease
TL;DR: As the authors gain a greater understanding of the mechanisms that control UPR activation, it should be possible to discover methods to activate or inhibit the UPR as desired for therapeutic benefit.
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Mitochondria and calcium: from cell signalling to cell death
TL;DR: Accumulation of Ca2+ into mitochondria regulates mitochondrial metabolism and causes a transient depolarisation of mitochondrial membrane potential, and alteration of spatiotemporal characteristics of cellular [Ca2+]c signalling and downregulates mitochondrial metabolism.
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Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels.
Gyorgy Szabadkai,Katiuscia Bianchi,Péter Várnai,Diego De Stefani,Mariusz R. Wieckowski,Mariusz R. Wieckowski,Dario Cavagna,Anikó Ilona Nagy,Tamas Balla,Rosario Rizzuto +9 more
TL;DR: It is demonstrated that VDAC1 is physically linked to the endoplasmic reticulum Ca2+-release channel inositol 1,4,5-trisphosphate receptor (IP3R) through the molecular chaperone glucose-regulated protein 75 (grp75) and functional interaction between the channels was shown by the recombinant expression of the ligand-binding domain of the IP3R on the ER or mitochondrial surface.