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      The Interface Between ER and Mitochondria: Molecular Compositions and Functions

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          Abstract

          Mitochondria and endoplasmic reticulum (ER) are essential organelles in eukaryotic cells, which play key roles in various biological pathways. Mitochondria are responsible for ATP production, maintenance of Ca 2+ homeostasis and regulation of apoptosis, while ER is involved in protein folding, lipid metabolism as well as Ca 2+ homeostasis. These organelles have their own functions, but they also communicate via mitochondrial-associated ER membrane (MAM) to provide another level of regulations in energy production, lipid process, Ca 2+ buffering, and apoptosis. Hence, defects in MAM alter cell survival and death. Here, we review components forming the molecular junctions of MAM and how MAM regulates cellular functions. Furthermore, we discuss the effects of impaired ER-mitochondrial communication in various neurodegenerative diseases.

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          An ER-mitochondria tethering complex revealed by a synthetic biology screen.

          Benoît Kornmann, Erin Currie, Sean R Collins … (2009)
          Communication between organelles is an important feature of all eukaryotic cells. To uncover components involved in mitochondria/endoplasmic reticulum (ER) junctions, we screened for mutants that could be complemented by a synthetic protein designed to artificially tether the two organelles. We identified the Mmm1/Mdm10/Mdm12/Mdm34 complex as a molecular tether between ER and mitochondria. The tethering complex was composed of proteins resident of both ER and mitochondria. With the use of genome-wide mapping of genetic interactions, we showed that the components of the tethering complex were functionally connected to phospholipid biosynthesis and calcium-signaling genes. In mutant cells, phospholipid biosynthesis was impaired. The tethering complex localized to discrete foci, suggesting that discrete sites of close apposition between ER and mitochondria facilitate interorganelle calcium and phospholipid exchange.
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            A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP.

            Bruno Mesmin, Joëlle Bigay, Joachim Moser von Filseck … (2013)
            Several proteins at endoplasmic reticulum (ER)-Golgi membrane contact sites contain a PH domain that interacts with the Golgi phosphoinositide PI(4)P, a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. This architecture suggests the ability to both tether organelles and transport lipids between them. We show that in oxysterol binding protein (OSBP) these two activities are coupled by a four-step cycle. Membrane tethering by the PH domain and the FFAT motif enables sterol transfer by the lipid transfer domain (ORD), followed by back transfer of PI(4)P by the ORD. Finally, PI(4)P is hydrolyzed in cis by the ER protein Sac1. The energy provided by PI(4)P hydrolysis drives sterol transfer and allows negative feedback when PI(4)P becomes limiting. Other lipid transfer proteins are tethered by the same mechanism. Thus, OSBP-mediated back transfer of PI(4)P might coordinate the transfer of other lipid species at the ER-Golgi interface. Copyright © 2013 Elsevier Inc. All rights reserved.
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              MAM (mitochondria-associated membranes) in mammalian cells: lipids and beyond.

              Jean Vance (2014)
              One mechanism by which communication between the endoplasmic reticulum (ER) and mitochondria is achieved is by close juxtaposition between these organelles via mitochondria-associated membranes (MAM). The MAM consist of a region of the ER that is enriched in several lipid biosynthetic enzyme activities and becomes reversibly tethered to mitochondria. Specific proteins are localized, sometimes transiently, in the MAM. Several of these proteins have been implicated in tethering the MAM to mitochondria. In mammalian cells, formation of these contact sites between MAM and mitochondria appears to be required for key cellular events including the transport of calcium from the ER to mitochondria, the import of phosphatidylserine into mitochondria from the ER for decarboxylation to phosphatidylethanolamine, the formation of autophagosomes, regulation of the morphology, dynamics and functions of mitochondria, and cell survival. This review focuses on the functions proposed for MAM in mediating these events in mammalian cells. In light of the apparent involvement of MAM in multiple fundamental cellular processes, recent studies indicate that impaired contact between MAM and mitochondria might underlie the pathology of several human neurodegenerative diseases, including Alzheimer's disease. Moreover, MAM has been implicated in modulating glucose homeostasis and insulin resistance, as well as in some viral infections. Copyright © 2013 Elsevier B.V. All rights reserved.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Mol Cells
                Journal ID (iso-abbrev): Mol. Cells
                Journal ID (publisher-id): ksmcb
                Title: Molecules and Cells
                Publisher: Korean Society for Molecular and Cellular Biology
                ISSN (Print): 1016-8478
                ISSN (Electronic): 0219-1032
                Publication date (Print): 31 December 2018
                Publication date (Electronic): 12 December 2018
                Volume: 41
                Issue: 12
                Pages: 1000-1007
                Affiliations
                [1 ]Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 44919, Korea
                [2 ]National Creative Research Initiative Center for Proteostasis, Ulsan National Institute of Science and Technology, Ulsan 44919, Korea
                Author notes
                [* ]Correspondence: ktaimin@ 123456unist.ac.kr
                Article
                Publisher ID: molce-41-12-1000
                DOI: 10.14348/molcells.2018.0438
                PMC ID: 6315321
                PubMed ID: 30590907
                SO-VID: 0424f248-bf49-4950-8d07-6390509bd766
                Copyright © © The Korean Society for Molecular and Cellular Biology. All rights reserved.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/.

                History
                Date received : 29 November 2018
                Date revision received : 08 December 2018
                Date accepted : 09 December 2018
                Categories
                Subject: Minireview

                Keywords: er-mitochondria tethering,mitochondrial-associated er membrane (mam),neurodegenerative disease
                Data availability:
                Keywords: er-mitochondria tethering, mitochondrial-associated er membrane (mam), neurodegenerative disease

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