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Journal articles on the topic 'Organelle contact sites'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 March 2023

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1

King, Christopher, Prabuddha Sengupta, Arnold Y. Seo, and Jennifer Lippincott-Schwartz. "ER membranes exhibit phase behavior at sites of organelle contact." Proceedings of the National Academy of Sciences 117, no. 13 (2020): 7225–35. http://dx.doi.org/10.1073/pnas.1910854117.

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The endoplasmic reticulum (ER) is the site of synthesis of secretory and membrane proteins and contacts every organelle of the cell, exchanging lipids and metabolites in a highly regulated manner. How the ER spatially segregates its numerous and diverse functions, including positioning nanoscopic contact sites with other organelles, is unclear. We demonstrate that hypotonic swelling of cells converts the ER and other membrane-bound organelles into micrometer-scale large intracellular vesicles (LICVs) that retain luminal protein content and maintain contact sites with each other through localiz

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2

Elbaz-Alon, Yael. "Mitochondria–organelle contact sites: the plot thickens." Biochemical Society Transactions 45, no. 2 (2017): 477–88. http://dx.doi.org/10.1042/bst20160130.

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Membrane contact sites (MCSs) are areas of close apposition between the membranes of two different organelles that enable non-vesicular transfer of ions and lipids. Recent studies reveal that mitochondria maintain contact sites with organelles other than the endoplasmic reticulum such as the vacuole, plasma membrane and peroxisomes. This review focuses on novel findings achieved mainly in yeast regarding tethers, function and regulation of mitochondria–organelle contact sites. The emerging network of MCSs linking virtually all cellular organelles is highly dynamic and integrated with cellular

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3

Mahen, Robert. "cNap1 bridges centriole contact sites to maintain centrosome cohesion." PLOS Biology 20, no. 10 (2022): e3001854. http://dx.doi.org/10.1371/journal.pbio.3001854.

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Centrioles are non-membrane-bound organelles that participate in fundamental cellular processes through their ability to form physical contacts with other structures. During interphase, two mature centrioles can associate to form a single centrosome—a phenomenon known as centrosome cohesion. Centrosome cohesion is important for processes such as cell migration, and yet how it is maintained is unclear. Current models indicate that pericentriolar fibres termed rootlets, also known as the centrosome linker, entangle to maintain centriole proximity. Here, I uncover a centriole–centriole contact si

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4

Prinz, William A. "Bridging the gap: Membrane contact sites in signaling, metabolism, and organelle dynamics." Journal of Cell Biology 205, no. 6 (2014): 759–69. http://dx.doi.org/10.1083/jcb.201401126.

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Regions of close apposition between two organelles, often referred to as membrane contact sites (MCSs), mostly form between the endoplasmic reticulum and a second organelle, although contacts between mitochondria and other organelles have also begun to be characterized. Although these contact sites have been noted since cells first began to be visualized with electron microscopy, the functions of most of these domains long remained unclear. The last few years have witnessed a dramatic increase in our understanding of MCSs, revealing the critical roles they play in intracellular signaling, meta

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Klemm, Robin W. "Getting in Touch Is an Important Step: Control of Metabolism at Organelle Contact Sites." Contact 4 (January 2021): 251525642199370. http://dx.doi.org/10.1177/2515256421993708.

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Metabolic pathways are often spread over several organelles and need to be functionally integrated by controlled organelle communication. Physical organelle contact-sites have emerged as critical hubs in the regulation of cellular metabolism, but the molecular understanding of mechanisms that mediate formation or regulation of organelle interfaces was until recently relatively limited. Mitochondria are central organelles in anabolic and catabolic pathways and therefore interact with a number of other cellular compartments including the endoplasmic reticulum (ER) and lipid droplets (LDs). An in

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6

Henne, W. Mike. "Organelle remodeling at membrane contact sites." Journal of Structural Biology 196, no. 1 (2016): 15–19. http://dx.doi.org/10.1016/j.jsb.2016.05.003.

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7

Picca, Anna, Riccardo Calvani, Hélio José Coelho-Junior, Francesco Landi, Roberto Bernabei, and Emanuele Marzetti. "Inter-Organelle Membrane Contact Sites and Mitochondrial Quality Control during Aging: A Geroscience View." Cells 9, no. 3 (2020): 598. http://dx.doi.org/10.3390/cells9030598.

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Mitochondrial dysfunction and failing mitochondrial quality control (MQC) are major determinants of aging. Far from being standalone organelles, mitochondria are intricately related with cellular other compartments, including lysosomes. The intimate relationship between mitochondria and lysosomes is reflected by the fact that lysosomal degradation of dysfunctional mitochondria is the final step of mitophagy. Inter-organelle membrane contact sites also allow bidirectional communication between mitochondria and lysosomes as part of nondegradative pathways. This interaction establishes a function

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8

Zhemkov, Vladimir, Jen Liou, and Ilya Bezprozvanny. "Sigma 1 Receptor, Cholesterol and Endoplasmic Reticulum Contact Sites." Contact 4 (January 2021): 251525642110265. http://dx.doi.org/10.1177/25152564211026505.

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Recent studies indicated potential importance of membrane contact sites (MCS) between the endoplasmic reticulum (ER) and other cellular organelles. These MCS have unique protein and lipid composition and serve as hubs for inter-organelle communication and signaling. Despite extensive investigation of MCS protein composition and functional roles, little is known about the process of MCS formation. In this perspective, we propose a hypothesis that MCS are formed not as a result of random interactions between membranes of ER and other organelles but on the basis of pre-existing cholesterol-enrich

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9

Zwilling, Emma, and Fulvio Reggiori. "Membrane Contact Sites in Autophagy." Cells 11, no. 23 (2022): 3813. http://dx.doi.org/10.3390/cells11233813.

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Eukaryotes utilize different communication strategies to coordinate processes between different cellular compartments either indirectly, through vesicular transport, or directly, via membrane contact sites (MCSs). MCSs have been implicated in lipid metabolism, calcium signaling and the regulation of organelle biogenesis in various cell types. Several studies have shown that MCSs play a crucial role in the regulation of macroautophagy, an intracellular catabolic transport route that is characterized by the delivery of cargoes (proteins, protein complexes or aggregates, organelles and pathogens)

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10

Ovciarikova, Jana, Shikha Shikha, and Lilach Sheiner. "Nuclear Interactions: A Spotlight on Nuclear Mitochondrial Membrane Contact Sites." Contact 5 (January 2022): 251525642210962. http://dx.doi.org/10.1177/25152564221096217.

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Membrane contact sites (MCS) are critical for cellular functions of eukaryotes, as they enable communication and exchange between organelles. Research over the last decade unravelled the function and composition of MCS between a variety of organelles including mitochondria, ER, plasma membrane, lysosomes, lipid droplets, peroxisome and endosome, to name a few. In fact, MCS are found between any pair of organelles studied to date, with common functions including lipid exchange, calcium signalling and organelle positioning in the cell. Work in the past year has started addressing the composition

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11

Poggio, Elena, Marisa Brini, and Tito Calì. "Get Closer to the World of Contact Sites: A Beginner's Guide to Proximity-Driven Fluorescent Probes." Contact 5 (January 2022): 251525642211357. http://dx.doi.org/10.1177/25152564221135748.

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To maintain cellular homeostasis and to coordinate the proper response to a specific stimulus, information must be integrated throughout the cell in a well-organized network, in which organelles are the crucial nodes and membrane contact sites are the main edges. Membrane contact sites are the cellular subdomains where two or more organelles come into close apposition and interact with each other. Even though many inter-organelle contacts have been identified, most of them are still not fully characterized, therefore their study is an appealing and expanding field of research. Thanks to signif

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12

David, Yotam, Inês G. Castro, and Maya Schuldiner. "The Fast and the Furious: Golgi Contact Sites." Contact 4 (January 2021): 251525642110344. http://dx.doi.org/10.1177/25152564211034424.

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Contact sites are areas of close apposition between two membranes that coordinate nonvesicular communication between organelles. Such interactions serve a wide range of cellular functions from regulating metabolic pathways to executing stress responses and coordinating organelle inheritance. The past decade has seen a dramatic increase in information on certain contact sites, mostly those involving the endoplasmic reticulum. However, despite its central role in the secretory pathway, the Golgi apparatus and its contact sites remain largely unexplored. In this review, we discuss the current kno

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13

Tamura, Yasushi, Shin Kawano, and Toshiya Endo. "Organelle contact zones as sites for lipid transfer." Journal of Biochemistry 165, no. 2 (2018): 115–23. http://dx.doi.org/10.1093/jb/mvy088.

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14

Ridgway, Neale D., and Kexin Zhao. "Cholesterol transfer at endosomal-organelle membrane contact sites." Current Opinion in Lipidology 29, no. 3 (2018): 212–17. http://dx.doi.org/10.1097/mol.0000000000000506.

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15

Cockcroft, Shamshad, and Padinjat Raghu. "Phospholipid transport protein function at organelle contact sites." Current Opinion in Cell Biology 53 (August 2018): 52–60. http://dx.doi.org/10.1016/j.ceb.2018.04.011.

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16

Bean, Björn D. M., Samantha K. Dziurdzik, Kathleen L. Kolehmainen, et al. "Competitive organelle-specific adaptors recruit Vps13 to membrane contact sites." Journal of Cell Biology 217, no. 10 (2018): 3593–607. http://dx.doi.org/10.1083/jcb.201804111.

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The regulated expansion of membrane contact sites, which mediate the nonvesicular exchange of lipids between organelles, requires the recruitment of additional contact site proteins. Yeast Vps13 dynamically localizes to membrane contacts that connect the ER, mitochondria, endosomes, and vacuoles and is recruited to the prospore membrane in meiosis, but its targeting mechanism is unclear. In this study, we identify the sorting nexin Ypt35 as a novel adaptor that recruits Vps13 to endosomal and vacuolar membranes. We characterize an interaction motif in the Ypt35 N terminus and identify related

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17

Henne, W. Mike, and Hanaa Hariri. "Endoplasmic Reticulum-Vacuole Contact Sites “Bloom” With Stress-Induced Lipid Droplets." Contact 1 (January 2018): 251525641875611. http://dx.doi.org/10.1177/2515256418756112.

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Lipid droplets (LDs) serve as specialized cytoplasmic organelles that harbor energy-rich lipids for long-term storage and may be mobilized as nutrient sources during extended starvation. How cells coordinate LD biogenesis and utilization in response to fluctuations in nutrient availability remains poorly understood. Here, we discuss our recent work revealing how yeast spatially organize LD budding at organelle contacts formed between the endoplasmic reticulum and yeast vacuole/lysosome (sites known as nucleus-vacuole junctions [NVJs]). During times of imminent nutrient exhaustion, we observe b

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18

Hertlein, Vanessa, Hector Flores-Romero, Kushal K. Das, et al. "MERLIN: a novel BRET-based proximity biosensor for studying mitochondria–ER contact sites." Life Science Alliance 3, no. 1 (2019): e201900600. http://dx.doi.org/10.26508/lsa.201900600.

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The contacts between the ER and mitochondria play a key role in cellular functions such as the exchange of lipids and calcium between both organelles, as well as in apoptosis and autophagy signaling. The molecular architecture and spatiotemporal regulation of these distinct contact regions remain obscure and there is a need for new tools that enable tackling these questions. Here, we present a new bioluminescence resonance energy transfer–based biosensor for the quantitative analysis of distances between the ER and mitochondria that we call MERLIN (Mitochondria–ER Length Indicator Nanosensor).

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19

Lee, Jason E., Peter I. Cathey, Haoxi Wu, Roy Parker, and Gia K. Voeltz. "Endoplasmic reticulum contact sites regulate the dynamics of membraneless organelles." Science 367, no. 6477 (2020): eaay7108. http://dx.doi.org/10.1126/science.aay7108.

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Tethered interactions between the endoplasmic reticulum (ER) and other membrane-bound organelles allow for efficient transfer of ions and/or macromolecules and provide a platform for organelle fission. Here, we describe an unconventional interface between membraneless ribonucleoprotein granules, such as processing bodies (P-bodies, or PBs) and stress granules, and the ER membrane. We found that PBs are tethered at molecular distances to the ER in human cells in a tunable fashion. ER-PB contact and PB biogenesis were modulated by altering PB composition, ER shape, or ER translational capacity.

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Di Mattia, Thomas, Catherine Tomasetto, and Fabien Alpy. "A Third Musketeer on the ER: MOSPD2 is a Novel VAP-related Receptor for FFAT Motifs." Contact 1 (January 2018): 251525641880973. http://dx.doi.org/10.1177/2515256418809730.

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Interorganelle membrane contact sites are subcellular structures that favor exchange and communication inside the cell. Such microdomains are built by molecular bridges that create a physical connection between two distinct organelles. The field of contact sites is now flourishing with discoveries of new tethering molecules. In that context, we identified by an unbiased proteomic approach a novel scaffold protein named MOtile SPerm Domain-containing protein 2 (MOSPD2). MOSPD2 is an endoplasmic reticulum (ER)-resident protein that is able to interact with several organelle-bound proteins that p

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21

Ma, Xiaowen, Hui Qian, Allen Chen, Hong-Min Ni, and Wen-Xing Ding. "Perspectives on Mitochondria–ER and Mitochondria–Lipid Droplet Contact in Hepatocytes and Hepatic Lipid Metabolism." Cells 10, no. 9 (2021): 2273. http://dx.doi.org/10.3390/cells10092273.

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Emerging evidence suggests that mitochondrion–endoplasmic reticulum (ER) and mitochondrion–lipid droplet (LD) contact sites are critical in regulating lipid metabolism in cells. It is well established that intracellular organelles communicate with each other continuously through membrane contact sites to maintain organelle function and cellular homeostasis. The accumulation of LDs in hepatocytes is an early indicator of non-alcoholic fatty liver disease (NAFLD) and alcohol-related liver disease (ALD), which may indicate a breakdown in proper inter-organelle communication. In this review, we di

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22

van Vliet, Alexander R., Maria Livia Sassano, and Patrizia Agostinis. "The Unfolded Protein Response and Membrane Contact Sites: Tethering as a Matter of Life and Death?" Contact 1 (January 2018): 251525641877051. http://dx.doi.org/10.1177/2515256418770512.

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The endoplasmic reticulum (ER) is the most extensive organelle of the eukaryotic cell and constitutes the major site of protein and lipid synthesis and regulation of intracellular Ca2+ levels. To exert these functions properly, the ER network is shaped in structurally and functionally distinct domains that dynamically remodel in response to intrinsic and extrinsic cues. Moreover, the ER establishes a tight communication with virtually all organelles of the cell through specific subdomains called membrane contact sites. These contact sites allow preferential, nonvesicular channeling of key biol

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23

Yadav, Shweta, Shamshad Cockcroft, and Padinjat Raghu. "The Drosophila photoreceptor as a model system for studying signalling at membrane contact sites." Biochemical Society Transactions 44, no. 2 (2016): 447–51. http://dx.doi.org/10.1042/bst20150256.

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Several recent studies have demonstrated the existence of membrane contact sites (MCS) between intracellular organelles in eukaryotic cells. Recent exciting studies have also demonstrated the existence of biomolecular interactions at these contact sites in mediating changes in the membrane composition of the cellular compartments. However, the role of such contact sites in regulating organelle function and physiological processes remains less clear. In this review we discuss the existence of a contact site between the plasma membrane (PM) and the endoplasmic reticulum (ER) in Drosophila photor

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Nieto-Garai, Jon Ander, June Olazar-Intxausti, Itxaso Anso, Maier Lorizate, Oihana Terrones, and Francesc-Xabier Contreras. "Super-Resolution Microscopy to Study Interorganelle Contact Sites." International Journal of Molecular Sciences 23, no. 23 (2022): 15354. http://dx.doi.org/10.3390/ijms232315354.

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Interorganelle membrane contact sites (MCS) are areas of close vicinity between the membranes of two organelles that are maintained by protein tethers. Recently, a significant research effort has been made to study MCS, as they are implicated in a wide range of biological functions, such as organelle biogenesis and division, apoptosis, autophagy, and ion and phospholipid homeostasis. Their composition, characteristics, and dynamics can be studied by different techniques, but in recent years super-resolution fluorescence microscopy (SRFM) has emerged as a powerful tool for studying MCS. In this

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Wong, Louise H., and Tim P. Levine. "Lipid transfer proteins do their thing anchored at membrane contact sites… but what is their thing?" Biochemical Society Transactions 44, no. 2 (2016): 517–27. http://dx.doi.org/10.1042/bst20150275.

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Membrane contact sites are structures where two organelles come close together to regulate flow of material and information between them. One type of inter-organelle communication is lipid exchange, which must occur for membrane maintenance and in response to environmental and cellular stimuli. Soluble lipid transfer proteins have been extensively studied, but additional families of transfer proteins have been identified that are anchored into membranes by transmembrane helices so that they cannot diffuse through the cytosol to deliver lipids. If such proteins target membrane contact sites the

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Castro, Inês Gomes, Maya Schuldiner, and Einat Zalckvar. "Mind the Organelle Gap – Peroxisome Contact Sites in Disease." Trends in Biochemical Sciences 43, no. 3 (2018): 199–210. http://dx.doi.org/10.1016/j.tibs.2018.01.001.

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Levine, Tim, and Chris Loewen. "Inter-organelle membrane contact sites: through a glass, darkly." Current Opinion in Cell Biology 18, no. 4 (2006): 371–78. http://dx.doi.org/10.1016/j.ceb.2006.06.011.

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Perico, Chiara, and Imogen Sparkes. "Plant organelle dynamics: cytoskeletal control and membrane contact sites." New Phytologist 220, no. 2 (2018): 381–94. http://dx.doi.org/10.1111/nph.15365.

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29

Henne, W. Mike, Jen Liou, and Scott D. Emr. "Molecular mechanisms of inter-organelle ER–PM contact sites." Current Opinion in Cell Biology 35 (August 2015): 123–30. http://dx.doi.org/10.1016/j.ceb.2015.05.001.

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Dickson, Eamonn J., Jill B. Jensen, and Bertil Hille. "Regulation of calcium and phosphoinositides at endoplasmic reticulum–membrane junctions." Biochemical Society Transactions 44, no. 2 (2016): 467–73. http://dx.doi.org/10.1042/bst20150262.

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Effective cellular function requires both compartmentalization of tasks in space and time, and coordination of those efforts. The endoplasmic reticulum's (ER) expansive and ramifying structure makes it ideally suited to serve as a regulatory platform for organelle–organelle communication through membrane contacts. These contact sites consist of two membranes juxtaposed at a distance less than 30 nm that mediate the exchange of lipids and ions without the need for membrane fission or fusion, a process distinct from classical vesicular transport. Membrane contact sites are positioned by organell

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Giamogante, Flavia, Lucia Barazzuol, Marisa Brini, and Tito Calì. "ER–Mitochondria Contact Sites Reporters: Strengths and Weaknesses of the Available Approaches." International Journal of Molecular Sciences 21, no. 21 (2020): 8157. http://dx.doi.org/10.3390/ijms21218157.

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Organelle intercommunication represents a wide area of interest. Over the last few decades, increasing evidence has highlighted the importance of organelle contact sites in many biological processes including Ca2+ signaling, lipid biosynthesis, apoptosis, and autophagy but also their involvement in pathological conditions. ER–mitochondria tethering is one of the most investigated inter-organelle communications and it is differently modulated in response to several cellular conditions including, but not limited to, starvation, Endoplasmic Reticulum (ER) stress, and mitochondrial shape modificat

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Grippa, Alexandra, Laura Buxó, Gabriel Mora, et al. "The seipin complex Fld1/Ldb16 stabilizes ER–lipid droplet contact sites." Journal of Cell Biology 211, no. 4 (2015): 829–44. http://dx.doi.org/10.1083/jcb.201502070.

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Lipid droplets (LDs) are storage organelles consisting of a neutral lipid core surrounded by a phospholipid monolayer and a set of LD-specific proteins. Most LD components are synthesized in the endoplasmic reticulum (ER), an organelle that is often physically connected with LDs. How LD identity is established while maintaining biochemical and physical connections with the ER is not known. Here, we show that the yeast seipin Fld1, in complex with the ER membrane protein Ldb16, prevents equilibration of ER and LD surface components by stabilizing the contact sites between the two organelles. In

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Elbaz, Yael, and Maya Schuldiner. "Staying in touch: the molecular era of organelle contact sites." Trends in Biochemical Sciences 36, no. 11 (2011): 616–23. http://dx.doi.org/10.1016/j.tibs.2011.08.004.

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Ellenrieder, Lars, Heike Rampelt, and Thomas Becker. "Connection of Protein Transport and Organelle Contact Sites in Mitochondria." Journal of Molecular Biology 429, no. 14 (2017): 2148–60. http://dx.doi.org/10.1016/j.jmb.2017.05.023.

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Bohnert, Maria. "Organelle Contact Sites: Lipid Droplets Hooked by Metabolically Controlled Tethers." Current Biology 29, no. 10 (2019): R375—R377. http://dx.doi.org/10.1016/j.cub.2019.03.049.

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Joshi, Amit S., Joey V. Ragusa, William A. Prinz, and Sarah Cohen. "Multiple C2 domain–containing transmembrane proteins promote lipid droplet biogenesis and growth at specialized endoplasmic reticulum subdomains." Molecular Biology of the Cell 32, no. 12 (2021): 1147–57. http://dx.doi.org/10.1091/mbc.e20-09-0590.

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MCTPs can tubulate the ER via reticulon homology domains. They localize to ER subdomains that are sites of lipid droplet (LD) biogenesis. MCTP reticulon homology domains promote LD biogenesis, while C2 domains mediate ER-LD contacts to promote LD growth. MCTPs may function more broadly to link ER tubules with organelle contact sites.

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Tamura, Yasushi, Shin Kawano, and Toshiya Endo. "Lipid homeostasis in mitochondria." Biological Chemistry 401, no. 6-7 (2020): 821–33. http://dx.doi.org/10.1515/hsz-2020-0121.

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AbstractMitochondria are surrounded by the two membranes, the outer and inner membranes, whose lipid compositions are optimized for proper functions and structural organizations of mitochondria. Although a part of mitochondrial lipids including their characteristic lipids, phosphatidylethanolamine and cardiolipin, are synthesized within mitochondria, their precursor lipids and other lipids are transported from other organelles, mainly the ER. Mitochondrially synthesized lipids are re-distributed within mitochondria and to other organelles, as well. Recent studies pointed to the important roles

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Murley, Andrew, Reta D. Sarsam, Alexandre Toulmay, Justin Yamada, William A. Prinz, and Jodi Nunnari. "Ltc1 is an ER-localized sterol transporter and a component of ER–mitochondria and ER–vacuole contacts." Journal of Cell Biology 209, no. 4 (2015): 539–48. http://dx.doi.org/10.1083/jcb.201502033.

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Organelle contact sites perform fundamental functions in cells, including lipid and ion homeostasis, membrane dynamics, and signaling. Using a forward proteomics approach in yeast, we identified new ER–mitochondria and ER–vacuole contacts specified by an uncharacterized protein, Ylr072w. Ylr072w is a conserved protein with GRAM and VASt domains that selectively transports sterols and is thus termed Ltc1, for Lipid transfer at contact site 1. Ltc1 localized to ER–mitochondria and ER–vacuole contacts via the mitochondrial import receptors Tom70/71 and the vacuolar protein Vac8, respectively. At

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Friedman, Jonathan R. "Mitochondria from the Outside in: The Relationship Between Inter-Organelle Crosstalk and Mitochondrial Internal Organization." Contact 5 (January 2022): 251525642211332. http://dx.doi.org/10.1177/25152564221133267.

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A fundamental role of membrane-bound organelles is the compartmentalization and organization of cellular processes. Mitochondria perform an immense number of metabolic chemical reactions and to efficiently regulate these, the organelle organizes its inner membrane into distinct morphological domains, including its characteristic cristae membranes. In recent years, a structural feature of increasing apparent importance is the inter-connection between the mitochondrial exterior and other organelles at membrane contact sites (MCSs). Mitochondria form MCSs with almost every other organelle in the

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Toulmay, A., and W. A. Prinz. "A conserved membrane-binding domain targets proteins to organelle contact sites." Journal of Cell Science 125, no. 1 (2012): 49–58. http://dx.doi.org/10.1242/jcs.085118.

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Wilhelm, Léa P., Catherine Tomasetto, and Fabien Alpy. "Touché! STARD3 and STARD3NL tether the ER to endosomes." Biochemical Society Transactions 44, no. 2 (2016): 493–98. http://dx.doi.org/10.1042/bst20150269.

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Membrane contact sites (MCSs) are subcellular regions where the membranes of distinct organelles come into close apposition. These specialized areas of the cell, which are involved in inter-organelle metabolite exchange, are scaffolded by specific complexes. STARD3 [StAR (steroidogenic acute regulatory protein)-related lipid transfer domain-3] and its close paralogue STARD3NL (STARD3 N-terminal like) are involved in the formation of contacts between late-endosomes and the endoplasmic reticulum (ER). The lipid transfer protein (LTP) STARD3 and STARD3NL, which are both anchored on the limiting m

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Dziurdzik, Samantha K., Björn D. M. Bean, and Elizabeth Conibear. "An Interorganellar Bidding War: Vps13 Localization by Competitive Organelle-Specific Adaptors." Contact 1 (January 2018): 251525641881462. http://dx.doi.org/10.1177/2515256418814621.

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Membrane contact sites are regulated through the controlled recruitment of constituent proteins. Yeast vacuolar protein sorting 13 (Vps13) dynamically localizes to membrane contact sites at endosomes, vacuoles, mitochondria, and the endoplasmic reticulum under different cellular conditions and is recruited to the prospore membrane during meiosis. Prior to our recent work, the mechanism for localization at contact sites was largely unknown. We identified Ypt35 as a novel Vps13 adaptor for endosomes and the nucleus-vacuole junction. Furthermore, we discovered a conserved recruitment motif in Ypt

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Picca, Anna, Flora Guerra, Riccardo Calvani, et al. "Circulating Mitochondrial DNA and Inter-Organelle Contact Sites in Aging and Associated Conditions." Cells 11, no. 4 (2022): 675. http://dx.doi.org/10.3390/cells11040675.

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Mitochondria are primarily involved in cell bioenergetics, regulation of redox homeostasis, and cell death/survival signaling. An immunostimulatory property of mitochondria has also been recognized which is deployed through the extracellular release of entire or portioned organelle and/or mitochondrial DNA (mtDNA) unloading. Dynamic homo- and heterotypic interactions involving mitochondria have been described. Each type of connection has functional implications that eventually optimize mitochondrial activity according to the bioenergetic demands of a specific cell/tissue. Inter-organelle commu

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Hariri, Hanaa, Rupali Ugrankar, Yang Liu, and W. Mike Henne. "Inter-organelle ER-endolysosomal contact sites in metabolism and disease across evolution." Communicative & Integrative Biology 9, no. 3 (2016): e1156278. http://dx.doi.org/10.1080/19420889.2016.1156278.

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Bohnert, Maria. "Tether Me, Tether Me Not—Dynamic Organelle Contact Sites in Metabolic Rewiring." Developmental Cell 54, no. 2 (2020): 212–25. http://dx.doi.org/10.1016/j.devcel.2020.06.026.

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Giamogante, Flavia, Lucia Barazzuol, Elena Poggio, Marta Tromboni, Marisa Brini, and Tito Calì. "Stable Integration of Inducible SPLICS Reporters Enables Spatio-Temporal Analysis of Multiple Organelle Contact Sites upon Modulation of Cholesterol Traffic." Cells 11, no. 10 (2022): 1643. http://dx.doi.org/10.3390/cells11101643.

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The study of organelle contact sites has received a great impulse due to increased interest in the understanding of their involvement in many disease conditions. Split-GFP-based contact sites (SPLICS) reporters emerged as essential tools to easily detect changes in a wide range of organelle contact sites in cultured cells and in vivo, e.g., in zebrafish larvae. We report here on the generation of a new vector library of SPLICS cloned into a piggyBac system for stable and inducible expression of the reporters in a cell line of interest to overcome any potential weakness due to variable protein

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Calì, Tito, and Marisa Brini. "Quantification of organelle contact sites by split-GFP-based contact site sensors (SPLICS) in living cells." Nature Protocols 16, no. 11 (2021): 5287–308. http://dx.doi.org/10.1038/s41596-021-00614-1.

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Kwak, Chulhwan, Sanghee Shin, Jong-Seok Park, et al. "Contact-ID, a tool for profiling organelle contact sites, reveals regulatory proteins of mitochondrial-associated membrane formation." Proceedings of the National Academy of Sciences 117, no. 22 (2020): 12109–20. http://dx.doi.org/10.1073/pnas.1916584117.

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The mitochondria-associated membrane (MAM) has emerged as a cellular signaling hub regulating various cellular processes. However, its molecular components remain unclear owing to lack of reliable methods to purify the intact MAM proteome in a physiological context. Here, we introduce Contact-ID, a split-pair system of BioID with strong activity, for identification of the MAM proteome in live cells. Contact-ID specifically labeled proteins proximal to the contact sites of the endoplasmic reticulum (ER) and mitochondria, and thereby identified 115 MAM-specific proteins. The identified MAM prote

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Leal, Nuno Santos, and Luís Miguel Martins. "Mind the Gap: Mitochondria and the Endoplasmic Reticulum in Neurodegenerative Diseases." Biomedicines 9, no. 2 (2021): 227. http://dx.doi.org/10.3390/biomedicines9020227.

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The way organelles are viewed by cell biologists is quickly changing. For many years, these cellular entities were thought to be unique and singular structures that performed specific roles. However, in recent decades, researchers have discovered that organelles are dynamic and form physical contacts. In addition, organelle interactions modulate several vital biological functions, and the dysregulation of these contacts is involved in cell dysfunction and different pathologies, including neurodegenerative diseases. Mitochondria–ER contact sites (MERCS) are among the most extensively studied an

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Saito, Atsushi, and Kazunori Imaizumi. "Unfolded Protein Response-Dependent Communication and Contact among Endoplasmic Reticulum, Mitochondria, and Plasma Membrane." International Journal of Molecular Sciences 19, no. 10 (2018): 3215. http://dx.doi.org/10.3390/ijms19103215.

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The function of the endoplasmic reticulum (ER) can be impaired by changes to the extra- and intracellular environment, such as disruption of calcium homeostasis, expression of mutated proteins, and oxidative stress. In response to disruptions to ER homeostasis, eukaryotic cells activate canonical branches of signal transduction cascades, collectively termed the unfolded protein response (UPR). The UPR functions to remove or recover the activity of misfolded proteins that accumulated in the ER and to avoid irreversible cellular damage. Additionally, the UPR plays unique physiological roles in t

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