Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions

Csordás, György; Weaver, David; Hajnóczky, György

doi:10.1016/j.tcb.2018.02.009

Cited by 625Mitochondrial Function and PathologyIon Channels and ReceptorsCellular transport and secretion

Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions

Open access

Csordás, György, Weaver, David, Hajnóczky, György·2018·Trends in Cell Biology

DOI 10.1016/j.tcb.2018.02.009PMC PMC6005738

Open this paper in CoChat — free account

Abstract

Interorganellar contacts are increasingly recognized as central to the control of cellular behavior. These contacts, which typically involve a small fraction of the endomembrane surface, are local communication hubs that resemble synapses. We propose the term contactology to denote the analysis of interorganellar contacts. Endoplasmic reticulum (ER) contacts with mitochondria were recognized several decades ago; major roles in ion and lipid transfer, signaling, and membrane dynamics have been established, while others continue to emerge. The functional diversity of ER-mitochondrial (ER-mito) contacts is mirrored in their structural heterogeneity, with subspecialization likely supported by multiple, different linker-forming protein structures. The nanoscale size of the contacts has made studying their structure, function, and dynamics difficult. This review focuses on the structure of the ER-mito contacts, methods for studying them, and the roles of contacts in Ca 2+ and reactive oxygen species (ROS) signaling.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.tcb.2018.02.009

Cites

160 of 160 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

MAM can allow Ca2+ fluxes from the SR to mitochondria and thereby speed up mitochondrial respiration.
“Indeed, MAM can allow Ca2+ fluxes from the SR to mitochondria and thereby speed up mitochondrial respiration (Csordas et al., 2018).”
From Impaired aerobic capacity and premature fatigue preceding muscle weakness in the skeletal muscle Tfam-knockout mouse model (2021) · cites this paper as Csordas et al., 2018
The Ca2+ signaling section (page unavailable) says ER/SR–mitochondrial contacts enable local Ca2+ transfer into mitochondria. The paper does not state there that this transfer speeds mitochondrial respiration; its References section lists a study linking increased ER–mitochondrial coupling to respiration, without establishing the claimed Ca2+-mediated link. (LLM, conf=0.82)
Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · see citing works
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works
Sigma-1 Receptor Chaperones at the ER- Mitochondrion Interface Regulate Ca2+ Signaling and Cell Survival
Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826 · see citing works
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413 · see citing works
Structural and functional features and significance of the physical linkage between ER and mitochondria
Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377 · see citing works
Self-citation
Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging
Dempsey, G. T., Vaughan, J. C., Chen, K. H., Bates, M., & Zhuang, X. (2011) · Nature Methods · doi:10.1038/nmeth.1768 · Cited by 1,374 · see citing works
PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323 · see citing works
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works
MitoCarta2.0: an updated inventory of mammalian mitochondrial proteins
Calvo, S. E., Clauser, K. R., & Mootha, V. K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1003 · Cited by 1,251 · see citing works
Microdomains with High Ca 2+ Close to IP 3 -Sensitive Channels that Are Sensed by Neighboring Mitochondria
Rizzuto, R., Brini, M., Murgia, M., & Pozzan, T. (1993) · Science · doi:10.1126/science.8235595 · Cited by 1,207 · see citing works
Inositol Trisphosphate Receptor Ca2+Release Channels
Foskett, J. K., White, C., Cheung, K.-H., & Mak, D.-O. D. (2007) · Physiological Reviews · doi:10.1152/physrev.00035.2006 · Cited by 1,188 · see citing works
Phospholipid synthesis in a membrane fraction associated with mitochondria.
Vance, J. E. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39106-9 · Cited by 1,153 · see citing works
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012 · see citing works
Vesicle Pools and Ca2+ Microdomains: New Tools for Understanding Their Roles in Neurotransmitter Release
Neher, E. (1998) · Neuron · doi:10.1016/s0896-6273(00)80983-6 · Cited by 1,010 · see citing works
Structure and function of ER membrane contact sites with other organelles
Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933 · see citing works
Structural Basis of Mitochondrial Tethering by Mitofusin Complexes
Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910 · see citing works
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871 · see citing works
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817 · see citing works
Phospholipid Synthesis and Transport in Mammalian Cells
Vance, J. E. (2014) · Traffic · doi:10.1111/tra.12230 · Cited by 777 · see citing works
Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface
Csordás, G., Várnai, P., Golenár, T., Roy, S., Purkins, G., Schneider, T. G., Balla, T., & Hajnóczky, G. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.029 · Cited by 750 · see citing works
Self-citation
Comprehensive Characterization of Genes Required for Protein Folding in the Endoplasmic Reticulum
Jonikas, M. C., Collins, S. R., Denic, V., Oh, E., Toyama, E. Q., Schmid, V., Weibezahn, J., Schwappach, B., Walter, P., Weissman, J. S., et al. (2009) · Science · doi:10.1126/science.1167983 · Cited by 713 · see citing works
Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses
MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia‐Cárcamo, I. L., Muir, J., Fransson, Å., Aspenström, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 677 · see citing works
ER-mitochondria contacts couple mtDNA synthesis with mitochondrial division in human cells
Lewis, S. C., Uchiyama, L. F., & Nunnari, J. (2016) · Science · doi:10.1126/science.aaf5549 · Cited by 673 · see citing works
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 665 · see citing works
Activation of mTORC2 by Association with the Ribosome
Zinzalla, V., Stracka, D., Oppliger, W., & Hall, M. N. (2011) · Cell · doi:10.1016/j.cell.2011.02.014 · Cited by 648 · see citing works
Upregulated function of mitochondria‐associated ER membranes in Alzheimer disease
Area‐Gomez, E., del Carmen Lara Castillo, M., Tambini, M. D., Guardia‐Laguarta, C., de Groof, A. J. C., Madra, M., Ikenouchi, J., Umeda, M., Bird, T. D., Sturley, S. L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.202 · Cited by 638 · see citing works
ER–mitochondria associations are regulated by the VAPB–PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43
Stoica, R., Vos, K. J. D., Paillusson, S., Mueller, S., Sancho, R. M., Lau, K., Vizcay‐Barrena, G., Lin, W.-L., Xu, Y.-F., Lewis, J. M., et al. (2014) · Nature Communications · doi:10.1038/ncomms4996 · Cited by 623 · see citing works
PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts
Chung, J., Torta, F. T., Masai, K., Lucast, L. J., Czapla, H., Tanner, L. B., Narayanaswamy, P., Wenk, M. R., Nakatsu, F., & Camilli, P. V. D. (2015) · Science · doi:10.1126/science.aab1370 · Cited by 620 · see citing works
Increased ER–mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress
Bravo, R., Vicencio, J. M., Parra, V., Troncoso, R., Muñoz, J. P., Bui, M., Quiroga, C., Rodriguez, A. E., Verdejo, H., Ferreira, J., et al. (2011) · Journal of Cell Science · doi:10.1242/jcs.080762 · Cited by 607 · see citing works
PACS‐2 controls endoplasmic reticulum–mitochondria communication and Bid‐mediated apoptosis
Simmen, T., Aslan, J. E., Blagoveshchenskaya, A. D., Thomas, L., Wan, L., Xiang, Y. K., Feliciangeli, S. F., Hung, C., Crump, C. M., & Thomas, G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600559 · Cited by 593 · see citing works
Mitofusin 2 ablation increases endoplasmic reticulum–mitochondria coupling
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504880112 · Cited by 578 · see citing works
VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis
Vos, K. J. D., Mórotz, G. M., Stoica, R., Tudor, E. L., Lau, K., Ackerley, S., Warley, A., Shaw, C. E., & Miller, C. C. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr559 · Cited by 573 · see citing works
X-ROS Signaling: Rapid Mechano-Chemo Transduction in Heart
Prosser, B. L., Ward, C. W., & Lederer, W. J. (2011) · Science · doi:10.1126/science.1202768 · Cited by 564 · see citing works
Calcium at the Center of Cell Signaling: Interplay between Endoplasmic Reticulum, Mitochondria, and Lysosomes
Raffaello, A., Mammucari, C., Gherardi, G., & Rizzuto, R. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.001 · Cited by 542 · see citing works
Bidirectional Ca 2+ -dependent control of mitochondrial dynamics by the Miro GTPase
Saotome, M., Safiulina, D., Szabadkai, G., Das, S., Fransson, Å., Aspenstrom, P., Rizzuto, R., & Hajnóczky, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808953105 · Cited by 538 · see citing works
Self-citation
mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology
Betz, C., Stracka, D., Prescianotto-Baschong, C., Frieden, M., Demaurex, N., & Hall, M. N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302455110 · Cited by 538 · see citing works
Quasi‐synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
Csordás, G., Thomas, A. P., & Hajnóczky, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.96 · Cited by 536 · see citing works
Self-citation
Critical reappraisal confirms that Mitofusin 2 is an endoplasmic reticulum–mitochondria tether
Naon, D., Zaninello, M., Giacomello, M., Varanita, T., Grespi, F., Lakshminaranayan, S., Serafini, A., Semenzato, M., Herkenne, S., Hernández-Alvarez, M. I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606786113 · Cited by 521 · see citing works
Fis1 and Bap31 bridge the mitochondria–ER interface to establish a platform for apoptosis induction
Iwasawa, R., Mahul‐Mellier, A., Datler, C., Pazarentzos, E., & Grimm, S. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.346 · Cited by 520 · see citing works
ER-mitochondria tethering by PDZD8 regulates Ca 2+ dynamics in mammalian neurons
Hirabayashi, Y., Kwon, S., Paek, H., Pernice, W. M., Paul, M. A., Lee, J., Erfani, P., Raczkowski, A. M., Petrey, D. S., Pon, L. A., et al. (2017) · Science · doi:10.1126/science.aan6009 · Cited by 495 · see citing works
Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
Horner, S. M., Liu, H. M., Park, H. S., Briley, J. D., & Gale, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110133108 · Cited by 492 · see citing works
Contacts between the endoplasmic reticulum and other membranes in neurons
Wu, Y., Whiteus, C., Xu, C. S., Hayworth, K. J., Weinberg, R. J., Hess, H. F., & Camilli, P. V. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701078114 · Cited by 481 · see citing works
Control of mitochondrial motility and distribution by the calcium signal
Yi, M., Weaver, D., & Hajnóczky, G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406038 · Cited by 476 · see citing works
Self-citation
Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria
Rapizzi, E., Pinton, P., Szabadkai, G., Wieckowski, M. R., Vandecasteele, G., Baird, G., Tuft, R. A., Fogarty, K. E., & Rizzuto, R. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205091 · Cited by 453 · see citing works
The coming of age of the mitochondria–ER contact: a matter of thickness
Giacomello, M., & Pellegrini, L. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.52 · Cited by 451 · see citing works
There's Something Wrong with my MAM; the ER–Mitochondria Axis and Neurodegenerative Diseases
Paillusson, S., Stoica, R., Gomez-Suaga, P., Lau, D. H. W., Mueller, S., Miller, T., & Miller, C. C. J. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.01.008 · Cited by 439 · see citing works
Enjoy the Trip: Calcium in Mitochondria Back and Forth
Stefani, D. D., Rizzuto, R., & Pozzan, T. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034216 · Cited by 424 · see citing works
The ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy
Gómez‐Suaga, P., Paillusson, S., Stoica, R., Noble, W. J., Hanger, D. P., & Miller, C. C. J. (2017) · Current Biology · doi:10.1016/j.cub.2016.12.038 · Cited by 413 · see citing works
ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules
Friedman, J. R., Webster, B. M., Mastronarde, D. N., Verhey, K. J., & Voeltz, G. K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911024 · Cited by 393 · see citing works
Bridging the gap: Membrane contact sites in signaling, metabolism, and organelle dynamics
Prinz, W. A. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201401126 · Cited by 391 · see citing works
The endoplasmic reticulum enzyme DGAT2 is found in mitochondria-associated membranes and has a mitochondrial targeting signal that promotes its association with mitochondria
Stone, S. J., Levin, M. C., Zhou, P., Han, J., Walther, T. C., & Farese, R. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805768200 · Cited by 390 · see citing works
Proteomic mapping of cytosol-facing outer mitochondrial and ER membranes in living human cells by proximity biotinylation
Hung, V., Lam, S. S., Udeshi, N. D., Svinkina, T., Guzman, G., Mootha, V. K., Carr, S. A., & Ting, A. Y. (2017) · eLife · doi:10.7554/elife.24463 · Cited by 378 · see citing works
Mitofusin 2-Containing Mitochondrial-Reticular Microdomains Direct Rapid Cardiomyocyte Bioenergetic Responses Via Interorganelle Ca 2+ Crosstalk
Chen, Y., Csordás, G., Jowdy, C. C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 348 · see citing works
Self-citation
A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division
Manor, U., Bartholomew, S. R., Golani, G., Christenson, E. T., Kozlov, M. M., Higgs, H. N., Spudich, J. A., & Lippincott‐Schwartz, J. (2015) · eLife · doi:10.7554/elife.08828 · Cited by 341 · see citing works
The Conserved GTPase Gem1 Regulates Endoplasmic Reticulum–Mitochondria Connections
Kornmann, B., Osman, C., & Walter, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111314108 · Cited by 335 · see citing works
Endoplasmic Reticulum Structure and Interconnections with Other OrganellesPreprint
English, A., & Voeltz, G. K. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013227 · Cited by 332 · see citing works
ER-Associated Mitochondrial Division Links the Distribution of Mitochondria and Mitochondrial DNA in Yeast
Murley, A., Lackner, L. L., Osman, C., West, M., Voeltz, G. K., Walter, P., & Nunnari, J. (2013) · eLife · doi:10.7554/elife.00422 · Cited by 326 · see citing works
VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria
Stefani, D. D., Bononi, A., Romagnoli, A., Messina, A. A., Pinto, V. D., Pinton, P., & Rizzuto, R. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.92 · Cited by 323 · see citing works
MAPL SUMOylation of Drp1 Stabilizes an ER/Mitochondrial Platform Required for Cell Death
Prudent, J., Zunino, R., Sugiura, A., Mattie, S., Shore, G. C., & McBride, H. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.001 · Cited by 321 · see citing works
Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer
Schauder, C. M., Wu, X., Saheki, Y., Narayanaswamy, P., Torta, F. T., Wenk, M. R., Camilli, P. V. D., & Reinisch, K. M. (2014) · Nature · doi:10.1038/nature13269 · Cited by 321 · see citing works
Binding of FUN14 domain containing 1 with inositol 1,4,5-trisphosphate receptor in mitochondria-associated endoplasmic reticulum membranes maintains mitochondrial dynamics and function in hearts in vivo
Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2017) · Circulation · doi:10.1161/circulationaha.117.030235 · Cited by 320 · see citing works
How mitochondrial dynamism orchestrates mitophagy
Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311 · see citing works
Redox Nanodomains Are Induced by and Control Calcium Signaling at the ER-Mitochondrial Interface
Booth, D. M., Enyedi, B., Geiszt, M., Várnai, P., & Hajnóczky, G. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.040 · Cited by 310 · see citing works
Self-citation
SR/ER–mitochondrial local communication: Calcium and ROS
Csordás, G., & Hajnóczky, G. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.06.004 · Cited by 309 · see citing works
Self-citation
A Conserved Endoplasmic Reticulum Membrane Protein Complex (EMC) Facilitates Phospholipid Transfer from the ER to Mitochondria
Lahiri, S., Chao, J. T., Tavassoli, S., Wong, A. K. O., Choudhary, V., Young, B. P., Loewen, C. J. R., & Prinz, W. A. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001969 · Cited by 306 · see citing works
MITOL Regulates Endoplasmic Reticulum-Mitochondria Contacts via Mitofusin2
Sugiura, A., Nagashima, S., Tokuyama, T., Amo, T., Matsuki, Y., Ishido, S., Kudo, Y., McBride, H. M., Fukuda, T., Matsushita, N., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.023 · Cited by 303 · see citing works
Mitochondria Are Linked to Calcium Stores in Striated Muscle by Developmentally Regulated Tethering Structures
Boncompagni, S., Rossi, A. E., Micaroni, M., Beznoussenko, G. V., Polishchuk, R., Dirksen, R. T., & Protasi, F. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0783 · Cited by 285 · see citing works
ORP5/ORP8 localize to endoplasmic reticulum–mitochondria contacts and are involved in mitochondrial function
Galmes, R., Houcine, A., van Vliet, A. R., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541108 · Cited by 281 · see citing works
The Type III Inositol 1,4,5-Trisphosphate Receptor Preferentially Transmits Apoptotic Ca2+ Signals into Mitochondria
Mendes, C. C. P., Gomes, D. A., Thompson, M., Souto, N. C., Góes, T. S., Goes, A. M., Rodrigues, M. Â., Gomez, M. V., Nathanson, M. H., & Leite, M. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506623200 · Cited by 270 · see citing works
ALS/FTD‐associated FUS activates GSK‐3β to disrupt the VAPB–PTPIP51 interaction and ER–mitochondria associations
Stoica, R., Paillusson, S., Gómez‐Suaga, P., Mitchell, J. C., Lau, D. H. W., Gray, E. H., Sancho, R. M., Vizcay‐Barrena, G., Vos, K. J. D., Shaw, C. E., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541726 · Cited by 254 · see citing works
In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM)
Poston, C. N., Krishnan, S. C., & Bazemore‐Walker, C. R. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2012.12.018 · Cited by 247 · see citing works
The intracellular redox state is a core determinant of mitochondrial fusion
Shutt, T. E., Geoffrion, M., Milne, R. W., & McBride, H. M. (2012) · EMBO Reports · doi:10.1038/embor.2012.128 · Cited by 243 · see citing works
Dynamic actin cycling through mitochondrial subpopulations locally regulates the fission–fusion balance within mitochondrial networks
Moore, A. S., Wong, Y., Simpson, C., & Holzbaur, E. (2016) · Nature Communications · doi:10.1038/ncomms12886 · Cited by 242 · see citing works
Three-dimensional electron microscopy reveals new details of membrane systems for Ca2+ signaling in the heart
Hayashi, T., Martone, M. E., Yu, Z., Thor, A., Doi, M., Holst, M., Ellisman, M. H., & Hoshijima, M. (2009) · Journal of Cell Science · doi:10.1242/jcs.028175 · Cited by 241 · see citing works
Propagation of the apoptotic signal by mitochondrial waves
Pacher, P., & Hajnóczky, G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4107 · Cited by 240 · see citing works
Self-citation
Cytosolic Phosphorylation of Calnexin Controls Intracellular Ca2+ Oscillations via an Interaction with Serca2b
Roderick, H. L., Lechleiter, J. D., & Camacho, P. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.6.1235 · Cited by 240 · see citing works
Activity of the mitochondrial calcium uniporter varies greatly between tissues
Fieni, F., Lee, S. B., Jan, Y. N., & Kirichok, Y. (2012) · Nature Communications · doi:10.1038/ncomms2325 · Cited by 231 · see citing works
Membrane Domains and the “Lipid Raft” Concept
Sonnino, S., & Prinetti, A. (2012) · Current Medicinal Chemistry · doi:10.2174/09298673130103 · Cited by 228 · see citing works
Mitofusin-2 Independent Juxtaposition of Endoplasmic Reticulum and Mitochondria: An Ultrastructural Study
Cosson, P., Marchetti, A., Ravazzola, M., & Orci, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046293 · Cited by 226 · see citing works
The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity to Control ER-Isolation Membrane Contacts for Autophagosome Formation
Zhao, Y. G., Chen, Y., Miao, G., Zhao, H., Qu, W., Li, D., Wang, Z., Liu, N., Li, L., Chen, S., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.005 · Cited by 226 · see citing works
Two-colour live-cell nanoscale imaging of intracellular targets
Bottanelli, F., Kromann, E. B., Allgeyer, E. S., Erdmann, R. S., Baguley, S. W., Sirinakis, G., Schepartz, A., Baddeley, D., Toomre, D. K., Rothman, J. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms10778 · Cited by 222 · see citing works
Palmitoylated TMX and calnexin target to the mitochondria‐associated membrane
Lynes, E. M., Bui, M., Yap, M. C., Benson, M. D., Schneider, B. L., Ellgaard, L., Berthiaume, L. G., & Simmen, T. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.384 · Cited by 220 · see citing works
Detergent-Resistant Microdomains Determine the Localization of σ-1 Receptors to the Endoplasmic Reticulum-Mitochondria Junction
Hayashi, T., & Fujimoto, M. (2010) · Molecular Pharmacology · doi:10.1124/mol.109.062539 · Cited by 219 · see citing works
Homology of SMP Domains to the TULIP Superfamily of Lipid-Binding Proteins Provides a Structural Basis for Lipid Exchange between ER and Mitochondria
Kopec, K. O., Alva, V., & Lupas, A. N. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq326 · Cited by 212 · see citing works
Transient assembly of F-actin on the outer mitochondrial membrane contributes to mitochondrial fission
Li, S., Xu, S., Roelofs, B. A., Boyman, L., Lederer, W. J., Sesaki, H., & Karbowski, M. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201404050 · Cited by 210 · see citing works
Ero1α Regulates Ca 2+ Fluxes at the Endoplasmic Reticulum–Mitochondria Interface (MAM)
Anelli, T., Bergamelli, L., Margittai, É., Rimessi, A., Fagioli, C., Malgaroli, A., Pinton, P., Ripamonti, M., Rizzuto, R., & Sitia, R. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4004 · Cited by 201 · see citing works
Mitochondria-associated membranes as hubs for neurodegeneration
Krols, M., Isterdael, G. V., Asselbergh, B., Kremer, A., Lippens, S., Timmerman, V., & Janssens, S. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1528-7 · Cited by 200 · see citing works
SLC25A46 is required for mitochondrial lipid homeostasis and cristae maintenance and is responsible for Leigh syndrome
Janer, A., Prudent, J., Paupe, V., Fahiminiya, S., Majewski, J., Sgarioto, N., Rosiers, C. D., Forest, A., Lin, Z., Gingras, A., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201506159 · Cited by 199 · see citing works
Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly
AhYoung, A. P., Jiang, J., Zhang, J., Dang, X. K., Loo, J. A., Zhou, Z. H., & Egea, P. F. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422363112 · Cited by 197 · see citing works
Peripheral ER structure and function
English, A., Zurek, N. A., & Voeltz, G. K. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.04.004 · Cited by 187 · see citing works
Transport of Ca2+ from Sarcoplasmic Reticulum to Mitochondria in Rat Ventricular Myocytes
Sharma, V. K., Ramesh, V., Franzini‐Armstrong, C., & Sheu, S. S. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005520714221 · Cited by 186 · see citing works
Interplay between hepatic mitochondria-associated membranes, lipid metabolism and caveolin-1 in mice
Sala‐Vila, A., Navarro‐Lérida, I., Sánchez‐Álvarez, M., Bosch, M., Calvo, C., López, J. A., Calvo, E., Ferguson, C., Giacomello, M., Serafini, A., et al. (2016) · Scientific Reports · doi:10.1038/srep27351 · Cited by 181 · see citing works
Redox controls UPR to control redox
Eletto, D., Chevet, É., Argon, Y., & Appenzeller‐Herzog, C. (2014) · Journal of Cell Science · doi:10.1242/jcs.153643 · Cited by 180 · see citing works
Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria.
Shore, G. C., & Tata, J. R. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.72.3.714 · Cited by 179 · see citing works
Palmitoylated calnexin is a key component of the ribosome–translocon complex
Lakkaraju, A. K., Abrami, L., Lemmin, T., Blašković, S., Kunz, B., Kihara, A., Peraro, M. D., & van der Goot, F. G. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.15 · Cited by 178 · see citing works
Rab32 Modulates Apoptosis Onset and Mitochondria-associated Membrane (MAM) Properties
Bui, M., Gilady, S. Y., Fitzsimmons, R., Benson, M. D., Lynes, E. M., Gesson, K., Alto, N. M., Strack, S., Scott, J. D., & Simmen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101584 · Cited by 177 · see citing works
Calcium Regulates the Association between Mitochondria and a Smooth Subdomain of the Endoplasmic Reticulum
Wang, H., Guay, G., Pogan, L., Sauvé, R., & Nabi, I. R. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1489 · Cited by 174 · see citing works
Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
Gilady, S. Y., Bui, M., Lynes, E. M., Benson, M. D., Watts, R., Vance, J. E., & Simmen, T. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0174-1 · Cited by 173 · see citing works
The AAA+ ATPase ATAD3A Controls Mitochondrial Dynamics at the Interface of the Inner and Outer Membranes
Gilquin, B., Taillebourg, E., Cherradi, N., Hubstenberger, A., Gay, O., Merle, N., Assard, N., Fauvarque, M.-O., Tomohiro, S., Kuge, O., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00007-10 · Cited by 171 · see citing works
Presenilin 2 Modulates Endoplasmic Reticulum-Mitochondria Coupling by Tuning the Antagonistic Effect of Mitofusin 2
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.013 · Cited by 170 · see citing works
Electron microscopic tomography of rat‐liver mitochondria and their interactions with the endoplasmic reticulum
Mannella, C. A., Buttle, K., Rath, B. K., & Marko, M. (1998) · BioFactors · doi:10.1002/biof.5520080309 · Cited by 167 · see citing works
TMX1 determines cancer cell metabolism as a thiol-based modulator of ER–mitochondria Ca2+ flux
Raturi, A., Gutiérrez, T., Ortiz-Sandoval, C. G., Ruangkittisakul, A., Herrera-Cruz, M. S., Rockley, J. P., Gesson, K., Ourdev, D., Lou, P., Lucchinetti, E., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201512077 · Cited by 149 · see citing works
Mitochondria-associated membrane formation in hormone-stimulated Leydig cell steroidogenesis: role of ATAD3
Issop, L., Fan, J., Lee, S., Rone, M. B., Basu, K., Mui, J., & Papadopoulos, V. (2015) · Endocrinology · doi:10.1210/en.2014-1503 · Cited by 147 · see citing works
Isoform- and Species-specific Control of Inositol 1,4,5-Trisphosphate (IP3) Receptors by Reactive Oxygen Species
Bánsághi, S., Golenár, T., Madesh, M., Csordás, G., RamachandraRao, S., Sharma, K., Yule, D. I., Joseph, S. K., & Hajnóczky, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.504159 · Cited by 145 · see citing works
Self-citation
FATE1 antagonizes calcium‐ and drug‐induced apoptosis by uncoupling ER and mitochondria
Doghman, M., Granatiero, V., Sbiera, S., Sbiera, I., Lacas‐Gervais, S., Brau, F., Faßnacht, M., Rizzuto, R., & Lalli, E. (2016) · EMBO Reports · doi:10.15252/embr.201541504 · Cited by 144 · see citing works
Palmitoylation is the Switch that Assigns Calnexin to Quality Control or ER Calcium Signaling
Lynes, E. M., Raturi, A., Shenkman, M., Sandoval, C. O., Yap, M. C., Wu, J., Janowicz, A., Myhill, N., Benson, M. D., Campbell, R. E., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.125856 · Cited by 143 · see citing works
The role of cholesterol in the association of endoplasmic reticulum membranes with mitochondria
Fujimoto, M., Hayashi, T., & Su, T.-P. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.12.022 · Cited by 140 · see citing works
Endoplasmic Reticulum-Mitochondria Communication Through Ca2+ Signaling: The Importance of Mitochondria-Associated Membranes (MAMs)
Marchi, S., Bittremieux, M., Missiroli, S., Morganti, C., Patergnani, S., Sbano, L., Rimessi, A., Kerkhofs, M., Parys, J. B., Bultynck, G., et al. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_4 · Cited by 138 · see citing works
Mitochondria Isolated from Rat Brown Adipose Tissue and Liver
Lever, J. D., & Chappell, J. (1958) · The Journal of Cell Biology · doi:10.1083/jcb.4.3.287 · Cited by 132 · see citing works
ROS Control Mitochondrial Motility through p38 and the Motor Adaptor Miro/Trak
Debattisti, V., Gerencser, A. A., Saotome, M., Das, S., & Hajnóczky, G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.060 · Cited by 132 · see citing works
Self-citation
Trichoplein/mitostatin regulates endoplasmic reticulum–mitochondria juxtaposition
Cerqua, C., Anesti, V., Pyakurel, A., Liu, D., Naón, D., Wiche, G., Baffa, R., Dimmer, K. S., & Scorrano, L. (2010) · EMBO Reports · doi:10.1038/embor.2010.151 · Cited by 129 · see citing works
Oxidative stress-induced mitochondrial fragmentation and movement in skeletal muscle myoblasts
Iqbal, S., & Hood, D. A. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00017.2014 · Cited by 129 · see citing works
Membrane Domains and the Lipid Raft Concept
Sonnino, S., & Prinetti, A. (2012) · Current Medicinal Chemistry · doi:10.2174/0929867311302010004 · Cited by 129 · see citing works
The Assembly of Calcium Release Units in Cardiac Muscle
Franzini‐Armstrong, C., Protasi, F., & Tijskens, P. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1341.007 · Cited by 127 · see citing works
Role of Mitofusin-2 in mitochondrial localization and calcium uptake in skeletal muscle
Ainbinder, A., Boncompagni, S., Protasi, F., & Dirksen, R. T. (2015) · Cell Calcium · doi:10.1016/j.ceca.2014.11.002 · Cited by 122 · see citing works
Proteomic Analysis of Mitochondrial-Associated ER Membranes (MAM) during RNA Virus Infection Reveals Dynamic Changes in Protein and Organelle Trafficking
Horner, S. M., Wilkins, C. R., Badil, S., Iskarpatyoti, J. A., & Gale, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117963 · Cited by 122 · see citing works
Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation cascade
Abrami, L., Dallavilla, T., Sandoz, P. A., Demir, M., Kunz, B., Savoglidis, G., Vassily Hatzimanikatis, A., & van der Goot, F. G. (2017) · eLife · doi:10.7554/elife.27826 · Cited by 121 · see citing works
Quantitative Proteomic Analyses of Human Cytomegalovirus-Induced Restructuring of Endoplasmic Reticulum-Mitochondrial Contacts at Late Times of Infection
Zhang, A., Williamson, C. D., Wong, D. S., Bullough, M. D., Brown, K. J., Hathout, Y., & Colberg‐Poley, A. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009936 · Cited by 119 · see citing works
Distinct mechanisms controlling rough and smooth endoplasmic reticulum-mitochondria contacts
Wang, P. T. C., Garcin, P. O., Fu, M., Masoudi, M., St-Pierre, P., Panté, N., & Nabi, I. R. (2015) · Journal of Cell Science · doi:10.1242/jcs.171132 · Cited by 111 · see citing works
ER–Mitochondria contact sites: A new regulator of cellular calcium flux comes into play
Krols, M., Bultynck, G., & Janssens, S. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201607124 · Cited by 111 · see citing works
A rapidly sedimenting fraction of rat liver endoplasmic reticulum
Lewis, J. A., & Tata, J. R. (1973) · Journal of Cell Science · doi:10.1242/jcs.13.2.447 · Cited by 107 · see citing works
Role for cER and Mmr1p in Anchorage of Mitochondria at Sites of Polarized Surface Growth in Budding Yeast
Swayne, T. C., Zhou, C. H., Boldogh, I. R., Charalel, J. K., McFaline-Figueroa, J. R., Thoms, S., Yang, C., Leung, G., McInnes, J., Erdmann, R., et al. (2011) · Current Biology · doi:10.1016/j.cub.2011.10.019 · Cited by 106 · see citing works
Coupling of ryanodine receptor 2 and voltage-dependent anion channel 2 is essential for Ca2+ transfer from the sarcoplasmic reticulum to the mitochondria in the heart
Min, C. K., Yeom, D. R., Lee, K., Kwon, H.-K., Kang, M., Kim, Y.-S., Park, Z., Jeon, H., & Kim, D. H. (2012) · Biochemical Journal · doi:10.1042/bj20120705 · Cited by 103 · see citing works
The Ryanodine Receptors Ca2 + Release Channels: Cellular Redox Sensors?
Hidalgo, C., Donoso, P., & Carrasco, M. A. (2005) · IUBMB Life · doi:10.1080/15216540500092328 · Cited by 102 · see citing works
DISC1-dependent Regulation of Mitochondrial Dynamics Controls the Morphogenesis of Complex Neuronal Dendrites
Norkett, R., Modi, S., Birsa, N., Atkin, T. A., Ivankovic, D., Pathania, M., Trossbach, S. V., Korth, C., Hirst, W. D., & Kittler, J. T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.699447 · Cited by 102 · see citing works
Analysis of ER-mitochondria contacts by correlative fluorescence microscopy and soft X-ray tomography of mammalian cells
Elgass, K., Smith, E. A., LeGros, M., Larabell, C. A., & Ryan, M. T. (2015) · Journal of Cell Science · doi:10.1242/jcs.169136 · Cited by 100 · see citing works
Sorting of calcium signals at the junctions of endoplasmic reticulum and mitochondria
Csordás, G., & Hajnóczky, G. (2001) · Cell Calcium · doi:10.1054/ceca.2000.0191 · Cited by 100 · see citing works
Self-citation
Hereditary spastic paraplegia‐linked REEP1 modulates endoplasmic reticulum/mitochondria contacts
Lim, Y., Cho, I., Schoel, L. J., Cho, G., & Golden, J. A. (2015) · Annals of Neurology · doi:10.1002/ana.24488 · Cited by 100 · see citing works
ATAD3 proteins: brokers of a mitochondria–endoplasmic reticulum connection in mammalian cells
Baudier, J. (2018) · Biological Reviews · doi:10.1111/brv.12373 · Cited by 99 · see citing works
Ascorbate peroxidase proximity labeling coupled with biochemical fractionation identifies promoters of endoplasmic reticulum–mitochondrial contacts
Cho, I., Adelmant, G., Lim, Y., Marto, J. A., Cho, G., & Golden, J. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.795286 · Cited by 89 · see citing works
Mitochondrial Ca2+ uptake by the voltage-dependent anion channel 2 regulates cardiac rhythmicity
Shimizu, H., Schredelseker, J., Huang, J., Lu, K., Naghdi, S., Lu, F., Franklin, S., Fiji, H. D. G., Wang, K., Zhu, H., et al. (2015) · eLife · doi:10.7554/elife.04801 · Cited by 88 · see citing works
Self-citation
Regulation of Calcium Fluxes by GPX8, a Type-II Transmembrane Peroxidase Enriched at the Mitochondria-Associated Endoplasmic Reticulum Membrane
Yoboue, E. D., Rimessi, A., Anelli, T., Pinton, P., & Sitia, R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6866 · Cited by 87 · see citing works
Comparative performance of airyscan and structured illumination superresolution microscopy in the study of the surface texture and 3D shape of pollen
Sivaguru, M., Urban, M. A., Fried, G., et al. (2016) · Microscopy Research and Technique · doi:10.1002/jemt.22732 · Cited by 86 · see citing works
A spastic paraplegia mouse model reveals REEP1-dependent ER shaping
Beetz, C., Koch, N., Khundadze, M., Zimmer‐Bensch, G., Nietzsche, S., Hertel, N., Huebner, A.-K., Mumtaz, R., Schweizer, M., Dirren, E., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65665 · Cited by 85 · see citing works
Simultaneous dual-color 3D STED microscopy
Osseforth, C., Moffitt, J. R., Schermelleh, L., et al. (2014) · Optics Express · doi:10.1364/oe.22.007028 · Cited by 84 · see citing works
Rapid degradation of mutant SLC25A46 by the ubiquitin-proteasome system results in MFN1/2-mediated hyperfusion of mitochondria
Steffen, J., Vashisht, A. A., Wan, J., Jen, J. C., Claypool, S. M., Wohlschlegel, J. A., & Koehler, C. M. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-07-0545 · Cited by 78 · see citing works
Flexible Architecture of IP3R1 by Cryo-EM
Ludtke, S. J., Tran, T. P., Ngo, Q. T., et al. (2011) · Structure · doi:10.1016/j.str.2011.05.003 · Cited by 77 · see citing works
Full-field dual-color 100-nm super-resolution imaging reveals organization and dynamics of mitochondrial and ER networks
Brunstein, M., Wicker, K., Hérault, K., et al. (2013) · Optics Express · doi:10.1364/oe.21.026162 · Cited by 74 · see citing works
IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, and by promoting ER-mitochondria contact
Bonneau, B., Ando, H., Kawaai, K., Hirose, M., Takahashi‐Iwanaga, H., & Mikoshiba, K. (2016) · eLife · doi:10.7554/elife.19896 · Cited by 72 · see citing works
Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels
Goetz, J. G., Genty, H., St-Pierre, P., Dang, T. T. P., Joshi, B., Sauvé, R., Vogl, A. W., & Nabi, I. R. (2007) · Journal of Cell Science · doi:10.1242/jcs.03486 · Cited by 66 · see citing works
Strategic Positioning and Biased Activity of the Mitochondrial Calcium Uniporter in Cardiac Muscle
de la Fuente, S., Fernández‐Sanz, C., Vail, C., Agra, E. J., Holmström, K. M., Sun, J., Mishra, J., Williams, D., Finkel, T., Murphy, E., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.755496 · Cited by 66 · see citing works
Self-citation
In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts
Sesaki, H., Adachi, Y., Kageyama, Y., Itoh, K., & Iijima, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.024 · Cited by 61 · see citing works
PTPIP51 regulates mouse cardiac ischemia/reperfusion through mediating the mitochondria-SR junction
Qiao, X., Shi, J. Y., Ye, J., Fang, X., Zhang, C., Cao, Y., Xu, C., Zhao, L., Zhu, Y., Wang, L., et al. (2017) · Scientific Reports · doi:10.1038/srep45379 · Cited by 61 · see citing works
Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
Tubbs, E., & Rieusset, J. (2016) · Journal of Visualized Experiments · doi:10.3791/54899 · Cited by 60 · see citing works
Mitochondrial contact sites as platforms for phospholipid exchange
Dimmer, K. S., & Rapaport, D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.07.010 · Cited by 56 · see citing works
Lipid synthesis and membrane contact sites: a crossroads for cellular physiology
Fernández-Murray, J. P., & McMaster, C. R. (2016) · Journal of Lipid Research · doi:10.1194/jlr.r070920 · Cited by 45 · see citing works
Alterations in Ca2+ Signalling via ER-Mitochondria Contact Site Remodelling in Cancer
Kerkhofs, M., Giorgi, C., Marchi, S., Seitaj, B., Parys, J. B., Pinton, P., Bultynck, G., & Bittremieux, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_17 · Cited by 42 · see citing works
Voltage-dependent anion channel 2 modulates resting Ca2+ sparks, but not action potential-induced Ca2+ signaling in cardiac myocytes
Subedi, K. P., Kim, J., Kang, M., et al. (2011) · Cell Calcium · doi:10.1016/j.ceca.2010.12.004 · Cited by 40 · see citing works
The Human Cytomegalovirus Protein UL37 Exon 1 Associates with Internal Lipid Rafts
Williamson, C. D., Zhang, A., & Colberg‐Poley, A. M. (2010) · Journal of Virology · doi:10.1128/jvi.01830-10 · Cited by 38 · see citing works
Personal recollections on the discovery of the ryanodine receptors of muscle
Fleischer, S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.119 · Cited by 35 · see citing works
Superresolution Imaging of Human Cytomegalovirus vMIA Localization in Sub-Mitochondrial Compartments
Bhuvanendran, S., Salka, K., Rainey, K. H., Sreetama, S. C., Williams, E. D., Leeker, M., Prasad, V., Boyd, J., Patterson, G. H., Jaiswal, J. K., et al. (2014) · Viruses · doi:10.3390/v6041612 · Cited by 30 · see citing works
Suppression of StarD7 promotes endoplasmic reticulum stress and induces ROS production
Flores‐Martín, J., Reyna, L., Ridano, M. E., Panzetta-Dutari, G. M., & Genti‐Raimondi, S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.08.023 · Cited by 29 · see citing works
Phylogenetic and Molecular Evolutionary Analysis of Mitophagy Receptors under Hypoxic Conditions
Wu, X., Wu, F.-H., Wu, Q.-R., Zhang, S., Chen, S., & Sima, M. W. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00539 · Cited by 29 · see citing works
Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail Anchor
Fueller, J., Egorov, M. V., Walther, K. A., Sabet, O., Mallah, J., Grabenbauer, M., & Kinkhabwala, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139429 · Cited by 21 · see citing works
Defining the Domain Arrangement of the Mammalian Target of Rapamycin Complex Component Rictor Protein
Zhou, P., Zhang, N., Nussinov, R., et al. (2015) · Journal of Computational Biology · doi:10.1089/cmb.2015.0103 · Cited by 21 · see citing works
Three-dimensional structure of recombinant type 1 inositol 1,4,5-trisphosphate receptor
Wolfram, F., Morris, E. P., & Taylor, C. W. (2010) · Biochemical Journal · doi:10.1042/bj20100143 · Cited by 19 · see citing works
PTPIP51—a myeloid lineage specific protein interacts with PTP1B in neutrophil granulocytes
Brobeil, A., Graf, M., Oeschger, S., et al. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.04.009 · Cited by 16 · see citing works
Membrane topology of human monoacylglycerol acyltransferase-2 and identification of regions important for its localization to the endoplasmic reticulum
McFie, P. J., Izzard, S., Vu, H., Jin, Y., Beauchamp, E., Berthiaume, L. G., & Stone, S. J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.06.021 · Cited by 5 · see citing works

Flagged first, then by citations

Sorted by citations

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Sies, H., Belousov, V. V., Chandel, N. S., Davies, M. J., Jones, D. P., Mann, G. E., Murphy, M. P., Yamamoto, M., & Winterbourn, C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00456-z · Cited by 1,735 · see citing works
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988 · see citing works
“In addition, endoplasmic reticulum (ER)-mitochondria contact sites provide a platform to regulate important cellular activities, including synthesis of phospholipids, calcium transport between ER and mitochondria, regulation of mitochondrial homeostasis, activation of inflammasome, and induction of apoptosis.(206,207)…”
Background
Microglia monitor and protect neuronal function through specialized somatic purinergic junctions
Cserép, C., Pósfai, B., Lénárt, N., Fekete, R., László, Z. I., Lele, Z., Orsolits, B., Molnár, G., Heindl, S., Schwarcz, A. D., et al. (2020) · Science · doi:10.1126/science.aax6752 · Cited by 684 · see citing works
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
Self-citation
Defective mitophagy in Alzheimer’s disease
Pradeepkiran, J. A., & Reddy, P. H. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101191 · Cited by 367 · see citing works
Shaping Neuronal Fate: Functional Heterogeneity of Direct Microglia-Neuron Interactions
Cserép, C., Pósfai, B., & Dénes, Á. (2021) · Neuron · doi:10.1016/j.neuron.2020.11.007 · Cited by 256 · see citing works
The roles of mitochondria in global and local intracellular calcium signalling
Cartes-Saavedra, B., Ghosh, A., & Hajnóczky, G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00820-1 · Cited by 126 · see citing works
Self-citation
Endoplasmic Reticulum Stress and the Unfolded Protein Response in Cerebral Ischemia/Reperfusion Injury
Wang, L., Liu, Y., Zhang, X., Ye, Y., Xiong, X., Zhang, S., Gu, L., Jian, Z., & Wang, H. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.864426 · Cited by 121 · see citing works
Nox4 regulates InsP3 receptor‐dependent Ca2+ release into mitochondria to promote cell survival
Beretta, M., Santos, C. X., Molenaar, C., Hafstad, A. D., Miller, C. C., Revazian, A., Betteridge, K., Schröder, K., Streckfuß‐Bömeke, K., Doroshow, J. H., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103530 · Cited by 93 · see citing works
Calcium, Bioenergetics, and Parkinson’s Disease
Zampese, E., & Surmeier, D. J. (2020) · Cells · doi:10.3390/cells9092045 · Cited by 79 · see citing works
Role of the Lipid Membrane and Membrane Proteins in Tau Pathology
Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61 · see citing works
Network Analysis of a Membrane-Enriched Brain Proteome across Stages of Alzheimer’s Disease
Higginbotham, L., Dammer, E., Duong, D., Modeste, E., Montine, T., Lah, J., Levey, A., & Seyfried, N. (2019) · Proteomes · doi:10.3390/proteomes7030030 · Cited by 32 · see citing works
Impaired aerobic capacity and premature fatigue preceding muscle weakness in the skeletal muscle Tfam-knockout mouse model
Chatel, B., Ducreux, S., Harhous, Z., Bendridi, N., Varlet, I., Ogier, A. C., Bernard, M., Gondin, J., Rieusset, J., Westerblad, H., et al. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.048981 · Cited by 8 · see citing works

Organization of transport from endoplasmic reticulum to Golgi in higher plants
Andreeva, A. V., Zheng, H., Saint‐Jore, C., et al. (2000) · Biochemical Society Transactions · doi:10.1042/bst0280505 · Cited by 60 · see citing works
The endoplasmic reticulum
Wang, Q., Smith, C. A., & Davis, E. (2013) · Oxford University Press eBooks · doi:10.1093/hesc/9780199697328.003.0008 · Cited by 8 · see citing works
Post-translational translocation into the endoplasmic reticulum
Johnson, N., Powis, K., & High, S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.12.008 · Cited by 118 · see citing works
A wound-inducible organelle derived from endoplasmic reticulum: a plant strategy against environmental stresses?
Hara‐Nishimura, I., & Matsushima, R. (2003) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2003.09.015 · Cited by 60 · see citing works
Exocyst and autophagy-related membrane trafficking in plants
Pečenková, T., Marković, V., Sabol, P., et al. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx363 · Cited by 62 · see citing works

Authors: Csordás, G., Weaver, D., & Hajnóczky, G.
Affiliations: Thomas Jefferson University (US)
Corresponding author: Csordás, György
Weaver, David
Hajnóczky, György
ORCID: Csordás, György
Hajnóczky, György
Venue: Trends in Cell Biology
Publisher: Elsevier BV
Published: 2018-07
Volume: 28
Issue: 7
Pages: 523-540
ISSN: 0962-8924 (ISSN-L)
DOI: 10.1016/j.tcb.2018.02.009
PMC: PMC6005738
OpenAlex: W2790109811
Cited by: 625
References: 160
Citations by year: 2026: 74 · 2025: 99 · 2024: 97 · 2023: 79 · 2022: 78 · 2021: 71 · 2020: 61 · 2019: 49 · 2018: 16 · 2017: 1
FWCI: 4.82
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Cell Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Heart, Lung, and Blood Institute (R01HL122124)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK051526)
National Institute of Environmental Health Sciences (R33ES025672, R21ES025672)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: endoplasmic reticulum-mitochondria contacts, lipid transfer, ion transfer, membrane dynamics, calcium signaling, reactive oxygen species signaling
MeSH terms: Animals, Calcium, Endoplasmic Reticulum, Humans, Mitochondria, Signal Transduction, Reactive Oxygen Species

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks