1 |
Bernhard, W., and Rouiller, C. (1956). Close topographical relationship between mitochondria and ergastoplasm of liver cells in a definite phase of cellular activity. J. Biophys. Biochem. Cytol. 2, 73-78.
DOI
|
2 |
Cali, T., Ottolini, D., Negro, A., and Brini, M. (2012). alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions. J. Biol. Chem. 287, 17914-17929.
DOI
|
3 |
Cheung, K.H., Shineman, D., Muller, M., Cardenas, C., Mei, L., Yang, J., Tomita, T., Iwatsubo, T., Lee, V.M., and Foskett, J.K. (2008). Mechanism of disruption in Alzheimer's disease by presenilin regulation of InsP3 receptor channel gating. Neuron 58, 871-883.
DOI
|
4 |
Matsuzaki, H., Fujimoto, T., Ota, T., Ogawa, M., Tsunoda, T., Doi, K., Hamabashiri, M., Tanaka, M., and Shirasawa, S. (2012). Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding protein in T and B lymphocytes. FEBS Open Bio. 2, 255-259.
DOI
|
5 |
Matsuzaki, H., Fujimoto, T., Tanaka, M., and Shirasawa, S. (2013). Tespa1 is a novel component of mitochondria-associated endoplasmic reticulum membranes and affects mitochondrial calcium flux. Biochem. Biophys. Res. Commun. 433, 322-326.
DOI
|
6 |
McCormack, J.G., and Denton, R.M. (1993). Mitochondrial transport and the role of intramitochondrial in the regulation of energy metabolism. Dev. Neurosci. 15, 165-173.
DOI
|
7 |
McLelland, G.L., Goiran, T., Yi, W., Dorval, G., Chen, C.X., Lauinger, N.D., Krahn, A.I., Valimehr, S., Rakovic, A., Rouiller, I., et al. (2018). Mfn2 ubiquitination by PINK1/parkin gates the p97-dependent release of ER from mitochondria to drive mitophagy. Elife 7.
|
8 |
Merkwirth, C., and Langer, T. (2008). Mitofusin 2 builds a bridge between ER and mitochondria. Cell 135, 1165-1167.
DOI
|
9 |
Wu, H., Carvalho, P., and Voeltz, G.K. (2018). Here, there, and everywhere: the importance of ER membrane contact sites. Science 361.
|
10 |
Wakana, Y., Takai, S., Nakajima, K.i., Tani, K., Yamamoto, A., Watson, P., Stephens, D.J., Hauri, H.P., Tagaya, M., and Linstedt, A. (2008). Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated degradation. Mol. Biol. Cell 19, 1825-1836.
DOI
|
11 |
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H., Li, S., et al. (2016). FUNDC1 regulates mitochondrial dynamics at the ER-mitochondrial contact site under hypoxic conditions. EMBO J. 35, 1368-1384.
DOI
|
12 |
Wu, Z., and Bowen, W.D. (2008). Role of sigma-1 receptor Cterminal segment in inositol 1,4,5-trisphosphate receptor activation: constitutive enhancement of calcium signaling in MCF-7 tumor cells. J. Biol. Chem. 283, 28198-28215.
DOI
|
13 |
Xu, H., Guan, N., Ren, Y.L., Wei, Q.J., Tao, Y.H., Yang, G.S., Liu, X.Y., Bu, D.F., Zhang, Y., and Zhu, S.N. (2018). IP3R-Grp75-VDAC1-MCU calcium regulation axis antagonists protect podocytes from apoptosis and decrease proteinuria in an Adriamycin nephropathy rat model. BMC Nephrol. 19, 140.
DOI
|
14 |
Copeland, D.E., and Dalton, A. J. (1959). An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost. J. Biophys. Biochem. Cytol. 5, 393-396.
DOI
|
15 |
Chung, J., Torta, F., Masai, K., Lucast, L., Czapla, H., Tanner, L.B., Narayanaswamy, P., Wenk, M.R., Nakatsu, F., and De Camilli, P. (2015). PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts. Science 349, 428-432.
|
16 |
Cipolat, S., Martins de Brito, O., Dal Zilio, B., and Scorrano, L. (2004). OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc. Natl. Acad. Sci. USA 101, 15927-15932.
DOI
|
17 |
Colombini, M. (2012). VDAC structure, selectivity, and dynamics. Biochim. Biophys. Acta. 1818, 1457-1465.
DOI
|
18 |
Csordas, G., Varnai, P., Golenar, T., Roy, S., Purkins, G., Schneider, T.G., Balla, T., and Hajnoczky, G. (2010). Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol. Cell 39, 121-132.
DOI
|
19 |
D'Angelo, G., Vicinanza, M., and De Matteis, M.A. (2008). Lipidtransfer proteins in biosynthetic pathways. Curr. Opin. Cell Biol. 20, 360-370.
DOI
|
20 |
Yu, C., Han, W., Shi, T., Lv, B., He, Q., Zhang, Y., Li, T., Zhang, Y., Song, Q., Wang, L., et al. (2008). PTPIP51, a novel 14-3-3 binding protein, regulates cell morphology and motility via Raf-ERK pathway. Cell Signal. 20, 2208-2220.
DOI
|
21 |
Zampese, E., Fasolato, C., Kipanyula, M.J., Bortolozzi, M., Pozzan, T., and Pizzo, P. (2011). Presenilin 2 modulates endoplasmic reticulum (ER)-mitochondria interactions and cross-talk. Proc. Natl. Acad. Sci. USA 108, 2777-2782.
DOI
|
22 |
Wadhwa, R., Taira, K., and Kaul, S.C. (2002). An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where? Cell Stress Chaperones. 7, 309.
DOI
|
23 |
Nguyen, M., Breckenridge, D.G., Ducret, A., and Shore, G.C. (2000). Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol. Biol. Cell 20, 6731-6740.
DOI
|
24 |
Mesmin, B., Bigay, J., Moser von Filseck, J., Lacas-Gervais, S., Drin, G., and Antonny, B. (2013). A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP. Cell 155, 830-843.
DOI
|
25 |
Mikoshiba, K. (2007). IP3 receptor/ channel: from discovery to new signaling concepts. J. Neurochem. 102, 1426-1446.
DOI
|
26 |
Myhill, N., Lynes, E.M., Nanji, J.A., Blagoveshchenskaya, A.D., Fei, H., Simmen, K.C., Cooper, T.J., Thomas, G., Simmen, T., and Linstedt, A. (2008). The subcellular distribution of calnexin is mediated by PACS-2. Mol. Biol. Cell 19, 2777-2788.
DOI
|
27 |
Patergnani, S., Suski, J.M., Agnoletto, C., Bononi, A., Bonora, M., De Marchi, E., Giorgi, C., Marchi, S., Missiroli, S., Poletti, F., et al. (2011). Calcium signaling around mitochondria associated membranes (MAMs). Cell Commun. Signal. 9, 19.
DOI
|
28 |
Nishimura, A.L., Mitne-Neto, M., Silva, H.C., Richieri-Costa, A., Middleton, S., Cascio, D., Kok, F., Oliveira, J.R., Gillingwater, T., Webb, J., et al. (2004). A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am. J. Hum. Genet. 75, 822-831.
DOI
|
29 |
O'Brien, R.J., and Wong, P.C. (2011). Amyloid precursor protein processing and Alzheimer's disease. Annu. Rev. Neurosci. 34, 185-204.
DOI
|
30 |
Ottolini, D., Cali, T., Negro, A., and Brini, M. (2013). The Parkinson disease-related protein DJ-1 counteracts mitochondrial impairment induced by the tumour suppressor protein p53 by enhancing endoplasmic reticulum-mitochondria tethering. Hum. Mol. Genet. 22, 2152-2168.
DOI
|
31 |
Detmer, S.A., and Chan, D.C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nat. Rev. Mol. Cell Biol. 8, 870-879.
DOI
|
32 |
Murphy, S.E., and Levine, T.P. (2016). VAP, a versatile access point for the endoplasmic reticulum: review and analysis of FFAT-like motifs in the VAPome. Biochim. Biophys. Acta. 1861, 952-961.
|
33 |
Das, A.M., and Harris, D.A. (1990). Control of mitochondrial ATP synthase in heart cells: inactive to active transitions caused by beating or positive inotropic agents. Cardiovasc. Res. 24, 411-417.
DOI
|
34 |
Davison, E.J., Pennington, K., Hung, C.-C., Peng, J., Rafiq, R., Ostareck-Lederer, A., Ostareck, D.H., Ardley, H.C., Banks, R.E., and Robinson, P.A. (2009). Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. PROTEOMICS 9, 4284-4297.
DOI
|
35 |
de Brito, O.M., and Scorrano, L. (2008). Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456, 605-610.
DOI
|
36 |
de Brito, O.M., and Scorrano, L. (2010). An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. EMBO J. 29, 2715-2723.
DOI
|
37 |
De Strooper, B. (2007). Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease. EMBO Rep. 8, 141-146.
DOI
|
38 |
De Vos, K.J., Morotz, G.M., Stoica, R., Tudor, E.L., Lau, K.F., Ackerley, S., Warley, A., Shaw, C.E., and Miller, C.C. (2012). VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis. Hum. Mol. Genet. 21, 1299-1311.
DOI
|
39 |
Eisenberg-Bord, M., Shai, N., Schuldiner, M., and Bohnert, M. (2016). A tether is a tether is a tether: tethering at membrane contact sites. Dev. Cell 39, 395-409.
DOI
|
40 |
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., and Pizzo, P. (2016). Presenilin 2 modulates endoplasmic reticulum-mitochodria coupling by tuning the antagonistic effect of mitofusin 2. Cell Rep. 15, 2226-2238.
DOI
|
41 |
Rostovtseva, T.K., Tan, W., and Colombini, M. (2005). On the role of VDAC in apoptosis: fact and fiction. J. Bioenerg. Biomembr. 37, 129-142.
DOI
|
42 |
Peretti, D., Dahan, N., Shimoni, E., Hirschberg, K., Lev, S., and Malhotra, V. (2008). Coordinated lipid transfer between the endoplasmic reticulum and the golgi complex requires the VAP proteins and is essential for golgi-mediated transport. Mol. Biol. Cell 19, 3871-3884.
DOI
|
43 |
Petronilli, V., Penzo, D., Scorrano, L., Bernardi, P., and Di Lisa, F. (2001). The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ. J. Biol. Chem. 276, 12030-12034.
DOI
|
44 |
Prinz, W.A. (2014). Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics. J. Cell Biol. 205, 759-769.
DOI
|
45 |
Raiborg, C., Wenzel, E.M., Pedersen, N.M., Olsvik, H., Schink, K.O., Schultz, S.W., Vietri, M., Nisi, V., Bucci, C., Brech, A., et al. (2015). Repeated ER-endosome contacts promote endosome translocation and neurite outgrowth. Nature 520, 234-238.
DOI
|
46 |
Rizzuto, R., Marchi, S., Bonora, M., Aguiari, P., Bononi, A., De Stefani, D., Giorgi, C., Leo, S., Rimessi, A., Siviero, R., et al. (2009). transfer from the ER to mitochondria: when, how and why. Biochim. Biophys. Acta. 1787, 1342-1351.
DOI
|
47 |
Rowland, A.A., Chitwood, P.J., Phillips, M.J., and Voeltz, G.K. (2014). ER contact sites define the position and timing of endosome fission. Cell 159, 1027-1041.
DOI
|
48 |
Rowland, A.A., and Voeltz, G.K. (2012). Endoplasmic reticulummitochondria contacts: function of the junction. Nat. Rev. Mol. Cell Biol. 13, 607-625.
DOI
|
49 |
Simmen, T., Aslan, J.E., Blagoveshchenskaya, A.D., Thomas, L., Wan, L., Xiang, Y., Feliciangeli, S.F., Hung, C.H., Crump, C.M., and Thomas, G. (2005). PACS‐2 controls endoplasmic reticulum–mitochondria communication and Bid‐mediated apoptosis. EMBO J. 24, 717-729.
DOI
|
50 |
Galmes, R., Houcine, A., van Vliet, A.R., Agostinis, P., Jackson, C.L., and Giordano, F. (2016). ORP5/ORP8 localize to endoplasmic reticulum-mitochondria contacts and are involved in mitochondrial function. EMBO Rep. 17, 800-810.
DOI
|
51 |
Stoica, R., De Vos, K.J., Paillusson, S., Mueller, S., Sancho, R.M., Lau, K.F., Vizcay-Barrena, G., Lin, W.L., Xu, Y.F., Lewis, J., et al. (2014). ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43. Nat. Commun. 5, 3996.
DOI
|
52 |
Harmon, M., Larkman, P., Hardingham, G., Jackson, M., and Skehel, P. (2017). A Bi-fluorescence complementation system to detect associations between the Endoplasmic reticulum and mitochondria. Sci. Rep. 7, 17467.
DOI
|
53 |
Gomez-Suaga, P., Paillusson, S., Stoica, R., Noble, W., Hanger, D.P., and Miller, C.C.J. (2017). The ER-mitochondria tethering complex VAPB-PTPIP51 regulates autophagy. Curr. Biol. 27, 371-385.
DOI
|
54 |
Guardia-Laguarta, C., Area-Gomez, E., Rub, C., Liu, Y., Magrane, J., Becker, D., Voos, W., Schon, E.A., and Przedborski, S. (2014). alpha-Synuclein is localized to mitochondria-associated ER membranes. J. Neurosci. 34, 249-259.
DOI
|
55 |
Hansford, R.G., and Zorov, D. (1998). Role of mitochondrial calcium transport in the control of substrate oxidation. Mol. Cell Biochem. 184, 359-369.
DOI
|
56 |
Haworth, R.A., and Hunter, D.R. (1979). The -induced membrane transition in mitochondria: II. Nature of the trigger site. Arch. Biochem. Biophys. 195, 460-467.
DOI
|
57 |
Hayashi, T., Rizzuto, R., Hajnoczky, G., and Su, T.P. (2009). MAM: more than just a housekeeper. Trends Cell Biol. 19, 81-88.
DOI
|
58 |
Hayashi, T., and Su, T.P. (2007). Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate signaling and cell survival. Cell 131, 596-610.
DOI
|
59 |
Hedskog, L., Pinho, C.M., Filadi, R., Ronnback, A., Hertwig, L., Wiehager, B., Larssen, P., Gellhaar, S., Sandebring, A., Westerlund, M., et al. (2013). Modulation of the endoplasmic reticulummitochondria interface in Alzheimer's disease and related models. Proc. Natl. Acad. Sci. USA 110, 7916-7921.
DOI
|
60 |
Stojanovski, D., Koutsopoulos, O.S., Okamoto, K., and Ryan, M.T. (2004). Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology. J. Cell Sci. 117, 1201-1210.
DOI
|
61 |
Stone, S.J., and Vance, J.E. (2000). Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J. Biol. Chem. 275, 34534-34540.
DOI
|
62 |
Su, T.P., Su, T.C., Nakamura, Y., and Tsai, S.Y. (2016). The sigma-1 receptor as a pluripotent modulator in living systems. Trends Pharmacol. Sci. 37, 262-278.
DOI
|
63 |
Szabadkai, G., Bianchi, K., Varnai, P., De Stefani, D., Wieckowski, M.R., Cavagna, D., Nagy, A.I., Balla, T., and Rizzuto, R. (2006). Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial channels. J. Cell Biol. 175, 901-911.
DOI
|
64 |
Van Laar, V.S., Roy, N., Liu, A., Rajprohat, S., Arnold, B., Dukes, A.A., Holbein, C.D., and Berman, S.B. (2015). Glutamate excitotoxicity in neurons triggers mitochondrial and endoplasmic reticulum accumulation of Parkin, and, in the presence of N-acetyl cysteine, mitophagy. Neurobiol. Dis. 74, 180-193.
DOI
|
65 |
Vance, J.E. (2014). MAM (mitochondria-associated membranes) in mammalian cells: lipids and beyond. Biochim. Biophys. Acta. 1841, 595-609.
DOI
|
66 |
Joseph, S.K., and Hajnoczky, G. (2007). IP3 receptors in cell survival and apoptosis: release and beyond. Apoptosis 12, 951-968.
DOI
|
67 |
Honrath, B., Metz, I., Bendridi, N., Rieusset, J., Culmsee, C., and Dolga, A.M. (2017). Glucose-regulated protein 75 determines ERmitochondrial coupling and sensitivity to oxidative stress in neuronal cells. Cell Death Discov. 3, 17076.
DOI
|
68 |
Hoppe, U.C. (2010). Mitochondrial calcium channels. FEBS Lett. 584, 1975-1981.
DOI
|
69 |
Iwasawa, R., Mahul-Mellier, A.L., Datler, C., Pazarentzos, E., and Grimm, S. (2011). Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction. EMBO J. 30, 556-568.
DOI
|
70 |
Kanekura, K., Nishimoto, I., Aiso, S., and Matsuoka, M. (2006). Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem. 281, 30223-30233.
DOI
|
71 |
Bernard-Marissal, N., Medard, J.J., Azzedine, H., and Chrast, R. (2015). Dysfunction in endoplasmic reticulum-mitochondria crosstalk underlies SIGMAR1 loss of function mediated motor neuron degeneration. Brain 138, 875-890.
DOI
|
72 |
Al-Saif, A., Al-Mohanna, F., and Bohlega, S. (2011). A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis. Ann. Neurol. 70, 913-919.
DOI
|
73 |
Area-Gomez, E., de Groof, A.J., Boldogh, I., Bird, T.D., Gibson, G.E., Koehler, C.M., Yu, W.H., Duff, K.E., Yaffe, M.P., Pon, L.A., et al. (2009). Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria. Am. J. Pathol. 175, 1810-1816.
DOI
|
74 |
Area-Gomez, E., Del Carmen Lara Castillo, M., Tambini, M.D., Guardia-Laguarta, C., de Groof, A.J., Madra, M., Ikenouchi, J., Umeda, M., Bird, T.D., Sturley, S.L., et al. (2012). Upregulated function of mitochondria-associated ER membranes in Alzheimer disease. EMBO J. 31, 4106-4123.
DOI
|
75 |
Liou, J., Fivaz, M., Inoue, T., and Meyer, T. (2007). Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after store depletion. Proc. Natl. Acad. Sci. USA 104, 9301-9306.
DOI
|
76 |
Kornmann, B., Currie, E., Collins, S.R., Schuldiner, M., Nunnari, J., Weissman, J.S., and Walter, P. (2009). An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325, 477-481.
DOI
|
77 |
Kroemer, G., Galluzzi, L., and Brenner, C. (2007). Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87, 99-163.
DOI
|
78 |
Liang, J., Lyu, J., Zhao, M., Li, D., Zheng, M., Fang, Y., Zhao, F., Lou, J., Guo, C., Wang, L., et al. (2017). Tespa1 regulates T cell receptorinduced calcium signals by recruiting inositol 1,4,5-trisphosphate receptors. Nat. Commun. 8, 15732.
DOI
|
79 |
Maries, E., Dass, B., Collier, T.J., Kordower, J.H., and Steece-Collier, K. (2003). The role of alpha-synuclein in Parkinson's disease: insights from animal models. Nat. Rev. Neurosci. 4, 727-738.
DOI
|
80 |
Marchi, S., and Pinton, P. (2014). The mitochondrial calcium uniporter complex: molecular components, structure and physiopathological implications. J. Physiol. 592, 829-839.
DOI
|
81 |
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C.A., Sou, Y.S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010). PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 189, 211-221.
DOI
|