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Volumn 108, Issue , 2012, Pages 131-145

Visualizing Mitochondrial Lipids and Fusion Events in Mammalian Cells

Author keywords

Cellular functioning; Dynamic organelle; Fission; Fusion; Mitochondria; Phospholipid

Indexed keywords


EID: 84863030606     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386487-1.00007-9     Document Type: Chapter
Times cited : (7)

References (51)
  • 1
    • 27644467457 scopus 로고    scopus 로고
    • Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae
    • Altmann K., Westermann B. Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell 2005, 16:5410-5417.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5410-5417
    • Altmann, K.1    Westermann, B.2
  • 2
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban T., et al. OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum. Mol. Genet. 2010, 19:2113-2122.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2113-2122
    • Ban, T.1
  • 3
    • 79952119926 scopus 로고    scopus 로고
    • Lipidomics profiling by high-resolution LC-MS and high-energy collisional dissociation fragmentation: focus on characterization of mitochondrial cardiolipins and monolysocardiolipins
    • Bird S.S., et al. Lipidomics profiling by high-resolution LC-MS and high-energy collisional dissociation fragmentation: focus on characterization of mitochondrial cardiolipins and monolysocardiolipins. Anal. Chem. 2011, 83:940-949.
    • (2011) Anal. Chem. , vol.83 , pp. 940-949
    • Bird, S.S.1
  • 4
    • 77958197158 scopus 로고    scopus 로고
    • Mitochondria and the culture of the Borg: understanding the integration of mitochondrial function within the reticulum, the cell, and the organism
    • Braschi E., McBride H.M. Mitochondria and the culture of the Borg: understanding the integration of mitochondrial function within the reticulum, the cell, and the organism. Bioessays 2010, 32:958-966.
    • (2010) Bioessays , vol.32 , pp. 958-966
    • Braschi, E.1    McBride, H.M.2
  • 5
    • 33750445482 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in mammals
    • Chan D.C. Mitochondrial fusion and fission in mammals. Ann. Rev. Cell Dev. Biol. 2006, 22:79-99.
    • (2006) Ann. Rev. Cell Dev. Biol. , vol.22 , pp. 79-99
    • Chan, D.C.1
  • 6
    • 77955287381 scopus 로고    scopus 로고
    • Physiological functions of mitochondrial fusion
    • Chen H., Chan D.C. Physiological functions of mitochondrial fusion. Ann. N. Y. Acad. Sci. 2010, 1201:21-25.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1201 , pp. 21-25
    • Chen, H.1    Chan, D.C.2
  • 7
    • 33750526473 scopus 로고    scopus 로고
    • A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis
    • Choi S.Y., et al. A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis. Nat. Cell Biol. 2006, 8:1255-1262.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1255-1262
    • Choi, S.Y.1
  • 8
    • 33847070746 scopus 로고    scopus 로고
    • Cardiolipin deficiency releases cytochrome c from the inner mitochondrial membrane and accelerates stimuli-elicited apoptosis
    • Choi S.Y., et al. Cardiolipin deficiency releases cytochrome c from the inner mitochondrial membrane and accelerates stimuli-elicited apoptosis. Cell Death Differ. 2007, 14:597-606.
    • (2007) Cell Death Differ. , vol.14 , pp. 597-606
    • Choi, S.Y.1
  • 9
    • 70349930116 scopus 로고    scopus 로고
    • Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion
    • DeVay R.M., et al. Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion. J. Cell Biol. 2009, 186:793-803.
    • (2009) J. Cell Biol. , vol.186 , pp. 793-803
    • DeVay, R.M.1
  • 10
    • 33847746323 scopus 로고    scopus 로고
    • A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production
    • Dries D.R., et al. A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production. J. Biol. Chem. 2007, 282:826-830.
    • (2007) J. Biol. Chem. , vol.282 , pp. 826-830
    • Dries, D.R.1
  • 11
    • 34548496498 scopus 로고    scopus 로고
    • Diacylglycerol is required for the formation of COPI vesicles in the Golgi-to-ER transport pathway
    • Fernandez-Ulibarri I., et al. Diacylglycerol is required for the formation of COPI vesicles in the Golgi-to-ER transport pathway. Mol. Biol. Cell 2007, 18:3250-3263.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3250-3263
    • Fernandez-Ulibarri, I.1
  • 12
    • 68949090311 scopus 로고    scopus 로고
    • Importance of lipid metabolism for intracellular and mitochondrial membrane fusion/fission processes
    • Furt F., Moreau P. Importance of lipid metabolism for intracellular and mitochondrial membrane fusion/fission processes. Int. J. Biochem. Cell Biol. 2009, 41:1828-1836.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1828-1836
    • Furt, F.1    Moreau, P.2
  • 13
    • 33750072605 scopus 로고    scopus 로고
    • Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling
    • Gallegos L.L., et al. Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling. J. Biol. Chem. 2006, 281:30947-30956.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30947-30956
    • Gallegos, L.L.1
  • 14
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • Gandre-Babbe S., van der Bliek A.M. The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 2008, 19:2402-2412.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    van der Bliek, A.M.2
  • 15
    • 72449137691 scopus 로고    scopus 로고
    • Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome
    • Gebert N., et al. Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome. Curr. Biol. 2009, 19:2133-2139.
    • (2009) Curr. Biol. , vol.19 , pp. 2133-2139
    • Gebert, N.1
  • 16
    • 33644981789 scopus 로고    scopus 로고
    • Increased membrane affinity of the C1 domain of protein kinase C delta compensates for the lack of involvement of its C2 domain in membrane recruitment
    • Giorgione J.R., et al. Increased membrane affinity of the C1 domain of protein kinase C delta compensates for the lack of involvement of its C2 domain in membrane recruitment. J. Biol. Chem. 2006, 281:1660-1669.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1660-1669
    • Giorgione, J.R.1
  • 17
    • 77955416276 scopus 로고    scopus 로고
    • A quantitative assay for mitochondrial fusion using Renilla luciferase complementation
    • Huang H., et al. A quantitative assay for mitochondrial fusion using Renilla luciferase complementation. Mitochondrion 2010, 10:559-566.
    • (2010) Mitochondrion , vol.10 , pp. 559-566
    • Huang, H.1
  • 18
    • 79952509006 scopus 로고    scopus 로고
    • PiRNA-associated germline nuage formation and spermatogenesis require MitoPLD pro-fusogenic mitochondrial-surface lipid signaling
    • Huang H., et al. piRNA-associated germline nuage formation and spermatogenesis require MitoPLD pro-fusogenic mitochondrial-surface lipid signaling. Dev. Cell 2011, 20:376-387.
    • (2011) Dev. Cell , vol.20 , pp. 376-387
    • Huang, H.1
  • 19
    • 19644377176 scopus 로고    scopus 로고
    • Insulin-stimulated plasma membrane fusion of Glut4 glucose transporter-containing vesicles is regulated by phospholipase D1
    • Huang P., et al. Insulin-stimulated plasma membrane fusion of Glut4 glucose transporter-containing vesicles is regulated by phospholipase D1. Mol. Biol. Cell 2005, 16:2614-2623.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2614-2623
    • Huang, P.1
  • 20
    • 34147172187 scopus 로고    scopus 로고
    • In vitro assays for mitochondrial fusion and division
    • Ingerman E., et al. In vitro assays for mitochondrial fusion and division. Methods Cell Biol. 2007, 80:707-720.
    • (2007) Methods Cell Biol. , vol.80 , pp. 707-720
    • Ingerman, E.1
  • 21
    • 78149407069 scopus 로고    scopus 로고
    • Mitochondrial fission and fusion and their roles in the heart
    • Kane L.A., Youle R.J. Mitochondrial fission and fusion and their roles in the heart. J. Mol. Med. 2010, 88:971-979.
    • (2010) J. Mol. Med. , vol.88 , pp. 971-979
    • Kane, L.A.1    Youle, R.J.2
  • 22
    • 58149308564 scopus 로고    scopus 로고
    • Membrane deformation under local pH gradient: mimicking mitochondrial cristae dynamics
    • Khalifat N., et al. Membrane deformation under local pH gradient: mimicking mitochondrial cristae dynamics. Biophys. J. 2008, 95:4924-4933.
    • (2008) Biophys. J. , vol.95 , pp. 4924-4933
    • Khalifat, N.1
  • 23
    • 77649268470 scopus 로고    scopus 로고
    • Organelle-specific, rapid induction of molecular activities and membrane tethering
    • Komatsu T., et al. Organelle-specific, rapid induction of molecular activities and membrane tethering. Nat. Methods 2010, 7:206-208.
    • (2010) Nat. Methods , vol.7 , pp. 206-208
    • Komatsu, T.1
  • 24
    • 3843075121 scopus 로고    scopus 로고
    • Structural basis of mitochondrial tethering by mitofusin complexes
    • Koshiba T., et al. Structural basis of mitochondrial tethering by mitofusin complexes. Science 2004, 305:858-862.
    • (2004) Science , vol.305 , pp. 858-862
    • Koshiba, T.1
  • 25
    • 0037974484 scopus 로고    scopus 로고
    • Membrane fission: model for intermediate structures
    • Kozlovsky Y., Kozlov M.M. Membrane fission: model for intermediate structures. Biophys. J. 2003, 85:85-96.
    • (2003) Biophys. J. , vol.85 , pp. 85-96
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 26
    • 78650987611 scopus 로고    scopus 로고
    • Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission
    • Mears J.A., et al. Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission. Nat. Struct. Mol. Biol. 2011, 18:20-26.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 20-26
    • Mears, J.A.1
  • 27
    • 65449184157 scopus 로고    scopus 로고
    • Monitoring mitochondrial dynamics with photoactivatable [corrected] green fluorescent protein
    • Molina A.J., Shirihai O.S. Monitoring mitochondrial dynamics with photoactivatable [corrected] green fluorescent protein. Methods Enzymol. 2009, 457:289-304.
    • (2009) Methods Enzymol. , vol.457 , pp. 289-304
    • Molina, A.J.1    Shirihai, O.S.2
  • 28
    • 77956634444 scopus 로고    scopus 로고
    • Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization
    • Montessuit S., et al. Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization. Cell 2010, 142:889-901.
    • (2010) Cell , vol.142 , pp. 889-901
    • Montessuit, S.1
  • 29
    • 1642546271 scopus 로고    scopus 로고
    • Positive and negative regulation of a SNARE protein by control of intracellular localization
    • Nakanishi H., et al. Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol. Biol. Cell 2004, 15:1802-1815.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1802-1815
    • Nakanishi, H.1
  • 30
    • 78149273391 scopus 로고    scopus 로고
    • Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Foster resonance energy transfer (FRET) biosensor
    • Nishioka T., et al. Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Foster resonance energy transfer (FRET) biosensor. J. Biol. Chem. 2010, 285:35979-35987.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35979-35987
    • Nishioka, T.1
  • 31
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari J., et al. Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 1997, 8:1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1
  • 32
    • 33745742425 scopus 로고    scopus 로고
    • Mitochondrial dynamics and disease, OPA1
    • Olichon A., et al. Mitochondrial dynamics and disease, OPA1. Biochim. Biophys. Acta 2006, 1763:500-509.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 500-509
    • Olichon, A.1
  • 33
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C., et al. Making heads or tails of phospholipids in mitochondria. J. Cell Biol. 2011, 192:7-16.
    • (2011) J. Cell Biol. , vol.192 , pp. 7-16
    • Osman, C.1
  • 34
    • 79952291364 scopus 로고    scopus 로고
    • Molecular mechanisms and physiologic functions of mitochondrial dynamics
    • Otera H., Mihara K. Molecular mechanisms and physiologic functions of mitochondrial dynamics. J. Biochem. 2011, 149:241-251.
    • (2011) J. Biochem. , vol.149 , pp. 241-251
    • Otera, H.1    Mihara, K.2
  • 35
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • Otera H., et al. Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 2010, 191:1141-1158.
    • (2010) J. Cell Biol. , vol.191 , pp. 1141-1158
    • Otera, H.1
  • 36
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras
    • Rizzo M.A., et al. The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 2000, 275:23911-23918.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23911-23918
    • Rizzo, M.A.1
  • 37
    • 70350418769 scopus 로고    scopus 로고
    • Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion
    • Rujiviphat J., et al. Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion. J. Biol. Chem. 2009, 284:28682-28686.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28682-28686
    • Rujiviphat, J.1
  • 38
    • 33748998746 scopus 로고    scopus 로고
    • Imaging diacylglycerol dynamics at organelle membranes
    • Sato M., et al. Imaging diacylglycerol dynamics at organelle membranes. Nat. Methods 2006, 3:797-799.
    • (2006) Nat. Methods , vol.3 , pp. 797-799
    • Sato, M.1
  • 39
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • Sekar R.B., Periasamy A. Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 2003, 160:629-633.
    • (2003) J. Cell Biol. , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 40
    • 62149152761 scopus 로고    scopus 로고
    • FIPI, a Phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis
    • Su W., et al. FIPI, a Phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis. Mol. Pharmacol. 2009, 75:437-446.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 437-446
    • Su, W.1
  • 41
    • 4644260485 scopus 로고    scopus 로고
    • Fluorescent biosensor for quantitative real-time measurements of inositol 1,4,5-trisphosphate in single living cells
    • Tanimura A., et al. Fluorescent biosensor for quantitative real-time measurements of inositol 1,4,5-trisphosphate in single living cells. J. Biol. Chem. 2004, 279:38095-38098.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38095-38098
    • Tanimura, A.1
  • 42
    • 25844499242 scopus 로고    scopus 로고
    • Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer
    • Thaler C., et al. Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer. Biophys. J. 2005, 89:2736-2749.
    • (2005) Biophys. J. , vol.89 , pp. 2736-2749
    • Thaler, C.1
  • 43
    • 33745714433 scopus 로고    scopus 로고
    • Tagging and tracking individual networks within a complex mitochondrial web with photoactivatable GFP
    • Twig G., et al. Tagging and tracking individual networks within a complex mitochondrial web with photoactivatable GFP. Am. J. Physiol. Cell Physiol. 2006, 291:C176-C184.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291
    • Twig, G.1
  • 44
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig G., et al. Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J. 2008, 27:433-446.
    • (2008) EMBO J. , vol.27 , pp. 433-446
    • Twig, G.1
  • 45
    • 1942487298 scopus 로고    scopus 로고
    • Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission
    • van Rheenen J., et al. Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission. Biophys. J. 2004, 86:2517-2529.
    • (2004) Biophys. J. , vol.86 , pp. 2517-2529
    • van Rheenen, J.1
  • 46
    • 33748333139 scopus 로고    scopus 로고
    • Live cell imaging of phosphoinositide dynamics with fluorescent protein domains
    • Varnai P., Balla T. Live cell imaging of phosphoinositide dynamics with fluorescent protein domains. Biochim. Biophys. Acta 2006, 1761:957-967.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 957-967
    • Varnai, P.1    Balla, T.2
  • 47
    • 33749527232 scopus 로고    scopus 로고
    • Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion
    • Vicogne J., et al. Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:14761-14766.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14761-14766
    • Vicogne, J.1
  • 48
    • 0035873494 scopus 로고    scopus 로고
    • Phospholipase D1: a key factor for the exocytotic machinery in neuroendocrine cells
    • Vitale N., et al. Phospholipase D1: a key factor for the exocytotic machinery in neuroendocrine cells. EMBO J. 2001, 20:2424-2434.
    • (2001) EMBO J. , vol.20 , pp. 2424-2434
    • Vitale, N.1
  • 49
    • 34247525092 scopus 로고    scopus 로고
    • A lethal defect of mitochondrial and peroxisomal fission
    • Waterham H.R., et al. A lethal defect of mitochondrial and peroxisomal fission. N. Engl. J. Med. 2007, 356:1736-1741.
    • (2007) N. Engl. J. Med. , vol.356 , pp. 1736-1741
    • Waterham, H.R.1
  • 50
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann B. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 2010, 11:872-884.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 872-884
    • Westermann, B.1
  • 51
    • 2442589922 scopus 로고    scopus 로고
    • Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
    • Zuchner S., et al. Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat. Genet. 2004, 36:449-451.
    • (2004) Nat. Genet. , vol.36 , pp. 449-451
    • Zuchner, S.1


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