메뉴 건너뛰기




Volumn 5, Issue 1, 2015, Pages

MIRO GTPases in mitochondrial transport, homeostasis and pathology

Author keywords

Milton; MIRO; Mitochondria; Mitochondrial transport; Small GTPases

Indexed keywords

CARRIER PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; GUANOSINE TRIPHOSPHATASE; MESYLIC ACID ETHYL ESTER; MITOCHONDRIAL DNA; MITOCHONDRIAL RHO GTPASE; NANOTUBE; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 85117875336     PISSN: None     EISSN: 20734409     Source Type: Journal    
DOI: 10.3390/cells5010001     Document Type: Review
Times cited : (44)

References (100)
  • 1
    • 84919371822 scopus 로고    scopus 로고
    • Eukaryotic origins: How and when was the mitochondrion acquired?
    • [CrossRef] [PubMed]
    • Poole, A.M.; Gribaldo, S. Eukaryotic origins: How and when was the mitochondrion acquired? Cold Spring Harb. Perspect. Biol. 2014, 6, a015990. [CrossRef] [PubMed]
    • (2014) Cold Spring Harb. Perspect. Biol , vol.6
    • Poole, A.M.1    Gribaldo, S.2
  • 2
    • 84923920171 scopus 로고    scopus 로고
    • The impact of mitochondrial endosymbiosis on the evolution of calcium signaling
    • [CrossRef] [PubMed]
    • Blackstone, N.W. The impact of mitochondrial endosymbiosis on the evolution of calcium signaling. Cell Calcium. 2015, 57, 133-139. [CrossRef] [PubMed]
    • (2015) Cell Calcium , vol.57 , pp. 133-139
    • Blackstone, N.W.1
  • 3
    • 84925397115 scopus 로고    scopus 로고
    • Molecular mechanism of mitochondrial calcium uptake
    • [CrossRef] [PubMed]
    • Wang, L.; Yang, X.; Shen, Y. Molecular mechanism of mitochondrial calcium uptake. Cell. Mol. Life Sci. 2015, 72, 1489-1498. [CrossRef] [PubMed]
    • (2015) Cell. Mol. Life Sci , vol.72 , pp. 1489-1498
    • Wang, L.1    Yang, X.2    Shen, Y.3
  • 4
    • 84929269425 scopus 로고    scopus 로고
    • Regulation of mitochondrial transport in neurons
    • [CrossRef] [PubMed]
    • Lin, M.Y.; Sheng, Z.H. Regulation of mitochondrial transport in neurons. Exp. Cell Res. 2015, 334, 35-44. [CrossRef] [PubMed]
    • (2015) Exp. Cell Res , vol.334 , pp. 35-44
    • Lin, M.Y.1    Sheng, Z.H.2
  • 5
    • 84937514988 scopus 로고    scopus 로고
    • Mitochondrial quality control pathways as determinants of metabolic health
    • [CrossRef] [PubMed]
    • Held, N.M.; Houtkooper, R.H. Mitochondrial quality control pathways as determinants of metabolic health. Bioessays 2015, 37, 867-876. [CrossRef] [PubMed]
    • (2015) Bioessays , vol.37 , pp. 867-876
    • Held, N.M.1    Houtkooper, R.H.2
  • 6
    • 84856710398 scopus 로고    scopus 로고
    • The Ras protein superfamily: Evolutionary tree and role of conserved amino acids
    • [CrossRef] [PubMed]
    • Rojas, A.M.; Fuentes, G.; Rausell, A.; Valencia, A. The Ras protein superfamily: Evolutionary tree and role of conserved amino acids. J. Cell Biol. 2012, 196, 189-201. [CrossRef] [PubMed]
    • (2012) J. Cell Biol , vol.196 , pp. 189-201
    • Rojas, A.M.1    Fuentes, G.2    Rausell, A.3    Valencia, A.4
  • 7
    • 84934443694 scopus 로고    scopus 로고
    • The Ras superfamily of small GTPases: The unlocked secrets
    • [PubMed]
    • Goitre, L.; Trapani, E.; Trabalzini, L.; Retta, S.F. The Ras superfamily of small GTPases: The unlocked secrets. Methods Mol. Biol. 2014, 1120, 1-18. [PubMed]
    • (2014) Methods Mol. Biol , vol.1120 , pp. 1-18
    • Goitre, L.1    Trapani, E.2    Trabalzini, L.3    Retta, S.F.4
  • 8
    • 16844387479 scopus 로고    scopus 로고
    • The Ras superfamily at a glance
    • [CrossRef] [PubMed]
    • Wennerberg, K.; Rossman, K.L.; Der, C.J. The Ras superfamily at a glance. J. Cell Sci. 2005, 118, 843-846. [CrossRef] [PubMed]
    • (2005) J. Cell Sci , vol.118 , pp. 843-846
    • Wennerberg, K.1    Rossman, K.L.2    Der, C.J.3
  • 9
    • 0037458579 scopus 로고    scopus 로고
    • Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis
    • [CrossRef] [PubMed]
    • Fransson, A.; Ruusala, A.; Aspenström, P. Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. J. Biol. Chem. 2003, 278, 6495-6502. [CrossRef] [PubMed]
    • (2003) J. Biol. Chem. , vol.278 , pp. 6495-6502
    • Fransson, A.1    Ruusala, A.2    Aspenström, P.3
  • 10
    • 79951672682 scopus 로고    scopus 로고
    • The Ras related GTPase Miro is not required for mitochondrial transport in Dictyostelium discoideum
    • [CrossRef] [PubMed]
    • Vlahou, G.; Eliáš, M.; von Kleist-Retzow, J.C.; Wiesner, R.J.; Rivero, F. The Ras related GTPase Miro is not required for mitochondrial transport in Dictyostelium discoideum. Eur. J. Cell Biol. 2011, 90, 342-355. [CrossRef] [PubMed]
    • (2011) Eur. J. Cell Biol , vol.90 , pp. 342-355
    • Vlahou, G.1    Eliáš, M.2    Von Kleist-Retzow, J.C.3    Wiesner, R.J.4    Rivero, F.5
  • 11
    • 5444257615 scopus 로고    scopus 로고
    • Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway
    • [CrossRef] [PubMed]
    • Frederick, R.L.; McCaffery, J.M.; Cunningham, K.W.; Okamoto, K.; Shaw, J.M. Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway. J. Cell Biol. 2004, 167, 87-98. [CrossRef] [PubMed]
    • (2004) J. Cell Biol , vol.167 , pp. 87-98
    • Frederick, R.L.1    McCaffery, J.M.2    Cunningham, K.W.3    Okamoto, K.4    Shaw, J.M.5
  • 12
    • 78650935783 scopus 로고    scopus 로고
    • Structure-function analysis of the yeast mitochondrial Rho GTPase, Gem1p: Implications for mitochondrial inheritance
    • [CrossRef] [PubMed]
    • Koshiba, T.; Holman, H.A.; Kubara, K.; Yasukawa, K.; Kawabata, S.I.; Okamoto, K.; MacFarlane, J.; Shaw, J.M. Structure-function analysis of the yeast mitochondrial Rho GTPase, Gem1p: Implications for mitochondrial inheritance. J. Biol. Chem. 2011, 286, 354-362. [CrossRef] [PubMed]
    • (2011) J. Biol. Chem , vol.286 , pp. 354-362
    • Koshiba, T.1    Holman, H.A.2    Kubara, K.3    Yasukawa, K.4    Kawabata, S.I.5    Okamoto, K.6    Macfarlane, J.7    Shaw, J.M.8
  • 14
    • 64549112144 scopus 로고    scopus 로고
    • Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking
    • [CrossRef] [PubMed]
    • Weihofen, A.; Thomas, K.J.; Ostaszewski, B.L.; Cookson, M.R.; Selkoe, D.J. Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 2009, 48, 2045-2052. [CrossRef] [PubMed]
    • (2009) Biochemistry , vol.48 , pp. 2045-2052
    • Weihofen, A.1    Thomas, K.J.2    Ostaszewski, B.L.3    Cookson, M.R.4    Selkoe, D.J.5
  • 15
    • 84901407276 scopus 로고    scopus 로고
    • Lysine 27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase
    • [CrossRef] [PubMed]
    • Birsa, N.; Norkett, R.; Wauer, T.; Mevissen, T.E.T.; Wu, H.C.; Foltynie, T.; Bhatia, K.; Hirst, W.D.; Komander, D.; Plun-Favreau, H.; et al. Lysine 27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase. J. Biol. Chem. 2014, 289, 14569-14582. [CrossRef] [PubMed]
    • (2014) J. Biol. Chem. , vol.289 , pp. 14569-14582
    • Birsa, N.1    Norkett, R.2    Wauer, T.3    Mevissen, T.E.T.4    Wu, H.C.5    Foltynie, T.6    Bhatia, K.7    Hirst, W.D.8    Komander, D.9    Plun-Favreau, H.10
  • 16
    • 84899454281 scopus 로고    scopus 로고
    • Phosphorylation of Parkin at Serine65 is essential for activation: Elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity
    • [CrossRef] [PubMed]
    • Kazlauskaite, A.; Kelly, V.; Johnson, C.; Baillie, C.; Hastie, C.J.; Peggie, M.; Macartney, T.; Woodroof, H.I.; Alessi, D.R.; Pedrioli, P.G.A.; et al. Phosphorylation of Parkin at Serine65 is essential for activation: Elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity. Open Biology 2014, 4, 130213. [CrossRef] [PubMed]
    • (2014) Open Biology , vol.4 , pp. 130213
    • Kazlauskaite, A.1    Kelly, V.2    Johnson, C.3    Baillie, C.4    Hastie, C.J.5    Peggie, M.6    Macartney, T.7    Woodroof, H.I.8    Alessi, D.R.9    Pedrioli, P.G.A.10
  • 17
    • 84979732912 scopus 로고    scopus 로고
    • The mitochondrial Ras-related GTPase Miro: Views from inside and outside the metazoan kingdom
    • [CrossRef] [PubMed]
    • Yamaoka, S.; Hara-Nishimura, I. The mitochondrial Ras-related GTPase Miro: Views from inside and outside the metazoan kingdom. Front. Plant Sci. 2014, 5, 350. [CrossRef] [PubMed]
    • (2014) Front. Plant Sci , vol.5 , pp. 350
    • Yamaoka, S.1    Hara-Nishimura, I.2
  • 18
    • 84887879281 scopus 로고    scopus 로고
    • Mitochondrial trafficking in neurons and the role of the Miro family of GTPase proteins
    • [CrossRef] [PubMed]
    • Birsa, N.; Norkett, R.; Higgs, N.; Lopez-Domenech, G.; Kittler, J.T. Mitochondrial trafficking in neurons and the role of the Miro family of GTPase proteins. Biochem. Soc. Trans. 2013, 41, 1525-1531. [CrossRef] [PubMed]
    • (2013) Biochem. Soc. Trans , vol.41 , pp. 1525-1531
    • Birsa, N.1    Norkett, R.2    Higgs, N.3    Lopez-Domenech, G.4    Kittler, J.T.5
  • 19
    • 84908376760 scopus 로고    scopus 로고
    • The myriad roles of Miro in the nervous system: Axonal transport of mitochondria and beyond
    • [CrossRef] [PubMed]
    • Lee, K.S.; Lu, B. The myriad roles of Miro in the nervous system: Axonal transport of mitochondria and beyond. Front. Cell. Neurosci. 2014, 8, 330. [CrossRef] [PubMed]
    • (2014) Front. Cell. Neurosci , vol.8 , pp. 330
    • Lee, K.S.1    Lu, B.2
  • 20
    • 0036149479 scopus 로고    scopus 로고
    • The EF-hand domain: A globally cooperative structural unit
    • [CrossRef] [PubMed]
    • Nelson, M.R.; Thulin, E.; Fagan, P.A.; Forsén, S.; Chazin, W.J. The EF-hand domain: A globally cooperative structural unit. Protein Sci. 2002, 11, 198-205. [CrossRef] [PubMed]
    • (2002) Protein Sci , vol.11 , pp. 198-205
    • Nelson, M.R.1    Thulin, E.2    Fagan, P.A.3    Forsén, S.4    Chazin, W.J.5
  • 21
    • 33646117742 scopus 로고    scopus 로고
    • The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking
    • [CrossRef] [PubMed]
    • Fransson, S.; Ruusala, A.; Aspenström, P. The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking. Biochem. Biophys. Res. Commun. 2006, 344, 500-510. [CrossRef] [PubMed]
    • (2006) Biochem. Biophys. Res. Commun , vol.344 , pp. 500-510
    • Fransson, S.1    Ruusala, A.2    Aspenström, P.3
  • 23
    • 84945414806 scopus 로고    scopus 로고
    • Characterization of the three zebrafish orthologs of the mitochondrial GTPase Miro/Rhot
    • [CrossRef] [PubMed]
    • Hollister, B.M.; Oonk, K.A.; Weiser, D.C.; Walsh, S. Characterization of the three zebrafish orthologs of the mitochondrial GTPase Miro/Rhot. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2015, 191, 126-134. [CrossRef] [PubMed]
    • (2015) Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.191 , pp. 126-134
    • Hollister, B.M.1    Oonk, K.A.2    Weiser, D.C.3    Walsh, S.4
  • 25
    • 60149097713 scopus 로고    scopus 로고
    • GTPase dependent recruitment of Grif-1 by Miro1 regulates mitochondrial trafficking in hippocampal neurons
    • [CrossRef] [PubMed]
    • MacAskill, A.F.; Brickley, K.; Stephenson, F.A.; Kittler, J.T. GTPase dependent recruitment of Grif-1 by Miro1 regulates mitochondrial trafficking in hippocampal neurons. Mol. Cell. Neurosci. 2009, 40, 301-312. [CrossRef] [PubMed]
    • (2009) Mol. Cell. Neurosci , vol.40 , pp. 301-312
    • Macaskill, A.F.1    Brickley, K.2    Stephenson, F.A.3    Kittler, J.T.4
  • 26
    • 58149091896 scopus 로고    scopus 로고
    • The mechanism of Ca2+ -dependent regulation of kinesin-mediated mitochondrial motility
    • [CrossRef] [PubMed]
    • Wang, X.; Schwarz, T.L. The mechanism of Ca2+ -dependent regulation of kinesin-mediated mitochondrial motility. Cell 2009, 136, 163-174. [CrossRef] [PubMed]
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 28
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex
    • [CrossRef] [PubMed]
    • Misko, A.; Jiang, S.; Wegorzewska, I.; Milbrandt, J.; Baloh, R.H. Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J. Neurosci. 2010, 30, 4232-4240. [CrossRef] [PubMed]
    • (2010) J. Neurosci , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 33
    • 67449124361 scopus 로고    scopus 로고
    • HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport
    • [CrossRef] [PubMed]
    • Li, Y.; Lim, S.; Hoffman, D.; Aspenstrom, P.; Federoff, H.J.; Rempe, D.A. HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport. J. Cell Biol. 2009, 185, 1065-1081. [CrossRef] [PubMed]
    • (2009) J. Cell Biol , vol.185 , pp. 1065-1081
    • Li, Y.1    Lim, S.2    Hoffman, D.3    Aspenstrom, P.4    Federoff, H.J.5    Rempe, D.A.6
  • 34
    • 74549168044 scopus 로고    scopus 로고
    • During hypoxia, HUMMR joins the mitochondrial dance
    • [CrossRef] [PubMed]
    • Li, Y.; Rempe, D.A. During hypoxia, HUMMR joins the mitochondrial dance. Cell Cycle 2010, 9, 50-57. [CrossRef] [PubMed]
    • (2010) Cell Cycle , vol.9 , pp. 50-57
    • Li, Y.1    Rempe, D.A.2
  • 35
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulummitochondria connections
    • [CrossRef] [PubMed]
    • Kornmann, B.; Osman, C.; Walter, P. The conserved GTPase Gem1 regulates endoplasmic reticulummitochondria connections. Proc. Natl. Acad. Sci. USA 2011, 108, 14151-14156. [CrossRef] [PubMed]
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14151-14156
    • Kornmann, B.1    Osman, C.2    Walter, P.3
  • 36
    • 84879059164 scopus 로고    scopus 로고
    • ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast
    • [CrossRef] [PubMed]
    • Murley, A.; Lackner, L.L.; Osman, C.; West, M.; Voeltz, G.K.; Walter, P.; Nunnari, J. ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. Elife 2013, 2, e00422. [CrossRef] [PubMed]
    • (2013) Elife , vol.2
    • Murley, A.1    Lackner, L.L.2    Osman, C.3    West, M.4    Voeltz, G.K.5    Walter, P.6    Nunnari, J.7
  • 38
    • 84865961091 scopus 로고    scopus 로고
    • Synaptic energy use and supply
    • [CrossRef] [PubMed]
    • Harris, J.J.; Jolivet, R.; Attwell, D. Synaptic energy use and supply. Neuron 2012, 75, 762-777. [CrossRef] [PubMed]
    • (2012) Neuron , vol.75 , pp. 762-777
    • Harris, J.J.1    Jolivet, R.2    Attwell, D.3
  • 39
    • 84937764107 scopus 로고    scopus 로고
    • Mitochondrial dynamics and inherited peripheral nerve diseases
    • [CrossRef] [PubMed]
    • Pareyson, D.; Saveri, P.; Sagnelli, A.; Piscosquito, G. Mitochondrial dynamics and inherited peripheral nerve diseases. Neurosci. Lett. 2015, 596, 66-77. [CrossRef] [PubMed]
    • (2015) Neurosci. Lett , vol.596 , pp. 66-77
    • Pareyson, D.1    Saveri, P.2    Sagnelli, A.3    Piscosquito, G.4
  • 40
    • 84872833228 scopus 로고    scopus 로고
    • Mitochondrial dynamics in neurodegeneration
    • [CrossRef] [PubMed]
    • Itoh, K.; Nakamura, K.; Iijima, M.; Sesaki, H. Mitochondrial dynamics in neurodegeneration. Trends Cell Biol. 2013, 23, 64-71. [CrossRef] [PubMed]
    • (2013) Trends Cell Biol , vol.23 , pp. 64-71
    • Itoh, K.1    Nakamura, K.2    Iijima, M.3    Sesaki, H.4
  • 42
    • 84936994657 scopus 로고    scopus 로고
    • Axonal transport defects in Alzheimer’s disease
    • [CrossRef] [PubMed]
    • Wang, Z.X.; Tan, L.; Yu, J.T. Axonal transport defects in Alzheimer’s disease. Mol. Neurobiol. 2015, 51, 1309-1321. [CrossRef] [PubMed]
    • (2015) Mol. Neurobiol , vol.51 , pp. 1309-1321
    • Wang, Z.X.1    Tan, L.2    Yu, J.T.3
  • 43
    • 84897567836 scopus 로고    scopus 로고
    • Mitochondrial trafficking and anchoring in neurons: New insight and implications
    • [CrossRef] [PubMed]
    • Sheng, Z.H. Mitochondrial trafficking and anchoring in neurons: New insight and implications. J. Cell Biol. 2014, 204, 1087-1098. [CrossRef] [PubMed]
    • (2014) J. Cell Biol , vol.204 , pp. 1087-1098
    • Sheng, Z.H.1
  • 45
    • 0037137704 scopus 로고    scopus 로고
    • Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein
    • [CrossRef]
    • Stowers, R.S.; Megeath, L.J.; Górska-Andrzejak, J.; Meinertzhagen, I.A.; Schwarz, T.L. Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein. Neuron 2002, 36, 1063-1077. [CrossRef]
    • (2002) Neuron , vol.36 , pp. 1063-1077
    • Stowers, R.S.1    Megeath, L.J.2    Górska-Andrzejak, J.3    Meinertzhagen, I.A.4    Schwarz, T.L.5
  • 46
    • 33646768127 scopus 로고    scopus 로고
    • Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent
    • [CrossRef] [PubMed]
    • Glater, E.E.; Megeath, L.J.; Stowers, R.S.; Schwarz, T.L. Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. J. Cell Biol. 2006, 173, 545-557. [CrossRef] [PubMed]
    • (2006) J. Cell Biol , vol.173 , pp. 545-557
    • Glater, E.E.1    Megeath, L.J.2    Stowers, R.S.3    Schwarz, T.L.4
  • 48
    • 37749053855 scopus 로고    scopus 로고
    • Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation
    • [CrossRef] [PubMed]
    • Kang, J.S.; Tian, J.H.; Pan, P.Y.; Zald, P.; Li, C.; Deng, C.; Sheng, Z.H. Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation. Cell 2008, 132, 137-148. [CrossRef] [PubMed]
    • (2008) Cell , vol.132 , pp. 137-148
    • Kang, J.S.1    Tian, J.H.2    Pan, P.Y.3    Zald, P.4    Li, C.5    Deng, C.6    Sheng, Z.H.7
  • 49
    • 84880806405 scopus 로고    scopus 로고
    • Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport
    • [CrossRef] [PubMed]
    • Chen, Y.; Sheng, Z.H. Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport. J. Cell Biol. 2013, 202, 351-364. [CrossRef] [PubMed]
    • (2013) J. Cell Biol , vol.202 , pp. 351-364
    • Chen, Y.1    Sheng, Z.H.2
  • 50
    • 65649107618 scopus 로고    scopus 로고
    • Drosophila Miro is required for both anterograde and retrograde axonal mitochondrial transport
    • [CrossRef] [PubMed]
    • Russo, G.J.; Louie, K.; Wellington, A.; Macleod, G.T.; Hu, F.; Panchumarthi, S.; Zinsmaier, K.E. Drosophila Miro is required for both anterograde and retrograde axonal mitochondrial transport. J. Neurosci. 2009, 29, 5443-5455. [CrossRef] [PubMed]
    • (2009) J. Neurosci. , vol.29 , pp. 5443-5455
    • Russo, G.J.1    Louie, K.2    Wellington, A.3    Macleod, G.T.4    Hu, F.5    Panchumarthi, S.6    Zinsmaier, K.E.7
  • 51
    • 84929353448 scopus 로고    scopus 로고
    • Miro’s N-terminal GTPase domain is required for transport of mitochondria into axons and dendrites
    • [CrossRef] [PubMed]
    • Babic, M.; Russo, G.J.; Wellington, A.J.; Sangston, R.M.; Gonzalez, M.; Zinsmaier, K.E. Miro’s N-terminal GTPase domain is required for transport of mitochondria into axons and dendrites. J. Neurosci. 2015, 35, 5754-5771. [CrossRef] [PubMed]
    • (2015) J. Neurosci. , vol.35 , pp. 5754-5771
    • Babic, M.1    Russo, G.J.2    Wellington, A.J.3    Sangston, R.M.4    Gonzalez, M.5    Zinsmaier, K.E.6
  • 53
    • 34447540081 scopus 로고    scopus 로고
    • Disrupted-in-schizophrenia-1 (DISC1): A key susceptibility factor for major mental illnesses
    • [CrossRef] [PubMed]
    • Sawamura, N.; Sawa, A. Disrupted-in-schizophrenia-1 (DISC1): A key susceptibility factor for major mental illnesses. Ann. N. Y. Acad. Sci. 2006, 1086, 126-133. [CrossRef] [PubMed]
    • (2006) Ann. N. Y. Acad. Sci , vol.1086 , pp. 126-133
    • Sawamura, N.1    Sawa, A.2
  • 54
    • 79151471696 scopus 로고    scopus 로고
    • Disrupted in Schizophrenia-1 regulates intracellular trafficking of mitochondria in neurons
    • [CrossRef] [PubMed]
    • Atkin, T.A.; MacAskill, A.F.; Brandon, N.J.; Kittler, J.T. Disrupted in Schizophrenia-1 regulates intracellular trafficking of mitochondria in neurons. Mol. Psychiatry 2011, 16, 122-124. [CrossRef] [PubMed]
    • (2011) Mol. Psychiatry , vol.16 , pp. 122-124
    • Atkin, T.A.1    Macaskill, A.F.2    Brandon, N.J.3    Kittler, J.T.4
  • 55
    • 84864501555 scopus 로고    scopus 로고
    • A t(1;11) translocation linked to schizophrenia and affective disorders gives rise to aberrant chimeric DISC1 transcripts that encode structurally altered, deleterious mitochondrial proteins
    • [CrossRef] [PubMed]
    • Eykelenboom, J.E.; Briggs, G.J.; Bradshaw, N.J.; Soares, D.C.; Ogawa, F.; Christie, S.; Malavasi, E.L.V.; Makedonopoulou, P.; Mackie, S.; Malloy, M.P.; et al. A t(1;11) translocation linked to schizophrenia and affective disorders gives rise to aberrant chimeric DISC1 transcripts that encode structurally altered, deleterious mitochondrial proteins. Hum. Mol. Genet. 2012, 21, 3374-3386. [CrossRef] [PubMed]
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3374-3386
    • Eykelenboom, J.E.1    Briggs, G.J.2    Bradshaw, N.J.3    Soares, D.C.4    Ogawa, F.5    Christie, S.6    Malavasi, E.L.V.7    Makedonopoulou, P.8    Mackie, S.9    Malloy, M.P.10
  • 56
    • 84930507352 scopus 로고    scopus 로고
    • Boymaw, overexpressed in brains with major psychiatric disorders, may encode a small protein to inhibit mitochondrial function and protein translation
    • [CrossRef] [PubMed]
    • Ji, B.; Kim, M.; Higa, K.K.; Zhou, X. Boymaw, overexpressed in brains with major psychiatric disorders, may encode a small protein to inhibit mitochondrial function and protein translation. Am. J. Med. Genet. B Neuropsychiatr. Genet. 2015, 168B, 284-295. [CrossRef] [PubMed]
    • (2015) Am. J. Med. Genet. B Neuropsychiatr. Genet , vol.168B , pp. 284-295
    • Ji, B.1    Kim, M.2    Higa, K.K.3    Zhou, X.4
  • 57
    • 84899860563 scopus 로고    scopus 로고
    • Miro1: New wheels for transferring mitochondria
    • [CrossRef] [PubMed]
    • Las, G.; Shirihai, O.S. Miro1: New wheels for transferring mitochondria. EMBO J. 2014, 33, 939-941. [CrossRef] [PubMed]
    • (2014) EMBO J , vol.33 , pp. 939-941
    • Las, G.1    Shirihai, O.S.2
  • 58
    • 84861361400 scopus 로고    scopus 로고
    • Wiring through tunneling nanotubes—From electrical signals to organelle transfer
    • [CrossRef] [PubMed]
    • Abounit, S.; Zurzolo, C. Wiring through tunneling nanotubes—From electrical signals to organelle transfer. J. Cell Sci. 2012, 125, 1089-1098. [CrossRef] [PubMed]
    • (2012) J. Cell Sci , vol.125 , pp. 1089-1098
    • Abounit, S.1    Zurzolo, C.2
  • 59
    • 84879841478 scopus 로고    scopus 로고
    • Tunneling nanotubes, an emerging intercellular communication route in development
    • [CrossRef] [PubMed]
    • Gerdes, H.H.; Rustom, A.; Wang, X. Tunneling nanotubes, an emerging intercellular communication route in development. Mech. Dev. 2013, 130, 381-387. [CrossRef] [PubMed]
    • (2013) Mech. Dev , vol.130 , pp. 381-387
    • Gerdes, H.H.1    Rustom, A.2    Wang, X.3
  • 60
    • 84892146772 scopus 로고    scopus 로고
    • Mesenchymal stem cells: Environmentally responsive therapeutics for regenerative medicine
    • [CrossRef] [PubMed]
    • Murphy, M.B.; Moncivais, K.; Caplan, A.I. Mesenchymal stem cells: Environmentally responsive therapeutics for regenerative medicine. Exp. Mol. Med. 2013, 45, e54. [CrossRef] [PubMed]
    • (2013) Exp. Mol. Med , vol.45
    • Murphy, M.B.1    Moncivais, K.2    Caplan, A.I.3
  • 61
    • 84939893615 scopus 로고    scopus 로고
    • A systematic review of preclinical studies on the therapeutic potential of mesenchymal stromal cell-derived microvesicles
    • [CrossRef] [PubMed]
    • Akyurekli, C.; Le, Y.; Richardson, R.B.; Fergusson, D.; Tay, J.; Allan, D.S. A systematic review of preclinical studies on the therapeutic potential of mesenchymal stromal cell-derived microvesicles. Stem Cell. Rev. 2015, 11, 150-160. [CrossRef] [PubMed]
    • (2015) Stem Cell. Rev , vol.11 , pp. 150-160
    • Akyurekli, C.1    Le, Y.2    Richardson, R.B.3    Fergusson, D.4    Tay, J.5    Allan, D.S.6
  • 62
    • 84889098431 scopus 로고    scopus 로고
    • Nanotubular crosstalk with distressed cardiomyocytes stimulates the paracrine repair function of mesenchymal stem cells
    • [CrossRef] [PubMed]
    • Figeac, F.; Lesault, P.F.; Le Coz, O.; Damy, T.; Souktani, R.; Trébeau, C.; Schmitt, A.; Ribot, J.; Mounier, R.; Guguin, A.; et al. Nanotubular crosstalk with distressed cardiomyocytes stimulates the paracrine repair function of mesenchymal stem cells. Stem Cells 2014, 32, 216-230. [CrossRef] [PubMed]
    • (2014) Stem Cells , vol.32 , pp. 216-230
    • Figeac, F.1    Lesault, P.F.2    Le Coz, O.3    Damy, T.4    Souktani, R.5    Trébeau, C.6    Schmitt, A.7    Ribot, J.8    Mounier, R.9    Guguin, A.10
  • 63
    • 84934958162 scopus 로고    scopus 로고
    • Lipid droplets as a novel cargo of tunnelling nanotubes in endothelial cells
    • [CrossRef] [PubMed]
    • Astanina, K.; Koch, M.; Jüngst, C.; Zumbusch, A.; Kiemer, A.K. Lipid droplets as a novel cargo of tunnelling nanotubes in endothelial cells. Sci. Rep. 2015, 5, 11453. [CrossRef] [PubMed]
    • (2015) Sci. Rep , vol.5 , pp. 11453
    • Astanina, K.1    Koch, M.2    Jüngst, C.3    Zumbusch, A.4    Kiemer, A.K.5
  • 64
    • 81055149523 scopus 로고    scopus 로고
    • Tunneling nanotubes mediate rescue of prematurely senescent endothelial cells by endothelial progenitors: Exchange of lysosomal pool
    • [PubMed]
    • Yasuda, K.; Khandare, A.; Burianovskyy, L.; Maruyama, S.; Zhang, F.; Nasjletti, A.; Goligorsky, M.S. Tunneling nanotubes mediate rescue of prematurely senescent endothelial cells by endothelial progenitors: Exchange of lysosomal pool. Aging 2011, 3, 597-608. [PubMed]
    • (2011) Aging , vol.3 , pp. 597-608
    • Yasuda, K.1    Khandare, A.2    Burianovskyy, L.3    Maruyama, S.4    Zhang, F.5    Nasjletti, A.6    Goligorsky, M.S.7
  • 66
    • 79959583875 scopus 로고    scopus 로고
    • Intercellular communication by exchange of cytoplasmic material via tunneling nano-tube like structures in primary human renal epithelial cells
    • [CrossRef] [PubMed]
    • Domhan, S.; Ma, L.; Tai, A.; Anaya, Z.; Beheshti, A.; Zeier, M.; Hlatky, L.; Abdollahi, A. Intercellular communication by exchange of cytoplasmic material via tunneling nano-tube like structures in primary human renal epithelial cells. PLoS ONE 2011, 6, e21283. [CrossRef] [PubMed]
    • (2011) Plos ONE , vol.6
    • Domhan, S.1    Ma, L.2    Tai, A.3    Anaya, Z.4    Beheshti, A.5    Zeier, M.6    Hlatky, L.7    Abdollahi, A.8
  • 67
    • 84930759485 scopus 로고    scopus 로고
    • Transfer of mitochondria via tunneling nanotubes rescues apoptotic PC12 cells
    • [CrossRef] [PubMed]
    • Wang, X.; Gerdes, H.H. Transfer of mitochondria via tunneling nanotubes rescues apoptotic PC12 cells. Cell Death Differ. 2015, 22, 1181-1191. [CrossRef] [PubMed]
    • (2015) Cell Death Differ , vol.22 , pp. 1181-1191
    • Wang, X.1    Gerdes, H.H.2
  • 68
    • 84866322157 scopus 로고    scopus 로고
    • Intercellular organelle trafficking by membranous nanotube connections: A possible new role in cellular rejuvenation?
    • [CrossRef] [PubMed]
    • Lim, Y.S.; Tang, B.L. Intercellular organelle trafficking by membranous nanotube connections: A possible new role in cellular rejuvenation? Cell Commun. Adhes. 2012, 19, 39-44. [CrossRef] [PubMed]
    • (2012) Cell Commun. Adhes. , vol.19 , pp. 39-44
    • Lim, Y.S.1    Tang, B.L.2
  • 69
    • 84895930290 scopus 로고    scopus 로고
    • Mesenchymal stem cells rescue injured endothelial cells in an in vitro ischemia-reperfusion model via tunneling nanotube like structure-mediated mitochondrial transfer
    • [CrossRef] [PubMed]
    • Liu, K.; Ji, K.; Guo, L.; Wu, W.; Lu, H.; Shan, P.; Yan, C. Mesenchymal stem cells rescue injured endothelial cells in an in vitro ischemia-reperfusion model via tunneling nanotube like structure-mediated mitochondrial transfer. Microvasc. Res. 2014, 92, 10-18. [CrossRef] [PubMed]
    • (2014) Microvasc. Res. , vol.92 , pp. 10-18
    • Liu, K.1    Ji, K.2    Guo, L.3    Wu, W.4    Lu, H.5    Shan, P.6    Yan, C.7
  • 70
    • 84906850885 scopus 로고    scopus 로고
    • Mitochondrial transfer of induced pluripotent stem cell-derived mesenchymal stem cells to airway epithelial cells attenuates cigarette smoke-induced damage
    • [CrossRef] [PubMed]
    • Li, X.; Zhang, Y.; Yeung, S.C.; Liang, Y.; Liang, X.; Ding, Y.; Ip, M.S.M.; Tse, H.F.; Mak, J.C.W.; Lian, Q. Mitochondrial transfer of induced pluripotent stem cell-derived mesenchymal stem cells to airway epithelial cells attenuates cigarette smoke-induced damage. Am. J. Respir. Cell. Mol. Biol. 2014, 51, 455-465. [CrossRef] [PubMed]
    • (2014) Am. J. Respir. Cell. Mol. Biol , vol.51 , pp. 455-465
    • Li, X.1    Zhang, Y.2    Yeung, S.C.3    Liang, Y.4    Liang, X.5    Ding, Y.6    Ip, M.S.M.7    Tse, H.F.8    Mak, J.C.W.9    Lian, Q.10
  • 72
    • 84869030015 scopus 로고    scopus 로고
    • Fusion and fission: Interlinked processes critical for mitochondrial health
    • [CrossRef] [PubMed]
    • Chan, D.C. Fusion and fission: Interlinked processes critical for mitochondrial health. Annu. Rev. Genet. 2012, 46, 265-287. [CrossRef] [PubMed]
    • (2012) Annu. Rev. Genet , vol.46 , pp. 265-287
    • Chan, D.C.1
  • 73
    • 84937969345 scopus 로고    scopus 로고
    • Mitochondrial dynamics: Orchestrating the journey to advanced age
    • [CrossRef] [PubMed]
    • Biala, A.K.; Dhingra, R.; Kirshenbaum, L.A. Mitochondrial dynamics: Orchestrating the journey to advanced age. J. Mol. Cell. Cardiol. 2015, 83, 37-43. [CrossRef] [PubMed]
    • (2015) J. Mol. Cell. Cardiol , vol.83 , pp. 37-43
    • Biala, A.K.1    Dhingra, R.2    Kirshenbaum, L.A.3
  • 74
    • 84903268566 scopus 로고    scopus 로고
    • In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts
    • [CrossRef] [PubMed]
    • Sesaki, H.; Adachi, Y.; Kageyama, Y.; Itoh, K.; Iijima, M. In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts. Biochim. Biophys Acta 2014, 1842, 1179-1185. [CrossRef] [PubMed]
    • (2014) Biochim. Biophys Acta , vol.1842 , pp. 1179-1185
    • Sesaki, H.1    Adachi, Y.2    Kageyama, Y.3    Itoh, K.4    Iijima, M.5
  • 75
    • 84922776083 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy in mammalian cells
    • [CrossRef] [PubMed]
    • Eiyama, A.; Okamoto, K. PINK1/Parkin-mediated mitophagy in mammalian cells. Curr. Opin. Cell. Biol. 2015, 33, 95-101. [CrossRef] [PubMed]
    • (2015) Curr. Opin. Cell. Biol , vol.33 , pp. 95-101
    • Eiyama, A.1    Okamoto, K.2
  • 76
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • [CrossRef] [PubMed]
    • Wang, X.; Winter, D.; Ashrafi, G.; Schlehe, J.; Wong, Y.L.; Selkoe, D.; Rice, S.; Steen, J.; LaVoie, M.J.; Schwarz, T.L. PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 2011, 147, 893-906. [CrossRef] [PubMed]
    • (2011) Cell , vol.147 , pp. 893-906
    • Wang, X.1    Winter, D.2    Ashrafi, G.3    Schlehe, J.4    Wong, Y.L.5    Selkoe, D.6    Rice, S.7    Steen, J.8    Lavoie, M.J.9    Schwarz, T.L.10
  • 77
    • 84859237566 scopus 로고    scopus 로고
    • Parkinson’s disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria
    • [CrossRef] [PubMed]
    • Liu, S.; Sawada, T.; Lee, S.; Yu, W.; Silverio, G.; Alapatt, P.; Millan, I.; Shen, A.; Saxton, W.; Kanao, T., et al. Parkinson’s disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria. PLoS Genet. 2012, 8, e1002537. [CrossRef] [PubMed]
    • (2012) Plos Genet , vol.8
    • Liu, S.1    Sawada, T.2    Lee, S.3    Yu, W.4    Silverio, G.5    Alapatt, P.6    Millan, I.7    Shen, A.8    Saxton, W.9    Kanao, T.10
  • 78
    • 48249084256 scopus 로고    scopus 로고
    • EMB2473/MIRO1, an Arabidopsis Miro GTPase, is required for embryogenesis and influences mitochondrial morphology in pollen
    • [CrossRef] [PubMed]
    • Yamaoka, S.; Leaver, C.J. EMB2473/MIRO1, an Arabidopsis Miro GTPase, is required for embryogenesis and influences mitochondrial morphology in pollen. Plant Cell 2008, 20, 589-601. [CrossRef] [PubMed]
    • (2008) Plant Cell , vol.20 , pp. 589-601
    • Yamaoka, S.1    Leaver, C.J.2
  • 79
    • 78651449517 scopus 로고    scopus 로고
    • MIRO1 influences the morphology and intracellular distribution of mitochondria during embryonic cell division in Arabidopsis
    • [CrossRef] [PubMed]
    • Yamaoka, S.; Nakajima, M.; Fujimoto, M.; Tsutsumi, N. MIRO1 influences the morphology and intracellular distribution of mitochondria during embryonic cell division in Arabidopsis. Plant Cell Rep. 2011, 30, 239-244. [CrossRef] [PubMed]
    • (2011) Plant Cell Rep , vol.30 , pp. 239-244
    • Yamaoka, S.1    Nakajima, M.2    Fujimoto, M.3    Tsutsumi, N.4
  • 80
    • 79954463057 scopus 로고    scopus 로고
    • Arabidopsis thaliana MIRO1 and MIRO2 GTPases are unequally redundant in pollen tube growth and fusion of polar nuclei during female gametogenesis
    • [CrossRef] [PubMed]
    • Sørmo, C.G.; Brembu, T.; Winge, P.; Bones, A.M. Arabidopsis thaliana MIRO1 and MIRO2 GTPases are unequally redundant in pollen tube growth and fusion of polar nuclei during female gametogenesis. PLoS ONE 2011, 6, e18530. [CrossRef] [PubMed]
    • (2011) Plos ONE , vol.6
    • Sørmo, C.G.1    Brembu, T.2    Winge, P.3    Bones, A.M.4
  • 81
    • 40849102944 scopus 로고    scopus 로고
    • Multiple pathways influence mitochondrial inheritance in budding yeast
    • [CrossRef] [PubMed]
    • Frederick, R.L.; Okamoto, K.; Shaw, J.M. Multiple pathways influence mitochondrial inheritance in budding yeast. Genetics 2008, 178, 825-837. [CrossRef] [PubMed]
    • (2008) Genetics , vol.178 , pp. 825-837
    • Frederick, R.L.1    Okamoto, K.2    Shaw, J.M.3
  • 82
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mitochondria contacts: Function of the junction
    • [CrossRef] [PubMed]
    • Rowland, A.A.; Voeltz, G.K. Endoplasmic reticulum-mitochondria contacts: Function of the junction. Nat. Rev. Mol. Cell Biol. 2012, 13, 607-625. [CrossRef] [PubMed]
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 83
    • 84925782876 scopus 로고    scopus 로고
    • ER-mitochondria contact sites in yeast: Beyond the myths of ERMES
    • [CrossRef] [PubMed]
    • Lang, A.; John Peter, A.T.; Kornmann, B. ER-mitochondria contact sites in yeast: Beyond the myths of ERMES. Curr. Opin. Cell Biol. 2015, 35, 7-12. [CrossRef] [PubMed]
    • (2015) Curr. Opin. Cell Biol , vol.35 , pp. 7-12
    • Lang, A.1    John Peter, A.T.2    Kornmann, B.3
  • 84
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • [CrossRef] [PubMed]
    • Kornmann, B.; Currie, E.; Collins, S.R.; Schuldiner, M.; Nunnari, J.; Weissman, J.S.; Walter, P. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 2009, 325, 477-481. [CrossRef] [PubMed]
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1    Currie, E.2    Collins, S.R.3    Schuldiner, M.4    Nunnari, J.5    Weissman, J.S.6    Walter, P.7
  • 85
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • [CrossRef] [PubMed]
    • De Brito, O.M.; Scorrano, L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456, 605-610. [CrossRef] [PubMed]
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 87
    • 84888627184 scopus 로고    scopus 로고
    • Location and membrane sources for autophagosome formation—From ER-mitochondria contact sites to Golgi-endosome-derived carriers
    • [CrossRef] [PubMed]
    • Chan, S.N.; Tang, B.L. Location and membrane sources for autophagosome formation—From ER-mitochondria contact sites to Golgi-endosome-derived carriers. Mol. Membr. Biol. 2013, 30, 394-402. [CrossRef] [PubMed]
    • (2013) Mol. Membr. Biol , vol.30 , pp. 394-402
    • Chan, S.N.1    Tang, B.L.2
  • 88
    • 84884879594 scopus 로고    scopus 로고
    • Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease
    • [CrossRef] [PubMed]
    • Yan, M.H.; Wang, X.; Zhu, X. Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease. Free Radic. Biol. Med. 2013, 62, 90-101. [CrossRef] [PubMed]
    • (2013) Free Radic. Biol. Med , vol.62 , pp. 90-101
    • Yan, M.H.1    Wang, X.2    Zhu, X.3
  • 89
    • 37349004102 scopus 로고    scopus 로고
    • Parkinson’s disease
    • [CrossRef] [PubMed]
    • Thomas, B.; Beal, M.F. Parkinson’s disease. Hum. Mol. Genet. 2007, 16, R183-R194. [CrossRef] [PubMed]
    • (2007) Hum. Mol. Genet , vol.16
    • Thomas, B.1    Beal, M.F.2
  • 90
    • 84928757484 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of Miro inhibits synaptic growth and protects dopaminergic neurons in Drosophila
    • [CrossRef] [PubMed]
    • Tsai, P.I.; Course, M.M.; Lovas, J.R.; Hsieh, C.H.; Babic, M.; Zinsmaier, K.E.; Wang, X. PINK1-mediated phosphorylation of Miro inhibits synaptic growth and protects dopaminergic neurons in Drosophila. Sci. Rep. 2014, 4, 6962. [CrossRef] [PubMed]
    • (2014) Sci. Rep , vol.4 , pp. 6962
    • Tsai, P.I.1    Course, M.M.2    Lovas, J.R.3    Hsieh, C.H.4    Babic, M.5    Zinsmaier, K.E.6    Wang, X.7
  • 92
    • 84897361663 scopus 로고    scopus 로고
    • Mitochondrial toxic effects of Aβ through mitofusins in the early pathogenesis of Alzheimer’s disease
    • [CrossRef] [PubMed]
    • Wu, Z.; Zhu, Y.; Cao, X.; Sun, S.; Zhao, B. Mitochondrial toxic effects of Aβ through mitofusins in the early pathogenesis of Alzheimer’s disease. Mol. Neurobiol. 2014, 50, 986-996. [CrossRef] [PubMed]
    • (2014) Mol. Neurobiol , vol.50 , pp. 986-996
    • Wu, Z.1    Zhu, Y.2    Cao, X.3    Sun, S.4    Zhao, B.5
  • 93
    • 84924571507 scopus 로고    scopus 로고
    • Loss of mitofusin 2 links beta-amyloid-mediated mitochondrial fragmentation and Cdk5-induced oxidative stress in neuron cells
    • [CrossRef] [PubMed]
    • Park, J.; Choi, H.; Min, J.S.; Kim, B.; Lee, S.R.; Yun, J.W.; Choi, M.S.; Chang, K.T.; Lee, D.S. Loss of mitofusin 2 links beta-amyloid-mediated mitochondrial fragmentation and Cdk5-induced oxidative stress in neuron cells. J. Neurochem. 2015, 132, 687-702. [CrossRef] [PubMed]
    • (2015) J. Neurochem , vol.132 , pp. 687-702
    • Park, J.1    Choi, H.2    Min, J.S.3    Kim, B.4    Lee, S.R.5    Yun, J.W.6    Choi, M.S.7    Chang, K.T.8    Lee, D.S.9
  • 94
    • 84866150232 scopus 로고    scopus 로고
    • Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer’s disease-related tau phosphorylation via PAR-1
    • [CrossRef] [PubMed]
    • Iijima-Ando, K.; Sekiya, M.; Maruko-Otake, A.; Ohtake, Y.; Suzuki, E.; Lu, B.; Iijima, K.M. Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer’s disease-related tau phosphorylation via PAR-1. PLoS Genet. 2012, 8, e1002918. [CrossRef] [PubMed]
    • (2012) Plos Genet , vol.8
    • Iijima-Ando, K.1    Sekiya, M.2    Maruko-Otake, A.3    Ohtake, Y.4    Suzuki, E.5    Lu, B.6    Iijima, K.M.7
  • 96
    • 84920975221 scopus 로고    scopus 로고
    • Mitochondrial fusion but not fission regulates larval growth and synaptic development through steroid hormone production
    • [CrossRef] [PubMed]
    • Sandoval, H.; Yao, C.K.; Chen, K.; Jaiswal, M.; Donti, T.; Lin, Y.Q.; Bayat, V.; Xiong, B.; Zhang, K.; David, G., et al. Mitochondrial fusion but not fission regulates larval growth and synaptic development through steroid hormone production. Elife 2014, 3, e03558. [CrossRef] [PubMed]
    • (2014) Elife , vol.3
    • Sandoval, H.1    Yao, C.K.2    Chen, K.3    Jaiswal, M.4    Donti, T.5    Lin, Y.Q.6    Bayat, V.7    Xiong, B.8    Zhang, K.9    David, G.10
  • 98
    • 84859246580 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria
    • [CrossRef] [PubMed]
    • Mórotz, G.M.; De Vos, K.J.; Vagnoni, A.; Ackerley, S.; Shaw, C.E.; Miller, C.C.J. Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria. Hum. Mol. Genet. 2012, 21, 1979-1988. [CrossRef] [PubMed]
    • (2012) Hum. Mol. Genet , vol.21 , pp. 1979-1988
    • Mórotz, G.M.1    De Vos, K.J.2    Vagnoni, A.3    Ackerley, S.4    Shaw, C.E.5    Miller, C.C.J.6
  • 99
    • 84910615187 scopus 로고    scopus 로고
    • Vibrio cholerae T3SS effector VopE modulates mitochondrial dynamics and innate immune signaling by targeting Miro GTPases
    • [CrossRef] [PubMed]
    • Suzuki, M.; Danilchanka, O.; Mekalanos, J.J. Vibrio cholerae T3SS effector VopE modulates mitochondrial dynamics and innate immune signaling by targeting Miro GTPases. Cell. Host Microbe 2014, 16, 581-591. [CrossRef] [PubMed]
    • (2014) Cell. Host Microbe , vol.16 , pp. 581-591
    • Suzuki, M.1    Danilchanka, O.2    Mekalanos, J.J.3
  • 100
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • [CrossRef] [PubMed]
    • Seth, R.B.; Sun, L.; Ea, C.K.; Chen, Z.J. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 2005, 122, 669-682. [CrossRef] [PubMed]
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.