메뉴 건너뛰기




Volumn 58, Issue 2, 2015, Pages 244-254

Extracellular Regulated Kinase Phosphorylates Mitofusin 1 to Control Mitochondrial Morphology and Apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

MITOFUSIN 1; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MYELIN BASIC PROTEIN; OXYGEN; PROTEIN BCL 2; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MFN1 PROTEIN, MOUSE; MITOCHONDRIAL PROTEIN; MITOFUSIN 1 PROTEIN, RAT;

EID: 84928212582     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2015.02.021     Document Type: Article
Times cited : (180)

References (52)
  • 2
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D., Grodet A., Lee Y.J., Estaquier J., Blackstone C. Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J.Biol. Chem. 2005, 280:35742-35750.
    • (2005) J.Biol. Chem. , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 3
    • 28444487509 scopus 로고    scopus 로고
    • Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death
    • Arnoult D., Rismanchi N., Grodet A., Roberts R.G., Seeburg D.P., Estaquier J., Sheng M., Blackstone C. Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death. Curr. Biol. 2005, 15:2112-2118.
    • (2005) Curr. Biol. , vol.15 , pp. 2112-2118
    • Arnoult, D.1    Rismanchi, N.2    Grodet, A.3    Roberts, R.G.4    Seeburg, D.P.5    Estaquier, J.6    Sheng, M.7    Blackstone, C.8
  • 4
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil S.A., Villén J., Gerber S.A., Rush J., Gygi S.P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 2006, 24:1285-1292.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villén, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 5
    • 34547442346 scopus 로고    scopus 로고
    • Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
    • Brooks C., Wei Q., Feng L., Dong G., Tao Y., Mei L., Xie Z.J., Dong Z. Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins. Proc. Natl. Acad. Sci. USA 2007, 104:11649-11654.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11649-11654
    • Brooks, C.1    Wei, Q.2    Feng, L.3    Dong, G.4    Tao, Y.5    Mei, L.6    Xie, Z.J.7    Dong, Z.8
  • 6
    • 77956230098 scopus 로고    scopus 로고
    • Mitochondrial shape changes: orchestrating cell pathophysiology
    • Campello S., Scorrano L. Mitochondrial shape changes: orchestrating cell pathophysiology. EMBO Rep. 2010, 11:678-684.
    • (2010) EMBO Rep. , vol.11 , pp. 678-684
    • Campello, S.1    Scorrano, L.2
  • 8
    • 77957851365 scopus 로고    scopus 로고
    • Inhibition of Drp1-dependent mitochondrial fragmentation and apoptosis by a polypeptide antagonist of calcineurin
    • Cereghetti G.M., Costa V., Scorrano L. Inhibition of Drp1-dependent mitochondrial fragmentation and apoptosis by a polypeptide antagonist of calcineurin. Cell Death Differ. 2010, 17:1785-1794.
    • (2010) Cell Death Differ. , vol.17 , pp. 1785-1794
    • Cereghetti, G.M.1    Costa, V.2    Scorrano, L.3
  • 9
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Chen Y., Dorn G.W. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 2013, 340:471-475.
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 10
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., Chan D.C. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J.Cell Biol. 2003, 160:189-200.
    • (2003) J.Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 11
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng E.H., Wei M.C., Weiler S., Flavell R.A., Mak T.W., Lindsten T., Korsmeyer S.J. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol. Cell 2001, 8:705-711.
    • (2001) Mol. Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 13
    • 0025881168 scopus 로고
    • Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase
    • Clark-Lewis I., Sanghera J.S., Pelech S.L. Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase. J.Biol. Chem. 1991, 266:15180-15184.
    • (1991) J.Biol. Chem. , vol.266 , pp. 15180-15184
    • Clark-Lewis, I.1    Sanghera, J.S.2    Pelech, S.L.3
  • 15
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs J.T., Strack S. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 2007, 8:939-944.
    • (2007) EMBO Rep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 16
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., Korsmeyer S.J. Cell death: critical control points. Cell 2004, 116:205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 17
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito O.M., Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 19
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • Dhillon A.S., Hagan S., Rath O., Kolch W. MAP kinase signalling pathways in cancer. Oncogene 2007, 26:3279-3290.
    • (2007) Oncogene , vol.26 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 23
    • 34347236921 scopus 로고    scopus 로고
    • Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts
    • Frezza C., Cipolat S., Scorrano L. Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts. Nat. Protoc. 2007, 2:287-295.
    • (2007) Nat. Protoc. , vol.2 , pp. 287-295
    • Frezza, C.1    Cipolat, S.2    Scorrano, L.3
  • 24
    • 84899674215 scopus 로고    scopus 로고
    • Resveratrol protects primary cortical neuron cultures from transient oxygen-glucose deprivation by inhibiting MMP-9
    • Gao D.K., Huang T., Jiang X.F., Hu S.J., Zhang L., Fei Z. Resveratrol protects primary cortical neuron cultures from transient oxygen-glucose deprivation by inhibiting MMP-9. Mol Med Rep 2014, 9:2197-2204.
    • (2014) Mol Med Rep , vol.9 , pp. 2197-2204
    • Gao, D.K.1    Huang, T.2    Jiang, X.F.3    Hu, S.J.4    Zhang, L.5    Fei, Z.6
  • 25
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis
    • Germain M., Mathai J.P., McBride H.M., Shore G.C. Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis. EMBO J. 2005, 24:1546-1556.
    • (2005) EMBO J. , vol.24 , pp. 1546-1556
    • Germain, M.1    Mathai, J.P.2    McBride, H.M.3    Shore, G.C.4
  • 26
    • 79960493052 scopus 로고    scopus 로고
    • Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1
    • Glauser L., Sonnay S., Stafa K., Moore D.J. Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1. J.Neurochem. 2011, 118:636-645.
    • (2011) J.Neurochem. , vol.118 , pp. 636-645
    • Glauser, L.1    Sonnay, S.2    Stafa, K.3    Moore, D.J.4
  • 27
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes L.C., Di Benedetto G., Scorrano L. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 2011, 13:589-598.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 28
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., Kroemer G. The pathophysiology of mitochondrial cell death. Science 2004, 305:626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 29
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N., Eura Y., Mihara K. Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity. J.Cell Sci. 2004, 117:6535-6546.
    • (2004) J.Cell Sci. , vol.117 , pp. 6535-6546
    • Ishihara, N.1    Eura, Y.2    Mihara, K.3
  • 30
    • 1242307475 scopus 로고    scopus 로고
    • Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis
    • Karbowski M., Arnoult D., Chen H., Chan D.C., Smith C.L., Youle R.J. Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J.Cell Biol. 2004, 164:493-499.
    • (2004) J.Cell Biol. , vol.164 , pp. 493-499
    • Karbowski, M.1    Arnoult, D.2    Chen, H.3    Chan, D.C.4    Smith, C.L.5    Youle, R.J.6
  • 32
    • 67349125439 scopus 로고    scopus 로고
    • Interplay between MEK and PI3 kinase signaling regulates the subcellular localization of protein kinases ERK1/2 and Akt upon oxidative stress
    • Kodiha M., Bański P., Stochaj U. Interplay between MEK and PI3 kinase signaling regulates the subcellular localization of protein kinases ERK1/2 and Akt upon oxidative stress. FEBS Lett. 2009, 583:1987-1993.
    • (2009) FEBS Lett. , vol.583 , pp. 1987-1993
    • Kodiha, M.1    Bański, P.2    Stochaj, U.3
  • 34
    • 84865395988 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis
    • Leboucher G.P., Tsai Y.C., Yang M., Shaw K.C., Zhou M., Veenstra T.D., Glickman M.H., Weissman A.M. Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis. Mol. Cell 2012, 47:547-557.
    • (2012) Mol. Cell , vol.47 , pp. 547-557
    • Leboucher, G.P.1    Tsai, Y.C.2    Yang, M.3    Shaw, K.C.4    Zhou, M.5    Veenstra, T.D.6    Glickman, M.H.7    Weissman, A.M.8
  • 36
    • 0344004866 scopus 로고    scopus 로고
    • Mgm101p is a novel component of the mitochondrial nucleoid that binds DNA and is required for the repair of oxidatively damaged mitochondrial DNA
    • Meeusen S., Tieu Q., Wong E., Weiss E., Schieltz D., Yates J.R., Nunnari J. Mgm101p is a novel component of the mitochondrial nucleoid that binds DNA and is required for the repair of oxidatively damaged mitochondrial DNA. J.Cell Biol. 1999, 145:291-304.
    • (1999) J.Cell Biol. , vol.145 , pp. 291-304
    • Meeusen, S.1    Tieu, Q.2    Wong, E.3    Weiss, E.4    Schieltz, D.5    Yates, J.R.6    Nunnari, J.7
  • 38
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment ofDrp1 during mitochondrial fission in mammalian cells
    • Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K. Mff is an essential factor for mitochondrial recruitment ofDrp1 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    Wang, C.2    Cleland, M.M.3    Setoguchi, K.4    Yokota, S.5    Youle, R.J.6    Mihara, K.7
  • 39
    • 84875273810 scopus 로고    scopus 로고
    • New insights into the function and regulation of mitochondrial fission
    • Otera H., Ishihara N., Mihara K. New insights into the function and regulation of mitochondrial fission. Biochim. Biophys. Acta 2013, 1833:1256-1268.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1256-1268
    • Otera, H.1    Ishihara, N.2    Mihara, K.3
  • 40
    • 0028359984 scopus 로고
    • Constitutive mutant and putative regulatory serine phosphorylation site of mammalian MAP kinase kinase (MEK1)
    • Pagès G., Brunet A., L'Allemain G., Pouysségur J. Constitutive mutant and putative regulatory serine phosphorylation site of mammalian MAP kinase kinase (MEK1). EMBO J. 1994, 13:3003-3010.
    • (1994) EMBO J. , vol.13 , pp. 3003-3010
    • Pagès, G.1    Brunet, A.2    L'Allemain, G.3    Pouysségur, J.4
  • 41
    • 79959987510 scopus 로고    scopus 로고
    • Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
    • Rambold A.S., Kostelecky B., Elia N., Lippincott-Schwartz J. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc. Natl. Acad. Sci. USA 2011, 108:10190-10195.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10190-10195
    • Rambold, A.S.1    Kostelecky, B.2    Elia, N.3    Lippincott-Schwartz, J.4
  • 42
    • 76249084726 scopus 로고    scopus 로고
    • Activation of mitochondrial ERK protects cancer cells from death through inhibition of the permeability transition
    • Rasola A., Sciacovelli M., Chiara F., Pantic B., Brusilow W.S., Bernardi P. Activation of mitochondrial ERK protects cancer cells from death through inhibition of the permeability transition. Proc. Natl. Acad. Sci. USA 2010, 107:726-731.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 726-731
    • Rasola, A.1    Sciacovelli, M.2    Chiara, F.3    Pantic, B.4    Brusilow, W.S.5    Bernardi, P.6
  • 45
    • 34547204160 scopus 로고    scopus 로고
    • The MEK/ERK cascade: from signaling specificity to diverse functions
    • Shaul Y.D., Seger R. The MEK/ERK cascade: from signaling specificity to diverse functions. Biochim. Biophys. Acta 2007, 1773:1213-1226.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1213-1226
    • Shaul, Y.D.1    Seger, R.2
  • 48
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z.G., Jiang H., Chen S., Du F.H., Wang X.D. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012, 148:228-243.
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.G.1    Jiang, H.2    Chen, S.3    Du, F.H.4    Wang, X.D.5
  • 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
    • 0042433119 scopus 로고    scopus 로고
    • Erasure of kinase phosphorylation in astrocytes during oxygen-glucose deprivation is controlled by ATP levels and activation of phosphatases
    • Yung H.W., Tolkovsky A.M. Erasure of kinase phosphorylation in astrocytes during oxygen-glucose deprivation is controlled by ATP levels and activation of phosphatases. J.Neurochem. 2003, 86:1281-1288.
    • (2003) J.Neurochem. , vol.86 , pp. 1281-1288
    • Yung, H.W.1    Tolkovsky, A.M.2
  • 52
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E., Tao R.N., Whitworth A.J. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. USA 2010, 107:5018-5023.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.