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Volumn 22, Issue 12, 2015, Pages 1047-1059

Beyond Mitophagy: Cytosolic PINK1 as a Messenger of Mitochondrial Health

Author keywords

[No Author keywords available]

Indexed keywords

NEUROTROPHIC FACTOR; PROTEIN SERINE THREONINE KINASE; PTEN INDUCED PUTATIVE KINASE 1; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; PROTEIN KINASE; PTEN-INDUCED PUTATIVE KINASE;

EID: 84926656581     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2014.6206     Document Type: Review
Times cited : (27)

References (125)
  • 1
    • 84906044094 scopus 로고    scopus 로고
    • Detailed analysis of mitochondrial respiratory chain defects caused by loss of PINK1
    • Amo T, Saiki S, Sawayama T, Sato S, and Hattori N. Detailed analysis of mitochondrial respiratory chain defects caused by loss of PINK1. Neurosci Lett 580: 37-40, 2014.
    • (2014) Neurosci Lett , vol.580 , pp. 37-40
    • Amo, T.1    Saiki, S.2    Sawayama, T.3    Sato, S.4    Hattori, N.5
  • 2
    • 78349309594 scopus 로고    scopus 로고
    • Mitochondrial membrane potential decrease caused by loss of PINK1 is not due to proton leak, but to respiratory chain defects
    • Amo T, Sato S, Saiki S, Wolf AM, Toyomizu M, Gautier CA, Shen J, Ohta S, and Hattori N. Mitochondrial membrane potential decrease caused by loss of PINK1 is not due to proton leak, but to respiratory chain defects. Neurobiol Dis 41: 111-118, 2011.
    • (2011) Neurobiol Dis , vol.41 , pp. 111-118
    • Amo, T.1    Sato, S.2    Saiki, S.3    Wolf, A.M.4    Toyomizu, M.5    Gautier, C.A.6    Shen, J.7    Ohta, S.8    Hattori, N.9
  • 3
    • 84880303306 scopus 로고    scopus 로고
    • PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage
    • Arena G, Gelmetti V, Torosantucci L, Vignone D, Lamorte G, De Rosa P, Cilia E, Jonas EA, and Valente EM. PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage. Cell Death Differ 20: 920-930, 2013.
    • (2013) Cell Death Differ , vol.20 , pp. 920-930
    • Arena, G.1    Gelmetti, V.2    Torosantucci, L.3    Vignone, D.4    Lamorte, G.5    De Rosa, P.6    Cilia, E.7    Jonas, E.A.8    Valente, E.M.9
  • 4
    • 84906861963 scopus 로고    scopus 로고
    • Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin
    • Ashrafi G, Schlehe JS, LaVoie MJ, and Schwarz TL. Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin. J Cell Biol 206: 655-670, 2014.
    • (2014) J Cell Biol , vol.206 , pp. 655-670
    • Ashrafi, G.1    Schlehe, J.S.2    LaVoie, M.J.3    Schwarz, T.L.4
  • 5
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • Ashrafi G and Schwarz TL. The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ 20: 31-42, 2013.
    • (2013) Cell Death Differ , vol.20 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 6
    • 84863308390 scopus 로고    scopus 로고
    • Pink1 kinase and its membrane potential (Deltapsi)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode
    • Becker D, Richter J, Tocilescu MA, Przedborski S, and Voos W. Pink1 kinase and its membrane potential (Deltapsi)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode. J Biol Chem 287: 22969-22987, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 22969-22987
    • Becker, D.1    Richter, J.2    Tocilescu, M.A.3    Przedborski, S.4    Voos, W.5
  • 7
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A, Van Der Brug M, Ahmad R, Kesavapany S, Miller DW, Petsko GA, and Cookson MR. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci U S A 102: 5703-5708, 2005.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5703-5708
    • Beilina, A.1    Van Der Brug, M.2    Ahmad, R.3    Kesavapany, S.4    Miller, D.W.5    Petsko, G.A.6    Cookson, M.R.7
  • 8
    • 79959344616 scopus 로고    scopus 로고
    • PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function
    • Billia F, Hauck L, Konecny F, Rao V, Shen J, and Mak TW. PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function. Proc Natl Acad Sci U S A 108: 9572-9577, 2011.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9572-9577
    • Billia, F.1    Hauck, L.2    Konecny, F.3    Rao, V.4    Shen, J.5    Mak, T.W.6
  • 12
    • 84858701257 scopus 로고    scopus 로고
    • Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • Cai Q, Zakaria HM, Simone A, and Sheng ZH. Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Curr Biol 22: 545-552, 2012.
    • (2012) Curr Biol , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 17
    • 77953877676 scopus 로고    scopus 로고
    • A pivotal role for PINK1 and autophagy in mitochondrial quality control: Implications for Parkinson disease
    • Chu CT. A pivotal role for PINK1 and autophagy in mitochondrial quality control: implications for Parkinson disease. Hum Mol Genet 19: R28-R37, 2010.
    • (2010) Hum Mol Genet , vol.19 , pp. R28-R37
    • Chu, C.T.1
  • 18
    • 71849104427 scopus 로고    scopus 로고
    • Tickled PINK1: Mitochondrial homeostasis and autophagy in recessive Parkinsonism
    • Chu CT. Tickled PINK1: mitochondrial homeostasis and autophagy in recessive Parkinsonism. Biochim Biophys Acta 1802: 20-28, 2010.
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 20-28
    • Chu, C.T.1
  • 21
    • 84891915522 scopus 로고    scopus 로고
    • PPARgamma activation rescues mitochondrial function from inhibition of complex I and loss of PINK1
    • Corona JC, de Souza SC, and Duchen MR. PPARgamma activation rescues mitochondrial function from inhibition of complex I and loss of PINK1. Exp Neurol 253: 16-27, 2014.
    • (2014) Exp Neurol , vol.253 , pp. 16-27
    • Corona, J.C.1    De Souza, S.C.2    Duchen, M.R.3
  • 22
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs JT and Strack S. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep 8: 939-944, 2007.
    • (2007) EMBO Rep , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 23
    • 79956278232 scopus 로고    scopus 로고
    • Silencing of PINK1 induces mitophagy via mitochondrial permeability transition in dopaminergic MN9D cells
    • Cui T, Fan C, Gu L, Gao H, Liu Q, Zhang T, Qi Z, Zhao C, Zhao H, Cai Q, and Yang H. Silencing of PINK1 induces mitophagy via mitochondrial permeability transition in dopaminergic MN9D cells. Brain Res 1394: 1-13, 2011.
    • (2011) Brain Res , vol.1394 , pp. 1-13
    • Cui, T.1    Fan, C.2    Gu, L.3    Gao, H.4    Liu, Q.5    Zhang, T.6    Qi, Z.7    Zhao, C.8    Zhao, H.9    Cai, Q.10    Yang, H.11
  • 24
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda RK, Cherra SJ, 3rd, Kulich SM, Tandon A, Park D, and Chu CT. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem 284: 13843-13855, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra, S.J.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 25
    • 81155128499 scopus 로고    scopus 로고
    • Mitochondrially localized PKA reverses mitochondrial pathology and dysfunction in a cellular model of Parkinson's disease
    • Dagda RK, Gusdon AM, Pien I, Strack S, Green S, Li C, Van Houten B, Cherra SJ, 3rd, and Chu CT. Mitochondrially localized PKA reverses mitochondrial pathology and dysfunction in a cellular model of Parkinson's disease. Cell Death Differ 18: 1914-1923, 2011.
    • (2011) Cell Death Differ , vol.18 , pp. 1914-1923
    • Dagda, R.K.1    Gusdon, A.M.2    Pien, I.3    Strack, S.4    Green, S.5    Li, C.6    Van Houten, B.7    Cherra, S.J.8    Chu, C.T.9
  • 31
    • 84879606527 scopus 로고    scopus 로고
    • Molecular signaling toward mitophagy and its physiological significance
    • Feng D, Liu L, Zhu Y, and Chen Q. Molecular signaling toward mitophagy and its physiological significance. Exp Cell Res 319: 1697-1705, 2013.
    • (2013) Exp Cell Res , vol.319 , pp. 1697-1705
    • Feng, D.1    Liu, L.2    Zhu, Y.3    Chen, Q.4
  • 35
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier CA, Kitada T, and Shen J. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc Natl Acad Sci U S A 105: 11364-11369, 2008.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 36
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, and Taanman JW. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum Mol Genet 19: 4861-4870, 2010.
    • (2010) Hum Mol Genet , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 37
    • 62749113469 scopus 로고    scopus 로고
    • Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells
    • Gegg ME, Cooper JM, Schapira AH, and Taanman JW. Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells. PLoS One 4: e4756, 2009.
    • (2009) PLoS One , vol.4 , pp. e4756
    • Gegg, M.E.1    Cooper, J.M.2    Schapira, A.H.3    Taanman, J.W.4
  • 40
    • 84908191333 scopus 로고    scopus 로고
    • Short Mitochondrial ARF Triggers Parkin/PINK1-dependent Mitophagy
    • Grenier K, Kontogiannea M, and Fon EA. Short Mitochondrial ARF Triggers Parkin/PINK1-dependent Mitophagy. J Biol Chem 289: 29519-29530, 2014.
    • (2014) J Biol Chem , vol.289 , pp. 29519-29530
    • Grenier, K.1    Kontogiannea, M.2    Fon, E.A.3
  • 41
    • 84883492814 scopus 로고    scopus 로고
    • Parkin- and PINK1-dependent mitophagy in neurons: Will the real pathway please stand up?
    • Grenier K, McLelland GL, and Fon EA. Parkin- and PINK1-dependent mitophagy in neurons: will the real pathway please stand up? Front Neurol 4: 100, 2013.
    • (2013) Front Neurol , vol.4 , pp. 100
    • Grenier, K.1    McLelland, G.L.2    Fon, E.A.3
  • 42
    • 79954603862 scopus 로고    scopus 로고
    • To eat or not to eat: Neuronal metabolism, mitophagy, and Parkinson's disease
    • Gusdon AM and Chu CT. To eat or not to eat: neuronal metabolism, mitophagy, and Parkinson's disease. Antioxid Redox Signal 14: 1979-1987, 2011.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1979-1987
    • Gusdon, A.M.1    Chu, C.T.2
  • 46
    • 84882754147 scopus 로고    scopus 로고
    • A neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1
    • Hertz NT, Berthet A, Sos ML, Thorn KS, Burlingame AL, Nakamura K, and Shokat KM. A neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1. Cell 154: 737-747, 2013.
    • (2013) Cell , vol.154 , pp. 737-747
    • Hertz, N.T.1    Berthet, A.2    Sos, M.L.3    Thorn, K.S.4    Burlingame, A.L.5    Nakamura, K.6    Shokat, K.M.7
  • 50
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin SM, Lazarou M, Wang C, Kane LA, Narendra DP, and Youle RJ. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol 191: 933-942, 2010.
    • (2010) J Cell Biol , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 51
    • 84861204926 scopus 로고    scopus 로고
    • PINK1- and Parkin-mediated mitophagy at a glance
    • Jin SM and Youle RJ. PINK1- and Parkin-mediated mitophagy at a glance. J Cell Sci 125: 795-799, 2012.
    • (2012) J Cell Sci , vol.125 , pp. 795-799
    • Jin, S.M.1    Youle, R.J.2
  • 52
    • 84887486172 scopus 로고    scopus 로고
    • The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria
    • Jin SM and Youle RJ. The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria. Autophagy 9: 1750-1757, 2013.
    • (2013) Autophagy , vol.9 , pp. 1750-1757
    • Jin, S.M.1    Youle, R.J.2
  • 55
    • 84874640848 scopus 로고    scopus 로고
    • Tom70 is essential for PINK1 import into mitochondria
    • Kato H, Lu Q, Rapaport D, and Kozjak-Pavlovic V. Tom70 is essential for PINK1 import into mitochondria. PLoS One 8: e58435, 2013.
    • (2013) PLoS One , vol.8 , pp. e58435
    • Kato, H.1    Lu, Q.2    Rapaport, D.3    Kozjak-Pavlovic, V.4
  • 61
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
    • Lazarou M, Jin SM, Kane LA, and Youle RJ. Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev Cell 22: 320-333, 2012.
    • (2012) Dev Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 63
    • 84904690794 scopus 로고    scopus 로고
    • Variants of mitochondrial autophagy: Types 1 and 2 mitophagy and micromitophagy (Type 3)
    • Lemasters JJ. Variants of mitochondrial autophagy: types 1 and 2 mitophagy and micromitophagy (Type 3). Redox Biol 2: 749-754, 2014.
    • (2014) Redox Biol , vol.2 , pp. 749-754
    • Lemasters, J.J.1
  • 65
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li Z, Okamoto K, Hayashi Y, and Sheng M. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 119: 873-887, 2004.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 66
    • 45249112594 scopus 로고    scopus 로고
    • Characterization of PINK1 processing, stability, and subcellular localization
    • Lin W and Kang UJ. Characterization of PINK1 processing, stability, and subcellular localization. J Neurochem 106: 464-474, 2008.
    • (2008) J Neurochem , vol.106 , pp. 464-474
    • Lin, W.1    Kang, U.J.2
  • 67
    • 84894098297 scopus 로고    scopus 로고
    • Loss of PINK1 attenuates HIF-1alpha induction by preventing 4E-BP1-dependent switch in protein translation under hypoxia
    • Lin W, Wadlington NL, Chen L, Zhuang X, Brorson JR, and Kang UJ. Loss of PINK1 attenuates HIF-1alpha induction by preventing 4E-BP1-dependent switch in protein translation under hypoxia. J Neurosci 34: 3079-3089, 2014.
    • (2014) J Neurosci , vol.34 , pp. 3079-3089
    • Lin, W.1    Wadlington, N.L.2    Chen, L.3    Zhuang, X.4    Brorson, J.R.5    Kang, U.J.6
  • 68
    • 84903817207 scopus 로고    scopus 로고
    • Receptor-mediated mitophagy in yeast and mammalian systems
    • Liu L, Sakakibara K, Chen Q, and Okamoto K. Receptor-mediated mitophagy in yeast and mammalian systems. Cell Res 24: 787-795, 2014.
    • (2014) Cell Res , vol.24 , pp. 787-795
    • Liu, L.1    Sakakibara, K.2    Chen, Q.3    Okamoto, K.4
  • 69
    • 78650694150 scopus 로고    scopus 로고
    • Reduction of protein translation and activation of autophagy protect against PINK1 pathogenesis in Drosophila melanogaster
    • Liu S and Lu B. Reduction of protein translation and activation of autophagy protect against PINK1 pathogenesis in Drosophila melanogaster. PLoS Genet 6: e1001237, 2010.
    • (2010) PLoS Genet , vol.6 , pp. e1001237
    • Liu, S.1    Lu, B.2
  • 71
  • 72
    • 84904266112 scopus 로고    scopus 로고
    • Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway
    • Maday S and Holzbaur EL. Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway. Dev Cell 30: 71-85, 2014.
    • (2014) Dev Cell , vol.30 , pp. 71-85
    • Maday, S.1    Holzbaur, E.L.2
  • 76
    • 84897863239 scopus 로고    scopus 로고
    • Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
    • McLelland GL, Soubannier V, Chen CX, McBride HM, and Fon EA. Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J 33: 282-295, 2014.
    • (2014) EMBO J , vol.33 , pp. 282-295
    • McLelland, G.L.1    Soubannier, V.2    Chen, C.X.3    McBride, H.M.4    Fon, E.A.5
  • 77
    • 79955667485 scopus 로고    scopus 로고
    • The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
    • Meissner C, Lorenz H, Weihofen A, Selkoe DJ, and Lemberg MK. The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. J Neurochem 117: 856-867, 2011.
    • (2011) J Neurochem , vol.117 , pp. 856-867
    • Meissner, C.1    Lorenz, H.2    Weihofen, A.3    Selkoe, D.J.4    Lemberg, M.K.5
  • 81
    • 41949098617 scopus 로고    scopus 로고
    • L347P PINK1 mutant that fails to bind to Hsp90/Cdc37 chaperones is rapidly degraded in a proteasome-dependent manner
    • Moriwaki Y, Kim YJ, Ido Y, Misawa H, Kawashima K, Endo S, and Takahashi R. L347P PINK1 mutant that fails to bind to Hsp90/Cdc37 chaperones is rapidly degraded in a proteasome-dependent manner. Neurosci Res 61: 43-48, 2008.
    • (2008) Neurosci Res , vol.61 , pp. 43-48
    • Moriwaki, Y.1    Kim, Y.J.2    Ido, Y.3    Misawa, H.4    Kawashima, K.5    Endo, S.6    Takahashi, R.7
  • 83
    • 79953185407 scopus 로고    scopus 로고
    • A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: Activation of AKT via mTORC2
    • Murata H, Sakaguchi M, Jin Y, Sakaguchi Y, Futami J, Yamada H, Kataoka K, and Huh NH. A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2. J Biol Chem 286: 7182-7189, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 7182-7189
    • Murata, H.1    Sakaguchi, M.2    Jin, Y.3    Sakaguchi, Y.4    Futami, J.5    Yamada, H.6    Kataoka, K.7    Huh, N.H.8
  • 88
    • 80052949842 scopus 로고    scopus 로고
    • Loss of PINK1 function decreases PP2A activity and promotes autophagy in dopaminergic cells and a murine model
    • Qi Z, Yang W, Liu Y, Cui T, Gao H, Duan C, Lu L, Zhao C, Zhao H, and Yang H. Loss of PINK1 function decreases PP2A activity and promotes autophagy in dopaminergic cells and a murine model. Neurochem Int 59: 572-581, 2011.
    • (2011) Neurochem Int , vol.59 , pp. 572-581
    • Qi, Z.1    Yang, W.2    Liu, Y.3    Cui, T.4    Gao, H.5    Duan, C.6    Lu, L.7    Zhao, C.8    Zhao, H.9    Yang, H.10
  • 89
    • 84901848121 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic profiling of PINK1-deficient cells identifies phosphorylation changes in nuclear proteins
    • Qin X, Zheng C, Yates JR, 3rd, and Liao L. Quantitative phosphoproteomic profiling of PINK1-deficient cells identifies phosphorylation changes in nuclear proteins. Mol Biosyst 10: 1719-1729, 2014.
    • (2014) Mol Biosyst , vol.10 , pp. 1719-1729
    • Qin, X.1    Zheng, C.2    Yates, J.R.3    Liao, L.4
  • 90
    • 84873843566 scopus 로고    scopus 로고
    • Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous parkin attenuates mitophagy: Study in human primary fibroblasts and induced pluripotent stem cell-derived neurons
    • Rakovic A, Shurkewitsch K, Seibler P, Grunewald A, Zanon A, Hagenah J, Krainc D, and Klein C. Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem cell-derived neurons. J Biol Chem 288: 2223-2237, 2013.
    • (2013) J Biol Chem , vol.288 , pp. 2223-2237
    • Rakovic, A.1    Shurkewitsch, K.2    Seibler, P.3    Grunewald, A.4    Zanon, A.5    Hagenah, J.6    Krainc, D.7    Klein, C.8
  • 91
    • 67650233672 scopus 로고    scopus 로고
    • Caenorhabditis elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth
    • Samann J, Hegermann J, Gromoff EV, Eimer S, Baumeister R, and Schmidt E. Caenorhabditis elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth. J Biol Chem 284: 16482-16491, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 16482-16491
    • Samann, J.1    Hegermann, J.2    Gromoff, E.V.3    Eimer, S.4    Baumeister, R.5    Schmidt, E.6
  • 97
    • 84866283918 scopus 로고    scopus 로고
    • Analysis of the regulatory and catalytic domains of PTEN-induced kinase-1 (PINK1)
    • Sim CH, Gabriel K, Mills RD, Culvenor JG, and Cheng HC. Analysis of the regulatory and catalytic domains of PTEN-induced kinase-1 (PINK1). Hum Mutat 33: 1408-1422, 2012.
    • (2012) Hum Mutat , vol.33 , pp. 1408-1422
    • Sim, C.H.1    Gabriel, K.2    Mills, R.D.3    Culvenor, J.G.4    Cheng, H.C.5
  • 98
    • 37549029702 scopus 로고    scopus 로고
    • Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1
    • Takatori S, Ito G, and Iwatsubo T. Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1. Neurosci Lett 430: 13-17, 2008.
    • (2008) Neurosci Lett , vol.430 , pp. 13-17
    • Takatori, S.1    Ito, G.2    Iwatsubo, T.3
  • 100
    • 84901615924 scopus 로고    scopus 로고
    • PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix
    • Thomas RE, Andrews LA, Burman JL, Lin WY, and Pallanck LJ. PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix. PLoS Genet 10: e1004279, 2014.
    • (2014) PLoS Genet , vol.10 , pp. e1004279
    • Thomas, R.E.1    Andrews, L.A.2    Burman, J.L.3    Lin, W.Y.4    Pallanck, L.J.5
  • 101
    • 84881376726 scopus 로고    scopus 로고
    • Advances in the genetics of Parkinson disease
    • Trinh J and Farrer M. Advances in the genetics of Parkinson disease. Nat Rev Neurol 9: 445-454, 2013.
    • (2013) Nat Rev Neurol , vol.9 , pp. 445-454
    • Trinh, J.1    Farrer, M.2
  • 104
    • 79551603345 scopus 로고    scopus 로고
    • Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization
    • Van Laar VS, Arnold B, Cassady SJ, Chu CT, Burton EA, and Berman SB. Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization. Hum Mol Genet 20: 927-940, 2011.
    • (2011) Hum Mol Genet , vol.20 , pp. 927-940
    • Van Laar, V.S.1    Arnold, B.2    Cassady, S.J.3    Chu, C.T.4    Burton, E.A.5    Berman, S.B.6
  • 105
    • 84872680354 scopus 로고    scopus 로고
    • The interplay of neuronal mitochondrial dynamics and bioenergetics: Implications for Parkinson's disease
    • Van Laar VS and Berman SB. The interplay of neuronal mitochondrial dynamics and bioenergetics: implications for Parkinson's disease. Neurobiol Dis 51: 43-55, 2013.
    • (2013) Neurobiol Dis , vol.51 , pp. 43-55
    • Van Laar, V.S.1    Berman, S.B.2
  • 107
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky A. The N-end rule pathway of protein degradation. Genes Cells 2: 13-28, 1997.
    • (1997) Genes Cells , vol.2 , pp. 13-28
    • Varshavsky, A.1
  • 112
    • 38849155699 scopus 로고    scopus 로고
    • Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1
    • Weihofen A, Ostaszewski B, Minami Y, and Selkoe DJ. Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1. Hum Mol Genet 17: 602-616, 2008.
    • (2008) Hum Mol Genet , vol.17 , pp. 602-616
    • Weihofen, A.1    Ostaszewski, B.2    Minami, Y.3    Selkoe, D.J.4
  • 113
    • 64549112144 scopus 로고    scopus 로고
    • Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking
    • Weihofen A, Thomas KJ, Ostaszewski BL, Cookson MR, and Selkoe DJ. Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 48: 2045-2052, 2009.
    • (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
  • 114
    • 58149397651 scopus 로고    scopus 로고
    • Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin
    • discussion 173
    • Whitworth AJ, Lee JR, Ho VM, Flick R, Chowdhury R, and McQuibban GA. Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin. Dis Model Mech 1: 168-174; discussion 173, 2008.
    • (2008) Dis Model Mech , vol.1 , pp. 168-174
    • Whitworth, A.J.1    Lee, J.R.2    Ho, V.M.3    Flick, R.4    Chowdhury, R.5    McQuibban, G.A.6
  • 115
    • 84908065760 scopus 로고    scopus 로고
    • Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
    • Wong, YC and Holzbaur EL. Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc Natl Acad Sci U S A 111: E4439-E4448, 2014.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. E4439-E4448
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 118
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • Yamano K and Youle RJ. PINK1 is degraded through the N-end rule pathway. Autophagy 9: 1758-1769, 2013.
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 119
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii SR, Kishi C, Ishihara N, and Mizushima N. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J Biol Chem 286: 19630-19640, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 120
    • 84906315018 scopus 로고    scopus 로고
    • PINK1 triggers autocatalytic activation of Parkin to specify cell fate decisions
    • Zhang C, Lee S, Peng Y, Bunker E, Giaime E, Shen J, Zhou Z, and Liu X. PINK1 triggers autocatalytic activation of Parkin to specify cell fate decisions. Curr Biol 24: 1854-1865, 2014.
    • (2014) Curr Biol , vol.24 , pp. 1854-1865
    • Zhang, C.1    Lee, S.2    Peng, Y.3    Bunker, E.4    Giaime, E.5    Shen, J.6    Zhou, Z.7    Liu, X.8
  • 121
    • 84901252533 scopus 로고    scopus 로고
    • Endothelial PINK1 mediates the protective effects of NLRP3 deficiency during lethal oxidant injury
    • Zhang Y, Sauler M, Shinn AS, Gong H, Haslip M, Shan P, Mannam P, and Lee PJ. Endothelial PINK1 mediates the protective effects of NLRP3 deficiency during lethal oxidant injury. J Immunol 192: 5296-5304, 2014.
    • (2014) J Immunol , vol.192 , pp. 5296-5304
    • Zhang, Y.1    Sauler, M.2    Shinn, A.S.3    Gong, H.4    Haslip, M.5    Shan, P.6    Mannam, P.7    Lee, P.J.8
  • 123
    • 77956213267 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • Zhu J and Chu CT. Mitochondrial dysfunction in Parkinson's disease. J Alzheimers Dis 20 Suppl 2: S325-S334, 2010.
    • (2010) J Alzheimers Dis , vol.20 , pp. S325-S334
    • Zhu, J.1    Chu, C.T.2
  • 124
    • 84887387419 scopus 로고    scopus 로고
    • After the banquet: Mitochondrial biogenesis, mitophagy and cell survival
    • Zhu J, Wang KZ, and Chu CT. After the banquet: mitochondrial biogenesis, mitophagy and cell survival. Autophagy 9: 1663-1676, 2013.
    • (2013) Autophagy , vol.9 , pp. 1663-1676
    • Zhu, J.1    Wang, K.Z.2    Chu, C.T.3
  • 125
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E, Tao RN, and Whitworth AJ. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A 107: 5018-5023, 2010.
    • (2010) Proc Natl Acad Sci U S A , 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.