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Volumn 20, Issue 7, 2013, Pages 920-930

PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage

Author keywords

Apoptosis; Mitochondria; Parkinson's disease; Post translational modifications

Indexed keywords

BECLIN 1; PINK 1 PROTEIN; PROTEIN; PROTEIN BCL XL; UNCLASSIFIED DRUG;

EID: 84880303306     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2013.19     Document Type: Article
Times cited : (127)

References (43)
  • 1
    • 0037501731 scopus 로고    scopus 로고
    • Update on Parkinson disease
    • Siderowf A, Stern M. Update on Parkinson disease. Ann Intern Med 2003; 138: 651-658.
    • (2003) Ann Intern Med , vol.138 , pp. 651-658
    • Siderowf, A.1    Stern, M.2
  • 2
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the etiology and pathogenesis of Parkinson's disease
    • Schapira AH. Mitochondria in the etiology and pathogenesis of Parkinson's disease. Lancet Neurol 2008; 7: 97-109.
    • (2008) Lancet Neurol , vol.7 , pp. 97-109
    • Schapira, A.H.1
  • 3
    • 40749152391 scopus 로고    scopus 로고
    • Parkinson's disease: A genetic perspective
    • Belin AC, Westerlund M. Parkinson's disease: a genetic perspective. FEBS J 2008; 275: 1377-1383.
    • (2008) FEBS J , vol.275 , pp. 1377-1383
    • Belin, A.C.1    Westerlund, M.2
  • 5
    • 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, Youle RJ. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol 2010; 191: 933-942.
    • (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
  • 6
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri L, Caputo V, Bellacchio E, Atorino L, Dallapiccola B, Valente EM et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum Mol Genet 2005; 14: 3477-3492.
    • (2005) Hum Mol Genet , vol.14 , pp. 3477-3492
    • Silvestri, L.1    Caputo, V.2    Bellacchio, E.3    Atorino, L.4    Dallapiccola, B.5    Valente, E.M.6
  • 8
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier CA, Kitada T, Shen J. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc Natl Acad Sci USA 2008; 105: 11364-11369.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 9
    • 48649094639 scopus 로고    scopus 로고
    • Late onset sporadic Parkinson's disease caused by PINK1 mutations: Clinical and functional study
    • Gelmetti V, Ferraris A, Brusa L, Romano F, Lombardi F, Barzaghi C et al. Late onset sporadic Parkinson's disease caused by PINK1 mutations: clinical and functional study. Mov Disord 2008; 23: 881-885.
    • (2008) Mov Disord , vol.23 , pp. 881-885
    • Gelmetti, V.1    Ferraris, A.2    Brusa, L.3    Romano, F.4    Lombardi, F.5    Barzaghi, C.6
  • 10
    • 49349087497 scopus 로고    scopus 로고
    • PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons
    • Wood-Kaczmar A, Gandhi S, Yao Z, Abramov AY, Miljan EA, Keen G et al. PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons. PLoS One 2008; 3: e2455.
    • (2008) PLoS One , vol.3
    • Wood-Kaczmar, A.1    Gandhi, S.2    Yao, Z.3    Abramov, A.Y.4    Miljan, E.A.5    Keen, G.6
  • 11
    • 61649088435 scopus 로고    scopus 로고
    • PINK1- associated Parkinson's disease is caused by neuronal vulnerability to calcium-induced cell death
    • Gandhi S, Wood-Kaczmar A, Yao Z, Plun-Favreau H, Deas E, Klupsch K et al. PINK1- associated Parkinson's disease is caused by neuronal vulnerability to calcium-induced cell death. Mol Cell 2009; 33: 627-638.
    • (2009) Mol Cell , vol.33 , pp. 627-638
    • Gandhi, S.1    Wood-Kaczmar, A.2    Yao, Z.3    Plun-Favreau, H.4    Deas, E.5    Klupsch, K.6
  • 12
    • 61349156769 scopus 로고    scopus 로고
    • Mutant Pink1 induces mitochondrial dysfunction in a neuronal cell model of Parkinson's disease by disturbing calcium flux
    • Marongiu R, Spencer B, Crews L, Adame A, Patrick C, Trejo M et al. Mutant Pink1 induces mitochondrial dysfunction in a neuronal cell model of Parkinson's disease by disturbing calcium flux. J Neurochem 2009; 108: 1561-1574.
    • (2009) J Neurochem , vol.108 , pp. 1561-1574
    • Marongiu, R.1    Spencer, B.2    Crews, L.3    Adame, A.4    Patrick, C.5    Trejo, M.6
  • 13
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • Plun-Favreau H, Klupsch K, Moisoi N, Gandhi S, Kjaer S, Frith D et al. The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 2007; 9: 1243-1252.
    • (2007) Nat Cell Biol , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    Moisoi, N.3    Gandhi, S.4    Kjaer, S.5    Frith, D.6
  • 14
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon JW, Olzmann JA, Chin LS, Li L. PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol 2007; 5: e172.
    • (2007) PLoS Biol , vol.5
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 15
    • 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 2010; 19: R28-R37.
    • (2010) Hum Mol Genet , vol.19
    • Chu, C.T.1
  • 19
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • Wang X, Winter D, Ashrafi G, Schlehe J, Wong YL, Selkoe D et al. PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 2011; 147: 893-906.
    • (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
  • 21
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • He C, Levine B. The Beclin 1 interactome. Curr Opin Cell Biol 2010; 22: 140-149.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 140-149
    • He, C.1    Levine, B.2
  • 22
    • 78751655392 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL play important roles in the crosstalk between autophagy and apoptosis
    • Zhou F, Yang Y, Bcl-2 XingD. and Bcl-xL play important roles in the crosstalk between autophagy and apoptosis. FEBS J 2011; 278: 403-413.
    • (2011) FEBS J , vol.278 , pp. 403-413
    • Zhou, F.1    Yang, Y.2    Xing, D.3
  • 23
    • 85047698632 scopus 로고    scopus 로고
    • Dynamics of expression of apoptosis-regulatory proteins Bid, Bcl-2, Bcl-X, Bax and Bak during development of murine nervous system
    • Krajewska M, Mai JK, Zapata JM, Ashwell KW, Schendel SL, Reed JC et al. Dynamics of expression of apoptosis-regulatory proteins Bid, Bcl-2, Bcl-X, Bax and Bak during development of murine nervous system. Cell Death Differ 2002; 9: 145-157.
    • (2002) Cell Death Differ , vol.9 , pp. 145-157
    • Krajewska, M.1    Mai, J.K.2    Zapata, J.M.3    Ashwell, K.W.4    Schendel, S.L.5    Reed, J.C.6
  • 24
    • 84859428688 scopus 로고    scopus 로고
    • Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
    • Greene AW, Grenier K, Aguileta MA, Muise S, Farazifard R, Haque ME et al. Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment. EMBO Rep 2012; 13: 378-385.
    • (2012) EMBO Rep , vol.13 , pp. 378-385
    • Greene, A.W.1    Grenier, K.2    Aguileta, M.A.3    Muise, S.4    Farazifard, R.5    Haque, M.E.6
  • 25
    • 34248998801 scopus 로고    scopus 로고
    • Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1
    • Maiuri MC, Le Toumelin G, Criollo A, Rain JC, Gautier F, Juin P et al. Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1. EMBO J 2007; 26: 2527-2539.
    • (2007) EMBO J , vol.26 , pp. 2527-2539
    • Maiuri, M.C.1    Le Toumelin, G.2    Criollo, A.3    Rain, J.C.4    Gautier, F.5    Juin, P.6
  • 26
  • 28
    • 84859763961 scopus 로고    scopus 로고
    • Alternative macroautophagic pathways
    • Juenemann K, Reits EA. Alternative macroautophagic pathways. Int J Cell Biol 2012; 2012: 189794.
    • (2012) Int J Cell Biol , vol.2012 , pp. 189794
    • Juenemann, K.1    Reits, E.A.2
  • 29
    • 58149090998 scopus 로고    scopus 로고
    • Identification of the major phosphorylation site in Bcl-xL induced by microtubule inhibitors and analysis of its functional significance
    • Upreti M, Galitovskaya EN, Chu R, Tackett AJ, Terrano DT, Granell S et al. Identification of the major phosphorylation site in Bcl-xL induced by microtubule inhibitors and analysis of its functional significance. J Biol Chem 2008; 283: 35517-35525.
    • (2008) J Biol Chem , vol.283 , pp. 35517-35525
    • Upreti, M.1    Galitovskaya, E.N.2    Chu, R.3    Tackett, A.J.4    Terrano, D.T.5    Granell, S.6
  • 30
    • 12444306413 scopus 로고    scopus 로고
    • Characterization of vinblastine-induced Bcl-xL and Bcl-2 phosphorylation: Evidence for a novel protein kinase and a coordinated phosphorylation/ dephosphorylation cycle associated with apoptosis induction
    • Du L, Lyle CS, Chambers TC. Characterization of vinblastine-induced Bcl-xL and Bcl-2 phosphorylation: evidence for a novel protein kinase and a coordinated phosphorylation/dephosphorylation cycle associated with apoptosis induction. Oncogene 2005; 24: 107-117.
    • (2005) Oncogene , vol.24 , pp. 107-117
    • Du, L.1    Lyle, C.S.2    Chambers, T.C.3
  • 31
    • 0036784080 scopus 로고    scopus 로고
    • Inhibition of bcl-x(l) phosphorylation by tea polyphenols or epigallocatechin-3-gallate is associated with prostate cancer cell apoptosis
    • Kazi A, Smith DM, Zhong Q, Dou QP. Inhibition of bcl-x(l) phosphorylation by tea polyphenols or epigallocatechin-3-gallate is associated with prostate cancer cell apoptosis. Mol Pharmacol 2002; 62: 765-771.
    • (2002) Mol Pharmacol , vol.62 , pp. 765-771
    • Kazi, A.1    Smith, D.M.2    Zhong, Q.3    Dou, Q.P.4
  • 32
    • 77950087454 scopus 로고    scopus 로고
    • Synchronised phosphorylation of BNIP3, Bcl-2 and Bcl-xL in response to microtubule-active drugs is JNK-independent and requires a mitotic kinase
    • Mellor HR, Rouschop KM, Wigfield SM, Wouters BG, Harris AL. Synchronised phosphorylation of BNIP3, Bcl-2 and Bcl-xL in response to microtubule-active drugs is JNK-independent and requires a mitotic kinase. Biochem Pharmacol 2010; 79: 1562-1572.
    • (2010) Biochem Pharmacol , vol.79 , pp. 1562-1572
    • Mellor, H.R.1    Rouschop, K.M.2    Wigfield, S.M.3    Wouters, B.G.4    Harris, A.L.5
  • 33
    • 48249092267 scopus 로고    scopus 로고
    • Bcl-2 family members: Dual regulators of apoptosis and autophagy
    • Levine B, Sinha S, Kroemer G. Bcl-2 family members: dual regulators of apoptosis and autophagy. Autophagy 2008; 4: 600-606.
    • (2008) Autophagy , vol.4 , pp. 600-606
    • Levine, B.1    Sinha, S.2    Kroemer, G.3
  • 34
    • 79953276389 scopus 로고    scopus 로고
    • Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol
    • Edlich F, Banerjee S, Suzuki M, Cleland MM, Arnoult D, Wang C et al. Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol. Cell 2011; 145: 104-116.
    • (2011) Cell , vol.145 , pp. 104-116
    • Edlich, F.1    Banerjee, S.2    Suzuki, M.3    Cleland, M.M.4    Arnoult, D.5    Wang, C.6
  • 35
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S, Konishi A, Kodama T, Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc Natl Acad Sci USA 2000; 97: 3100-3105.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 38
    • 35148865254 scopus 로고    scopus 로고
    • Are Parkinson disease patients protected from some but not all cancers?
    • Inzelberg R, Jankovic J. Are Parkinson disease patients protected from some but not all cancers? Neurology 2007; 69: 1542-1550.
    • (2007) Neurology , vol.69 , pp. 1542-1550
    • Inzelberg, R.1    Jankovic, J.2
  • 39
    • 0035958558 scopus 로고    scopus 로고
    • Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway
    • Unoki M, Nakamura Y. Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway. Oncogene 2001; 20: 4457-4465.
    • (2001) Oncogene , vol.20 , pp. 4457-4465
    • Unoki, M.1    Nakamura, Y.2
  • 40
    • 78650006375 scopus 로고    scopus 로고
    • PINK1 displays tissue-specific subcellular location and regulates apoptosis and cell growth in breast cancer cells
    • Berthier A, Navarro S, Jimenez-Sainz J, Rogla I, Ripoll F, Cervera J et al. PINK1 displays tissue-specific subcellular location and regulates apoptosis and cell growth in breast cancer cells. Hum Pathol 2011; 42: 75-87.
    • (2011) Hum Pathol , vol.42 , pp. 75-87
    • Berthier, A.1    Navarro, S.2    Jimenez-Sainz, J.3    Rogla, I.4    Ripoll, F.5    Cervera, J.6
  • 41
    • 84856299100 scopus 로고    scopus 로고
    • Partial sensitization of human bladder cancer cells to a gene-therapeutic
    • Jin Y, Murata H, Sakaguchi M, Kataoka K, Watanabe M, Nasu Y et al. Partial sensitization of human bladder cancer cells to a gene-therapeutic. Oncol Rep 2012; 27: 695-699.
    • (2012) Oncol Rep , vol.27 , pp. 695-699
    • Jin, Y.1    Murata, H.2    Sakaguchi, M.3    Kataoka, K.4    Watanabe, M.5    Nasu, Y.6
  • 42
    • 58149473473 scopus 로고    scopus 로고
    • Kinase-inactivated ULK. proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism
    • Chan EY, Longatti A, McKnight NC, Tooze SA, Kinase-inactivated ULK. proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism. Mol Cell Biol 2009; 29: 157-171.
    • (2009) Mol Cell Biol , vol.29 , pp. 157-171
    • Chan, E.Y.1    Longatti, A.2    McKnight, N.C.3    Tooze, S.A.4
  • 43
    • 0034729759 scopus 로고    scopus 로고
    • Unmasking of phosphorylation-sensitive epitopes on p53 and Mdm2 by a simple Western-phosphatase procedure
    • Maya R, Oren M. Unmasking of phosphorylation-sensitive epitopes on p53 and Mdm2 by a simple Western-phosphatase procedure. Oncogene 2000; 19: 3213-3215.
    • (2000) Oncogene , vol.19 , pp. 3213-3215
    • Maya, R.1    Oren, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.