메뉴 건너뛰기




Volumn 10, Issue 12, 2014, Pages

Phosphorylation of Mitochondrial Polyubiquitin by PINK1 Promotes Parkin Mitochondrial Tethering

Author keywords

[No Author keywords available]

Indexed keywords

PARKIN; POLYUBIQUITIN; PROTEIN PINK1; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; PROTEIN BINDING; PROTEIN KINASE; PTEN-INDUCED PUTATIVE KINASE; UBIQUITIN PROTEIN LIGASE;

EID: 84919629959     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004861     Document Type: Article
Times cited : (141)

References (51)
  • 1
    • 84896870884 scopus 로고    scopus 로고
    • RBR E3 ubiquitin ligases: new structures, new insights, new question
    • Spratt DE, Walden H, Shaw GS, (2014) RBR E3 ubiquitin ligases: new structures, new insights, new questions. Biochem J 458: 421–437.
    • (2014) Biochem J , vol.458 , pp. 421-437
    • Spratt, D.E.1    Walden, H.2    Shaw, G.S.3
  • 2
    • 67649383293 scopus 로고    scopus 로고
    • Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parki
    • Hristova VA, Beasley SA, Rylett RJ, Shaw GS, (2009) Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin. J Biol Chem 284: 14978–14986.
    • (2009) J Biol Chem , vol.284 , pp. 14978-14986
    • Hristova, V.A.1    Beasley, S.A.2    Rylett, R.J.3    Shaw, G.S.4
  • 3
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonis
    • Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605–608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5
  • 4
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parki
    • Clark IE, Dodson MW, Jiang C, Cao JH, Huh JR, et al. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441: 1162–1166.
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5
  • 5
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parki
    • Park J, Lee SB, Lee S, Kim Y, Song S, et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441: 1157–1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5
  • 6
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parki
    • Yang Y, Gehrke S, Imai Y, Huang Z, Ouyang Y, et al. (2006) Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc Natl Acad Sci U S A 103: 10793–10798.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3    Huang, Z.4    Ouyang, Y.5
  • 9
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophag
    • Matsuda N, Sato S, Shiba K, Okatsu K, Saisho K, et al. (2010) PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol 189: 211–221.
    • (2010) J Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5
  • 10
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parki
    • Narendra DP, Jin SM, Tanaka A, Suen DF, Gautier CA, et al. (2010) PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol 8: e1000298.
    • (2010) PLoS Biol , vol.8 , pp. 1000298
    • Narendra, D.P.1    Jin, S.M.2    Tanaka, A.3    Suen, D.F.4    Gautier, C.A.5
  • 11
    • 77950371695 scopus 로고    scopus 로고
    • PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophag
    • Kawajiri S, Saiki S, Sato S, Sato F, Hatano T, et al. (2010) PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy. FEBS Lett 584: 1073–1079.
    • (2010) FEBS Lett , vol.584 , pp. 1073-1079
    • Kawajiri, S.1    Saiki, S.2    Sato, S.3    Sato, F.4    Hatano, T.5
  • 12
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK
    • Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, et al. (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304: 1158–1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5
  • 13
    • 37549029702 scopus 로고    scopus 로고
    • Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK
    • Takatori S, Ito G, Iwatsubo T, (2008) Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1. Neurosci Lett 430: 13–17.
    • (2008) Neurosci Lett , vol.430 , pp. 13-17
    • Takatori, S.1    Ito, G.2    Iwatsubo, T.3
  • 14
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathwa
    • Yamano K, Youle RJ, (2013) PINK1 is degraded through the N-end rule pathway. Autophagy 9: 1758–1769.
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 15
    • 84864267876 scopus 로고    scopus 로고
    • PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 6
    • Kondapalli C, Kazlauskaite A, Zhang N, Woodroof HI, Campbell DG, et al. (2012) PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol 2: 120080.
    • (2012) Open Biol , vol.2 , pp. 120080
    • Kondapalli, C.1    Kazlauskaite, A.2    Zhang, N.3    Woodroof, H.I.4    Campbell, D.G.5
  • 16
    • 84866072587 scopus 로고    scopus 로고
    • PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondri
    • Okatsu K, Oka T, Iguchi M, Imamura K, Kosako H, et al. (2012) PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nat Commun 3: 1016.
    • (2012) Nat Commun , vol.3 , pp. 1016
    • Okatsu, K.1    Oka, T.2    Iguchi, M.3    Imamura, K.4    Kosako, H.5
  • 17
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophag
    • Narendra D, Tanaka A, Suen DF, Youle RJ, (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 795–803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 18
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parki
    • Tanaka A, Cleland MM, Xu S, Narendra DP, Suen DF, et al. (2010) Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J Cell Biol 191: 1367–1380.
    • (2010) J Cell Biol , vol.191 , pp. 1367-1380
    • Tanaka, A.1    Cleland, M.M.2    Xu, S.3    Narendra, D.P.4    Suen, D.F.5
  • 19
    • 77954695260 scopus 로고    scopus 로고
    • p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondri
    • Okatsu K, Saisho K, Shimanuki M, Nakada K, Shitara H, et al. (2010) p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria. Genes Cells 15: 887–900.
    • (2010) Genes Cells , vol.15 , pp. 887-900
    • Okatsu, K.1    Saisho, K.2    Shimanuki, M.3    Nakada, K.4    Shitara, H.5
  • 20
    • 79954520907 scopus 로고    scopus 로고
    • Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophag
    • Chan NC, Salazar AM, Pham AH, Sweredoski MJ, Kolawa NJ, et al. (2011) Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy. Hum Mol Genet 20: 1726–1737.
    • (2011) Hum Mol Genet , vol.20 , pp. 1726-1737
    • Chan, N.C.1    Salazar, A.M.2    Pham, A.H.3    Sweredoski, M.J.4    Kolawa, N.J.5
  • 21
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrid
    • Wenzel DM, Lissounov A, Brzovic PS, Klevit RE, (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474: 105–108.
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 22
    • 84873045973 scopus 로고    scopus 로고
    • PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial bindin
    • Lazarou M, Narendra DP, Jin SM, Tekle E, Banerjee S, et al. (2013) PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J Cell Biol 200: 163–172.
    • (2013) J Cell Biol , vol.200 , pp. 163-172
    • Lazarou, M.1    Narendra, D.P.2    Jin, S.M.3    Tekle, E.4    Banerjee, S.5
  • 23
    • 79960649509 scopus 로고    scopus 로고
    • Autoregulation of Parkin activity through its ubiquitin-like domai
    • Chaugule VK, Burchell L, Barber KR, Sidhu A, Leslie SJ, et al. (2011) Autoregulation of Parkin activity through its ubiquitin-like domain. EMBO J 30: 2853–2867.
    • (2011) EMBO J , vol.30 , pp. 2853-2867
    • Chaugule, V.K.1    Burchell, L.2    Barber, K.R.3    Sidhu, A.4    Leslie, S.J.5
  • 24
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophag
    • Shiba-Fukushima K, Imai Y, Yoshida S, Ishihama Y, Kanao T, et al. (2012) PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep 2: 1002.
    • (2012) Sci Rep , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5
  • 25
  • 26
    • 84899539731 scopus 로고    scopus 로고
    • PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activit
    • Kane LA, Lazarou M, Fogel AI, Li Y, Yamano K, et al. (2014) PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol 205: 143–153.
    • (2014) J Cell Biol , vol.205 , pp. 143-153
    • Kane, L.A.1    Lazarou, M.2    Fogel, A.I.3    Li, Y.4    Yamano, K.5
  • 27
    • 84901751574 scopus 로고    scopus 로고
    • Ubiquitin is phosphorylated by PINK1 to activate parki
    • Koyano K, Okatsu K, Kosako H, Tamura Y, Go E, et al. (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510: 162–166.
    • (2014) Nature , vol.510 , pp. 162-166
    • Koyano, K.1    Okatsu, K.2    Kosako, H.3    Tamura, Y.4    Go, E.5
  • 28
    • 34250007128 scopus 로고    scopus 로고
    • The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress toleranc
    • Ryu KY, Maehr R, Gilchrist CA, Long MA, Bouley DM, et al. (2007) The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance. EMBO J 26: 2693–2706.
    • (2007) EMBO J , vol.26 , pp. 2693-2706
    • Ryu, K.Y.1    Maehr, R.2    Gilchrist, C.A.3    Long, M.A.4    Bouley, D.M.5
  • 29
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanis
    • Zheng X, Hunter T, (2013) Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res 23: 886–897.
    • (2013) Cell Res , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2
  • 30
    • 84879251778 scopus 로고    scopus 로고
    • Structure of parkin reveals mechanisms for ubiquitin ligase activatio
    • Trempe JF, Sauve V, Grenier K, Seirafi M, Tang MY, et al. (2013) Structure of parkin reveals mechanisms for ubiquitin ligase activation. Science 340: 1451–1455.
    • (2013) Science , vol.340 , pp. 1451-1455
    • Trempe, J.F.1    Sauve, V.2    Grenier, K.3    Seirafi, M.4    Tang, M.Y.5
  • 31
    • 84881477223 scopus 로고    scopus 로고
    • Structure of the human Parkin ligase domain in an autoinhibited stat
    • Wauer T, Komander D, (2013) Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J 32: 2099–2112.
    • (2013) EMBO J , vol.32 , pp. 2099-2112
    • Wauer, T.1    Komander, D.2
  • 32
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusi
    • Ziviani E, Tao RN, Whitworth AJ, (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A 107: 5018–5023.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 33
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathwa
    • Poole AC, Thomas RE, Yu S, Vincow ES, Pallanck L, (2010) The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. PLoS One 5: e10054.
    • (2010) PLoS One , vol.5 , pp. 10054
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 34
    • 84876886863 scopus 로고    scopus 로고
    • The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEM
    • Muller-Rischart AK, Pilsl A, Beaudette P, Patra M, Hadian K, et al. (2013) The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO. Mol Cell 49: 908–921.
    • (2013) Mol Cell , vol.49 , pp. 908-921
    • Muller-Rischart, A.K.1    Pilsl, A.2    Beaudette, P.3    Patra, M.4    Hadian, K.5
  • 35
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-kappaB activatio
    • Tokunaga F, Sakata S, Saeki Y, Satomi Y, Kirisako T, et al. (2009) Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation. Nat Cell Biol 11: 123–132.
    • (2009) Nat Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1    Sakata, S.2    Saeki, Y.3    Satomi, Y.4    Kirisako, T.5
  • 36
    • 84878118233 scopus 로고    scopus 로고
    • Parkin overexpression during aging reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespa
    • Rana A, Rera M, Walker DW, (2013) Parkin overexpression during aging reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan. Proc Natl Acad Sci U S A 110: 8638–8643.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 8638-8643
    • Rana, A.1    Rera, M.2    Walker, D.W.3
  • 37
    • 84922434418 scopus 로고    scopus 로고
    • Ordureau A, Sarraf SA, Duda DM, Heo JM, Jedrychowski MP, et al. (2014) Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis. Mol Cell. in press
  • 38
    • 84912061592 scopus 로고    scopus 로고
    • Shiba-Fukushima K, Inoshita T, Hattori N, Imai Y (2014) Lysine 63-Linked Polyubiquitination Is Dispensable for Parkin-Mediated Mitophagy. J Biol Chem. in press
  • 39
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activit
    • Imai Y, Soda M, Takahashi R, (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 275: 35661–35664.
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 41
    • 84903485895 scopus 로고    scopus 로고
    • PINK1-Mediated Phosphorylation of Parkin Boosts Parkin Activity in Drosophil
    • Shiba-Fukushima K, Inoshita T, Hattori N, Imai Y, (2014) PINK1-Mediated Phosphorylation of Parkin Boosts Parkin Activity in Drosophila. PLoS Genet 10: e1004391.
    • (2014) PLoS Genet , vol.10 , pp. 1004391
    • Shiba-Fukushima, K.1    Inoshita, T.2    Hattori, N.3    Imai, Y.4
  • 42
    • 84878931274 scopus 로고    scopus 로고
    • PINK1 rendered temperature sensitive by disease-associated and engineered mutation
    • Narendra DP, Wang C, Youle RJ, Walker JE, (2013) PINK1 rendered temperature sensitive by disease-associated and engineered mutations. Hum Mol Genet 22: 2572–2589.
    • (2013) Hum Mol Genet , vol.22 , pp. 2572-2589
    • Narendra, D.P.1    Wang, C.2    Youle, R.J.3    Walker, J.E.4
  • 43
    • 84893856499 scopus 로고    scopus 로고
    • Phosphoproteome analysis of formalin-fixed and paraffin-embedded tissue sections mounted on microscope slide
    • Wakabayashi M, Yoshihara H, Masuda T, Tsukahara M, Sugiyama N, et al. (2014) Phosphoproteome analysis of formalin-fixed and paraffin-embedded tissue sections mounted on microscope slides. J Proteome Res 13: 915–924.
    • (2014) J Proteome Res , vol.13 , pp. 915-924
    • Wakabayashi, M.1    Yoshihara, H.2    Masuda, T.3    Tsukahara, M.4    Sugiyama, N.5
  • 44
    • 84857059905 scopus 로고    scopus 로고
    • Human proteome analysis by using reversed phase monolithic silica capillary columns with enhanced sensitivit
    • Iwasaki M, Sugiyama N, Tanaka N, Ishihama Y, (2012) Human proteome analysis by using reversed phase monolithic silica capillary columns with enhanced sensitivity. J Chromatogr A 1228: 292–297.
    • (2012) J Chromatogr A , vol.1228 , pp. 292-297
    • Iwasaki, M.1    Sugiyama, N.2    Tanaka, N.3    Ishihama, Y.4
  • 45
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localizatio
    • Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP, (2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol 24: 1285–1292.
    • (2006) Nat Biotechnol , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 46
    • 84864197915 scopus 로고    scopus 로고
    • Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutation
    • Woodroof HI, Pogson JH, Begley M, Cantley LC, Deak M, et al. (2011) Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations. Open Biol 1: 110012.
    • (2011) Open Biol , vol.1 , pp. 110012
    • Woodroof, H.I.1    Pogson, J.H.2    Begley, M.3    Cantley, L.C.4    Deak, M.5
  • 47
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosi
    • Ellenberg J, Siggia ED, Moreira JE, Smith CL, Presley JF, et al. (1997) Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J Cell Biol 138: 1193–1206.
    • (1997) J Cell Biol , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5
  • 48
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stres
    • Pesah Y, Pham T, Burgess H, Middlebrooks B, Verstreken P, et al. (2004) Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131: 2183–2194.
    • (2004) Development , vol.131 , pp. 2183-2194
    • Pesah, Y.1    Pham, T.2    Burgess, H.3    Middlebrooks, B.4    Verstreken, P.5
  • 49
    • 22544458436 scopus 로고    scopus 로고
    • Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophil
    • Cha GH, Kim S, Park J, Lee E, Kim M, et al. (2005) Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila. Proc Natl Acad Sci U S A 102: 10345–10350.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10345-10350
    • Cha, G.H.1    Kim, S.2    Park, J.3    Lee, E.4    Kim, M.5
  • 50
    • 78650716707 scopus 로고    scopus 로고
    • The loss of PGAM5 suppresses the mitochondrial degeneration caused by inactivation of PINK1 in Drosophil
    • Imai Y, Kanao T, Sawada T, Kobayashi Y, Moriwaki Y, et al. (2010) The loss of PGAM5 suppresses the mitochondrial degeneration caused by inactivation of PINK1 in Drosophila. PLoS Genet 6: e1001229.
    • (2010) PLoS Genet , vol.6 , pp. 1001229
    • Imai, Y.1    Kanao, T.2    Sawada, T.3    Kobayashi, Y.4    Moriwaki, Y.5
  • 51
    • 51949090816 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophil
    • Imai Y, Gehrke S, Wang HQ, Takahashi R, Hasegawa K, et al. (2008) Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila. EMBO J 27: 2432–2443.
    • (2008) EMBO J , vol.27 , pp. 2432-2443
    • Imai, Y.1    Gehrke, S.2    Wang, H.Q.3    Takahashi, R.4    Hasegawa, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.