메뉴 건너뛰기




Volumn 209, Issue 1, 2015, Pages 111-128

Phosphorylated ubiquitin chain is the genuine Parkin receptor

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN; POLYUBIQUITIN; PROTEIN SERINE THREONINE KINASE; PTEN INDUCED PUTATIVE KINASE 1; RECOMBINANT PARKIN; RECOMBINANT PROTEIN; RECOMBINANT RECEPTOR; TETRA UBIQUITIN; TETRA UBIQUITIN(S65D); UNCLASSIFIED DRUG; PARKIN; PROTEIN BINDING; PROTEIN KINASE; PTEN-INDUCED PUTATIVE KINASE; UBIQUITIN PROTEIN LIGASE;

EID: 84922794336     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201410050     Document Type: Article
Times cited : (211)

References (68)
  • 3
    • 79960649509 scopus 로고    scopus 로고
    • Autoregulation of Parkin activity through its ubiquitin-like domain
    • Chaugule, V.K., L. Burchell, K.R. Barber, A. Sidhu, S.J. Leslie, G.S. Shaw, and H. Walden. 2011. Autoregulation of Parkin activity through its ubiquitin-like domain. EMBO J. 30:2853-2867. http://dx.doi.org/10.1038/emboj.2011.204
    • (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    Shaw, G.S.6    Walden, H.7
  • 4
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Chen, Y., and G.W. Dorn II. 2013. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science. 340:471-475. http://dx.doi.org/10.1126/science.1231031
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 5
    • 84883542252 scopus 로고    scopus 로고
    • Ubiquitination-induced fluorescence complementation (UiFC) for detection of K48 ubiquitin chains in vitro and in live cells
    • Chen, Z., Y. Zhong, Y. Wang, S. Xu, Z. Liu, I.V. Baskakov, M.J. Monteiro, M. Karbowski, Y. Shen, and S. Fang. 2013. Ubiquitination-induced fluorescence complementation (UiFC) for detection of K48 ubiquitin chains in vitro and in live cells. PLoS ONE. 8:e73482.
    • (2013) PLoS ONE , vol.8
    • Chen, Z.1    Zhong, Y.2    Wang, Y.3    Xu, S.4    Liu, Z.5    Baskakov, I.V.6    Monteiro, M.J.7    Karbowski, M.8    Shen, Y.9    Fang, S.10
  • 6
    • 79957517961 scopus 로고    scopus 로고
    • Parkin mediates apparent E2-independent monoubiquitination in vitro and contains an intrinsic activity that catalyzes polyubiquitination
    • Chew, K.C., N. Matsuda, K. Saisho, G.G. Lim, C. Chai, H.M. Tan, K. Tanaka, and K.L. Lim. 2011. Parkin mediates apparent E2-independent monoubiquitination in vitro and contains an intrinsic activity that catalyzes polyubiquitination. PLoS ONE. 6:e19720. http://dx.doi.org/10.1371/journal.pone.0019720
    • (2011) PLoS ONE , vol.6
    • Chew, K.C.1    Matsuda, N.2    Saisho, K.3    Lim, G.G.4    Chai, C.5    Tan, H.M.6    Tanaka, K.7    Lim, K.L.8
  • 7
    • 84866006042 scopus 로고    scopus 로고
    • Governance of endocytic trafficking and signaling by reversible ubiquitylation
    • Clague, M.J., H. Liu, and S. Urbé. 2012. Governance of endocytic trafficking and signaling by reversible ubiquitylation. Dev. Cell. 23:457-467. http://dx.doi.org/10.1016/j.devcel.2012.08.011
    • (2012) Dev. Cell , vol.23 , pp. 457-467
    • Clague, M.J.1    Liu, H.2    Urbé, S.3
  • 8
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark, I.E., M.W. Dodson, C. Jiang, J.H. Cao, J.R. Huh, J.H. Seol, S.J. Yoo, B.A. Hay, and M. Guo. 2006. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature. 441:1162-1166. http://dx.doi.org/10.1038/nature04779
    • (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    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 10
    • 84906071009 scopus 로고    scopus 로고
    • A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently
    • Fiesel, F.C., E.L. Moussaud-Lamodière, M. Ando, and W. Springer. 2014. A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently. J. Cell Sci. 127:3488-3504. http://dx.doi.org/10.1242/jcs.147520
    • (2014) J. Cell Sci. , vol.127 , pp. 3488-3504
    • Fiesel, F.C.1    Moussaud-Lamodière, E.L.2    Ando, M.3    Springer, W.4
  • 11
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkindependent manner upon induction of mitophagy
    • Gegg, M.E., J.M. Cooper, K.Y. Chau, M. Rojo, A.H. Schapira, and J.W. Taanman. 2010. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkindependent manner upon induction of mitophagy. Hum. Mol. Genet. 19:4861-4870. http://dx.doi.org/10.1093/hmg/ddq419
    • (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
  • 13
    • 84905482172 scopus 로고    scopus 로고
    • The ubiquitinconjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy
    • Geisler, S., S. Vollmer, S. Golombek, and P.J. Kahle. 2014. The ubiquitinconjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy. J. Cell Sci. 127:3280-3293. http://dx.doi.org/10.1242/jcs.146035
    • (2014) J. Cell Sci. , vol.127 , pp. 3280-3293
    • Geisler, S.1    Vollmer, S.2    Golombek, S.3    Kahle, P.J.4
  • 17
    • 84857850213 scopus 로고    scopus 로고
    • Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy
    • Itakura, E., C. Kishi-Itakura, I. Koyama-Honda, and N. Mizushima. 2012. Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J. Cell Sci. 125:1488-1499. http://dx.doi.org/10.1242/jcs.094110
    • (2012) J. Cell Sci. , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3    Mizushima, N.4
  • 20
    • 33645714857 scopus 로고    scopus 로고
    • Phosphate-binding tag, a new tool to visualize phosphorylated proteins
    • Kinoshita, E., E. Kinoshita-Kikuta, K. Takiyama, and T. Koike. 2006. Phosphate-binding tag, a new tool to visualize phosphorylated proteins. Mol. Cell. Proteomics. 5:749-757. http://dx.doi.org/10.1074/mcp.T500024-MCP200
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 749-757
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Takiyama, K.3    Koike, T.4
  • 21
    • 84855963980 scopus 로고    scopus 로고
    • Phos-tag SDS-PAGE systems for phosphorylation profiling of proteins with a wide range of molecular masses under neutral pH conditions
    • Kinoshita, E., E. Kinoshita-Kikuta, and T. Koike. 2012. Phos-tag SDS-PAGE systems for phosphorylation profiling of proteins with a wide range of molecular masses under neutral pH conditions. Proteomics. 12:192-202. http://dx.doi.org/10.1002/pmic.201100524
    • (2012) Proteomics , vol.12 , pp. 192-202
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Koike, T.3
  • 23
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander, D., F. Reyes-Turcu, J.D. Licchesi, P. Odenwaelder, K.D. Wilkinson, and D. Barford. 2009. Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep. 10:466-473. http://dx.doi.org/10.1038/embor.2009.55
    • (2009) EMBO Rep. , vol.10 , pp. 466-473
    • Komander, D.1    Reyes-Turcu, F.2    Licchesi, J.D.3    Odenwaelder, P.4    Wilkinson, K.D.5    Barford, D.6
  • 26
    • 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., S.M. Jin, L.A. Kane, and R.J. Youle. 2012. 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. http://dx.doi.org/10.1016/j.devcel.2011.12.014
    • (2012) Dev. Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 27
    • 84873045973 scopus 로고    scopus 로고
    • PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
    • Lazarou, M., D.P. Narendra, S.M. Jin, E. Tekle, S. Banerjee, and R.J. Youle. 2013. PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J. Cell Biol. 200:163-172. http://dx.doi.org/10.1083/jcb.201210111
    • (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    Youle, R.J.6
  • 28
    • 84859237566 scopus 로고    scopus 로고
    • Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria
    • Liu, S., T. Sawada, S. Lee, W. Yu, G. Silverio, P. Alapatt, I. Millan, A. Shen, W. Saxton, T. Kanao, et al. 2012. Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria. PLoS Genet. 8:e1002537. http://dx.doi.org/10.1371/journal.pgen.1002537
    • (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
  • 30
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda, N., S. Sato, K. Shiba, K. Okatsu, K. Saisho, C.A. Gautier, Y.S. Sou, S. Saiki, S. Kawajiri, F. Sato, 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. http://dx.doi.org/10.1083/jcb.200910140
    • (2010) J. Cell Biol. , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6    Sou, Y.S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 31
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., A. Tanaka, D.F. Suen, and R.J. Youle. 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
  • 32
    • 78649300971 scopus 로고    scopus 로고
    • p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra, D., L.A. Kane, D.N. Hauser, I.M. Fearnley, and R.J. Youle. 2010a. p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy. 6:1090-1106. http://dx.doi.org/10.4161/auto.6.8.13426
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 34
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism
    • Narendra, D., J.E. Walker, and R. Youle. 2012. Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism. Cold Spring Harb. Perspect. Biol. 4:a011338. http://dx.doi.org/10.1101/cshperspect.a011338
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Narendra, D.1    Walker, J.E.2    Youle, R.3
  • 38
    • 84866072587 scopus 로고    scopus 로고
    • PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
    • Okatsu, K., T. Oka, M. Iguchi, K. Imamura, H. Kosako, N. Tani, M. Kimura, E. Go, F. Koyano, M. Funayama, et al. 2012b. PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nat. Commun. 3:1016. http://dx.doi.org/10.1038/ncomms2016
    • (2012) Nat. Commun. , vol.3 , pp. 1016
    • Okatsu, K.1    Oka, T.2    Iguchi, M.3    Imamura, K.4    Kosako, H.5    Tani, N.6    Kimura, M.7    Go, E.8    Koyano, F.9    Funayama, M.10
  • 39
    • 84890957474 scopus 로고    scopus 로고
    • A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment
    • Okatsu, K., M. Uno, F. Koyano, E. Go, M. Kimura, T. Oka, K. Tanaka, and N. Matsuda. 2013. A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment. J. Biol. Chem. 288:36372-36384. http://dx.doi.org/10.1074/jbc. M113.509653
    • (2013) J. Biol. Chem. , vol.288 , pp. 36372-36384
    • Okatsu, K.1    Uno, M.2    Koyano, F.3    Go, E.4    Kimura, M.5    Oka, T.6    Tanaka, K.7    Matsuda, N.8
  • 40
    • 84901044873 scopus 로고    scopus 로고
    • Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulate PTS1 protein import
    • Okumoto, K., H. Noda, and Y. Fujiki. 2014. Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulate PTS1 protein import. J. Biol. Chem. 289:14089-14108. http://dx.doi.org/10.1074/jbc. M113.527937
    • (2014) J. Biol. Chem. , vol.289 , pp. 14089-14108
    • Okumoto, K.1    Noda, H.2    Fujiki, Y.3
  • 42
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park, J., S.B. Lee, S. Lee, Y. Kim, S. Song, S. Kim, E. Bae, J. Kim, M. Shong, J.M. Kim, and J. Chung. 2006. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature. 441:1157-1161. http://dx.doi.org/10.1038/nature04788
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.M.10    Chung, J.11
  • 43
    • 70350447348 scopus 로고    scopus 로고
    • Pex2 and pex12 function as protein-ubiquitin ligases in peroxisomal protein import
    • Platta, H.W., F. El Magraoui, B.E. Bäumer, D. Schlee, W. Girzalsky, and R. Erdmann. 2009. Pex2 and pex12 function as protein-ubiquitin ligases in peroxisomal protein import. Mol. Cell. Biol. 29:5505-5516. http://dx.doi.org/10.1128/MCB.00388-09
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5505-5516
    • Platta, H.W.1    El Magraoui, F.2    Bäumer, B.E.3    Schlee, D.4    Girzalsky, W.5    Erdmann, R.6
  • 44
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway
    • Poole, A.C., R.E. Thomas, S. Yu, E.S. Vincow, and L. Pallanck. 2010. The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. PLoS ONE. 5:e10054. http://dx.doi.org/10.1371/journal.pone.0010054
    • (2010) PLoS ONE , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 47
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Saeki, Y., T. Kudo, T. Sone, Y. Kikuchi, H. Yokosawa, A. Toh-e, and K. Tanaka. 2009. Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J. 28:359-371. http://dx.doi.org/10.1038/emboj.2008.305
    • (2009) EMBO J. , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-e, A.6    Tanaka, K.7
  • 48
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • Sarraf, S.A., M. Raman, V. Guarani-Pereira, M.E. Sowa, E.L. Huttlin, S.P. Gygi, and J.W. Harper. 2013. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature. 496:372-376. http://dx.doi.org/10.1038/nature12043
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3    Sowa, M.E.4    Huttlin, E.L.5    Gygi, S.P.6    Harper, J.W.7
  • 49
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the Parkin ubiquitinlike domain primes mitochondrial translocation of Parkin and regulates mitophagy
    • Shiba-Fukushima, K., Y. Imai, S. Yoshida, Y. Ishihama, T. Kanao, S. Sato, and N. Hattori. 2012. PINK1-mediated phosphorylation of the Parkin ubiquitinlike domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep. 2:1002. http://dx.doi.org/10.1038/srep01002
    • (2012) Sci Rep , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5    Sato, S.6    Hattori, N.7
  • 54
    • 84866300942 scopus 로고    scopus 로고
    • Fluorescence-based sensors to monitor localization and functions of linear and K63-linked ubiquitin chains in cells
    • van Wijk, S.J., E. Fiskin, M. Putyrski, F. Pampaloni, J. Hou, P. Wild, T. Kensche, H.E. Grecco, P. Bastiaens, and I. Dikic. 2012. Fluorescence-based sensors to monitor localization and functions of linear and K63-linked ubiquitin chains in cells. Mol. Cell. 47:797-809. http://dx.doi.org/10.1016/j.molcel.2012.06.017
    • (2012) Mol. Cell , vol.47 , pp. 797-809
    • van Wijk, S.J.1    Fiskin, E.2    Putyrski, M.3    Pampaloni, F.4    Hou, J.5    Wild, P.6    Kensche, T.7    Grecco, H.E.8    Bastiaens, P.9    Dikic, I.10
  • 56
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • Wang, X., D. Winter, G. Ashrafi, J. Schlehe, Y.L. Wong, D. Selkoe, S. Rice, J. Steen, M.J. LaVoie, and T.L. Schwarz. 2011. PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell. 147:893-906. http://dx.doi.org/10.1016/j.cell.2011.10.018
    • (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
  • 57
    • 84881477223 scopus 로고    scopus 로고
    • Structure of the human Parkin ligase domain in an autoinhibited state
    • Wauer, T., and D. Komander. 2013. Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J. 32:2099-2112. http://dx.doi.org/10.1038/emboj.2013.125
    • (2013) EMBO J. , vol.32 , pp. 2099-2112
    • Wauer, T.1    Komander, D.2
  • 58
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel, D.M., A. Lissounov, P.S. Brzovic, and R.E. Klevit. 2011. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature. 474:105-108. http://dx.doi.org/10.1038/nature09966
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 59
    • 34248359155 scopus 로고    scopus 로고
    • MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity
    • Wiley, S.E., A.N. Murphy, S.A. Ross, P. van der Geer, and J.E. Dixon. 2007. MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. Proc. Natl. Acad. Sci. USA. 104:5318-5323. http://dx.doi.org/10.1073/pnas.0701078104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5318-5323
    • Wiley, S.E.1    Murphy, A.N.2    Ross, S.A.3    van der Geer, P.4    Dixon, J.E.5
  • 61
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNF? and IL-1?
    • Xu, M., B. Skaug, W. Zeng, and Z.J. Chen. 2009. A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNF? and IL-1?. Mol. Cell. 36:302-314. http://dx.doi.org/10.1016/j.molcel.2009.10.002
    • (2009) Mol. Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 62
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • Yamano, K., and R.J. Youle. 2013. PINK1 is degraded through the N-end rule pathway. Autophagy. 9:1758-1769. http://dx.doi.org/10.4161/auto.24633
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 63
    • 80053430054 scopus 로고    scopus 로고
    • Spatiotemporally controlled initiation of Parkin-mediated mitophagy within single cells
    • Yang, J.Y., and W.Y. Yang. 2011. Spatiotemporally controlled initiation of Parkin-mediated mitophagy within single cells. Autophagy. 7:1230-1238. http://dx.doi.org/10.4161/auto.7.10.16626
    • (2011) Autophagy , vol.7 , pp. 1230-1238
    • Yang, J.Y.1    Yang, W.Y.2
  • 64
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin
    • Yang, Y., S. Gehrke, Y. Imai, Z. Huang, Y. Ouyang, J.W. Wang, L. Yang, M.F. Beal, H. Vogel, and B. Lu. 2006. Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl. Acad. Sci. USA. 103:10793-10798. http://dx.doi.org/10.1073/pnas.0602493103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3    Huang, Z.4    Ouyang, Y.5    Wang, J.W.6    Yang, L.7    Beal, M.F.8    Vogel, H.9    Lu, B.10
  • 65
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii, S.R., C. Kishi, N. Ishihara, and N. Mizushima. 2011. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J. Biol. Chem. 286:19630-19640. http://dx.doi.org/10.1074/jbc. M110.209338
    • (2011) J. Biol. Chem. , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 66
    • 84906315018 scopus 로고    scopus 로고
    • PINK1 triggers autocatalytic activation of Parkin to specify cell fate decisions
    • Zhang, C., S. Lee, Y. Peng, E. Bunker, E. Giaime, J. Shen, Z. Zhou, and X. Liu. 2014. PINK1 triggers autocatalytic activation of Parkin to specify cell fate decisions. Curr. Biol. 24:1854-1865. http://dx.doi.org/10.1016/j.cub.2014.07.014
    • (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
  • 67
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
    • Zheng, X., and T. Hunter. 2013. Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res. 23:886-897. http://dx.doi.org/10.1038/cr.2013.66
    • (2013) Cell Res. , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2
  • 68
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani, E., R.N. Tao, and A.J. Whitworth. 2010. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. USA. 107:5018-5023. http://dx.doi.org/10.1073/pnas.0913485107
    • (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.