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Volumn 524, Issue 7565, 2015, Pages 309-314

The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy

Author keywords

[No Author keywords available]

Indexed keywords

OPTINEURIN; OUTER MEMBRANE PROTEIN; PARKIN; PHOSPHOTRANSFERASE; PINK1 PROTEIN; PROTEIN P62; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; CARRIER PROTEIN; MAP1LC3B PROTEIN, HUMAN; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; MITOCHONDRIAL PROTEIN; NUCLEAR DOT PROTEIN 52, HUMAN; NUCLEAR PROTEIN; OPTN PROTEIN, HUMAN; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; PTEN-INDUCED PUTATIVE KINASE; SIGNAL PEPTIDE; TBK1 PROTEIN, HUMAN; TRANSCRIPTION FACTOR IIIA; UBIQUITIN; ULK1 PROTEIN, HUMAN; WIPI-1 PROTEIN, HUMAN; ZFYVE1 PROTEIN, HUMAN;

EID: 84939804206     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14893     Document Type: Article
Times cited : (2030)

References (42)
  • 2
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz, A., Ernst, A. & Dikic, I. Cargo recognition and trafficking in selective autophagy. Nature Cell Biol. 16, 495-501 (2014).
    • (2014) Nature Cell Biol. , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 3
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate parkin
    • Narendra, D. P. et al. PINK1 is selectively stabilized on impaired mitochondria to activate parkin. PLoS Biol. 8, e1000298 (2010).
    • (2010) PLoS Biol. , vol.8
    • Narendra, D.P.1
  • 4
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D. F. & Youle, R. J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183, 795-803 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 5
    • 84899539731 scopus 로고    scopus 로고
    • PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
    • Kane, L. A. et al. PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J. Cell Biol. 205, 143-153 (2014).
    • (2014) J. Cell Biol. , vol.205 , pp. 143-153
    • Kane, L.A.1
  • 6
    • 84899421556 scopus 로고    scopus 로고
    • Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
    • Kazlauskaite, A. et al. Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem. J. 460, 127-139 (2014).
    • (2014) Biochem. J. , vol.460 , pp. 127-139
    • Kazlauskaite, A.1
  • 7
    • 84901751574 scopus 로고    scopus 로고
    • Ubiquitin is phosphorylated by PINK1 to activate parkin
    • Koyano, F. et al. Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510, 162-166 (2014).
    • (2014) Nature , vol.510 , pp. 162-166
    • Koyano, F.1
  • 8
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • Geisler, S. et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nature Cell Biol. 12, 119-131 (2010).
    • (2010) Nature Cell Biol. , vol.12 , pp. 119-131
    • Geisler, S.1
  • 9
    • 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, Y. C. & Holzbaur, E. L. F. Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc. Natl Acad. Sci. USA 111, E4439-E4448 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111
    • Wong, Y.C.1    Holzbaur, E.L.F.2
  • 10
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra, D., Kane, L. A., Hauser, D. N., Fearnley, I. M.& Youle, R. J. p62/SQSTM1is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6, 1090-1106 (2010).
    • (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
  • 11
    • 77954695260 scopus 로고    scopus 로고
    • P62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
    • Okatsu, K. et al. p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria. Genes Cells 15, 887-900 (2010).
    • (2010) Genes Cells , vol.15 , pp. 887-900
    • Okatsu, K.1
  • 12
    • 84905491871 scopus 로고    scopus 로고
    • Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family
    • Lu, K., Psakhye, I. & Jentsch, S. Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family. Cell 158, 549-563 (2014).
    • (2014) Cell , vol.158 , pp. 549-563
    • Lu, K.1    Psakhye, I.2    Jentsch, S.3
  • 13
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild, P. et al. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333, 228-233 (2011).
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1
  • 14
    • 18244385269 scopus 로고    scopus 로고
    • Adult-onset primary open-angle glaucoma caused by mutations in optineurin
    • Rezaie, T. et al. Adult-onset primary open-angle glaucoma caused by mutations in optineurin. Science 295, 1077-1079 (2002).
    • (2002) Science , vol.295 , pp. 1077-1079
    • Rezaie, T.1
  • 15
    • 77952419246 scopus 로고    scopus 로고
    • Mutations ofoptineurin inamyotrophic lateral sclerosis
    • Maruyama, H. et al.Mutations ofoptineurin inamyotrophic lateral sclerosis. Nature 465, 223-226 (2010).
    • (2010) Nature , vol.465 , pp. 223-226
    • Maruyama, H.1
  • 16
    • 84880617946 scopus 로고    scopus 로고
    • Association between variants of PRDM1 and NDP52 and Crohn's disease, based on exome sequencing and functional studies
    • Ellinghaus, D. et al. Association between variants of PRDM1 and NDP52 and Crohn's disease, based on exome sequencing and functional studies. Gastroenterology 145, 339-347 (2013).
    • (2013) Gastroenterology , vol.145 , pp. 339-347
    • Ellinghaus, D.1
  • 17
    • 77649269693 scopus 로고    scopus 로고
    • Optineurin negatively regulates the induction of IFNb in response to RNA virus infection
    • Mankouri, J. et al. Optineurin negatively regulates the induction of IFNb in response to RNA virus infection. PLoS Pathog. 6, e1000778 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Mankouri, J.1
  • 18
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitincoated bacteria
    • Thurston, T. L., Ryzhakov, G., Bloor, S., von Muhlinen, N. & Randow, F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitincoated bacteria. Nature Immunol. 10, 1215-1221 (2009).
    • (2009) Nature Immunol. , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 19
    • 40149097099 scopus 로고    scopus 로고
    • Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma
    • Morton, S., Hesson, L., Peggie, M. & Cohen, P. Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma. FEBS Lett. 582, 997-1002 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 997-1002
    • Morton, S.1    Hesson, L.2    Peggie, M.3    Cohen, P.4
  • 20
    • 84875814149 scopus 로고    scopus 로고
    • Crystal structure and mechanism of activation of TANK-binding kinase 1
    • Larabi, A. et al. Crystal structure and mechanism of activation of TANK-binding kinase 1. Cell Rep. 3, 734-746 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 734-746
    • Larabi, A.1
  • 21
    • 84922434418 scopus 로고    scopus 로고
    • Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis
    • Ordureau, A. et al. Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis. Mol. Cell 56, 360-375 (2014).
    • (2014) Mol. Cell , vol.56 , pp. 360-375
    • Ordureau, A.1
  • 22
    • 84922235969 scopus 로고    scopus 로고
    • Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis
    • Wauer, T. et al. Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis. EMBO J. 34, 307-325 (2015).
    • (2015) EMBO J. , vol.34 , pp. 307-325
    • Wauer, T.1
  • 23
    • 84864267876 scopus 로고    scopus 로고
    • PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
    • Kondapalli, C. et al. PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol. 2, 120080 (2012).
    • (2012) Open Biol. , vol.2 , pp. 120080
    • Kondapalli, C.1
  • 24
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • Sarraf, S. A. et al. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 496, 372-376 (2013).
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1
  • 25
    • 84919629959 scopus 로고    scopus 로고
    • Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering
    • Shiba-Fukushima, K. et al. Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering. PLoS Genet. 10, e1004861 (2014).
    • (2014) PLoS Genet. , vol.10
    • Shiba-Fukushima, K.1
  • 26
    • 84922794336 scopus 로고    scopus 로고
    • Phosphorylated ubiquitin chain is the genuine Parkin receptor
    • Okatsu, K. et al. Phosphorylated ubiquitin chain is the genuine Parkin receptor. J. Cell Biol. 209, 111-128 (2015).
    • (2015) J. Cell Biol. , vol.209 , pp. 111-128
    • Okatsu, K.1
  • 27
    • 84929691103 scopus 로고    scopus 로고
    • Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy
    • Ordureau, A. et al. Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy. Proc. Natl Acad. Sci. USA 112, 6637-6642 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 6637-6642
    • Ordureau, A.1
  • 28
    • 84869080400 scopus 로고    scopus 로고
    • LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy
    • von Muhlinen, N. et al. LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. Mol. Cell 48, 329-342 (2012).
    • (2012) Mol. Cell , vol.48 , pp. 329-342
    • Von Muhlinen, N.1
  • 29
    • 84891461247 scopus 로고    scopus 로고
    • The LC3 interactome at a glance
    • Wild, P., McEwan, D. G. & Dikic, I. The LC3 interactome at a glance. J. Cell Sci. 127, 3-9 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 3-9
    • Wild, P.1    McEwan, D.G.2    Dikic, I.3
  • 30
  • 31
    • 84883499836 scopus 로고    scopus 로고
    • Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy
    • Fogel, A. I. et al. Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy. Mol. Cell. Biol. 33, 3675-3688 (2013).
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 3675-3688
    • Fogel, A.I.1
  • 32
    • 84885662059 scopus 로고    scopus 로고
    • Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site
    • Koyama-Honda, I., Itakura, E., Fujiwara, T. K. & Mizushima, N. Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site. Autophagy 9, 1491-1499 (2013).
    • (2013) Autophagy , vol.9 , pp. 1491-1499
    • Koyama-Honda, I.1    Itakura, E.2    Fujiwara, T.K.3    Mizushima, N.4
  • 33
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J., Kundu, M., Viollet, B. & Guan, K. L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nature Cell Biol. 13, 132-141 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 34
    • 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., Kishi-Itakura, C., Koyama-Honda, I. & Mizushima, N. Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J. Cell Sci. 125, 1488-1499 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3    Mizushima, N.4
  • 35
    • 84939820927 scopus 로고    scopus 로고
    • MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5
    • Nezich, C. L., Wang, C., Fogel, A. I. & Youle, R. J. MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5. J. Cell Biol. 210, 435-450 (2015).
    • (2015) J. Cell Biol. , vol.210 , pp. 435-450
    • Nezich, C.L.1    Wang, C.2    Fogel, A.I.3    Youle, R.J.4
  • 36
    • 0038783254 scopus 로고    scopus 로고
    • Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
    • Santel, A. et al. Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells. J. Cell Sci. 116, 2763-2774 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 2763-2774
    • Santel, A.1
  • 37
    • 79961185942 scopus 로고    scopus 로고
    • Heritable gene targeting in zebrafish using customized TALENs
    • Huang, P. et al. Heritable gene targeting in zebrafish using customized TALENs. Nature Biotechnol. 29, 699-700 (2011).
    • (2011) Nature Biotechnol. , vol.29 , pp. 699-700
    • Huang, P.1
  • 38
    • 84890429468 scopus 로고    scopus 로고
    • High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy
    • Hasson, S. A. et al. High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy. Nature 504, 291-295 (2013).
    • (2013) Nature , vol.504 , pp. 291-295
    • Hasson, S.A.1
  • 39
    • 79551685675 scopus 로고    scopus 로고
    • A TALE nuclease architecture for efficient genome editing
    • Miller, J. C. et al. A TALE nuclease architecture for efficient genome editing. Nature Biotechnol. 29, 143-148 (2011).
    • (2011) Nature Biotechnol. , vol.29 , pp. 143-148
    • Miller, J.C.1
  • 40
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • Mali, P. et al. RNA-guided human genome engineering via Cas9. Science 339, 823-826 (2013).
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1
  • 41
    • 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, S. M., Kane, L. A. & Youle, R. J. 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
  • 42
    • 80052145606 scopus 로고    scopus 로고
    • A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery
    • Katayama, H., Kogure, T., Mizushima, N., Yoshimori, T. & Miyawaki, A. A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery. Chem. Biol. 18, 1042-1052 (2011).
    • (2011) Chem. Biol. , vol.18 , pp. 1042-1052
    • Katayama, H.1    Kogure, T.2    Mizushima, N.3    Yoshimori, T.4    Miyawaki, A.5


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