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Volumn 59, Issue 4, 2015, Pages 522-539

Organelle-Specific Initiation of Autophagy

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHAGY; CELL COMPARTMENTALIZATION; CELL MEMBRANE; CELL ORGANELLE; CYTOSOL; HOMEOSTASIS; HUMAN; LYSOSOME; MITOCHONDRION; NONHUMAN; PEROXISOME; REGULATORY MECHANISM; RETICULAR FORMATION; RETICULOENDOTHELIAL SYSTEM; REVIEW; ANIMAL; CELL NUCLEUS; ENDOPLASMIC RETICULUM; MITOCHONDRIAL MEMBRANE POTENTIAL; PHAGOSOME; PHYSIOLOGY;

EID: 84939482242     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2015.07.021     Document Type: Review
Times cited : (170)

References (144)
  • 4
    • 84866431363 scopus 로고    scopus 로고
    • Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1
    • Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 2012, 150:1196-1208.
    • (2012) Cell , vol.150 , pp. 1196-1208
    • Bar-Peled, L.1    Schweitzer, L.D.2    Zoncu, R.3    Sabatini, D.M.4
  • 5
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • Bellot G., Garcia-Medina R., Gounon P., Chiche J., Roux D., Pouysségur J., Mazure N.M. Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol. Cell. Biol. 2009, 29:2570-2581.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3    Chiche, J.4    Roux, D.5    Pouysségur, J.6    Mazure, N.M.7
  • 6
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales S., McDonald K.L., Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 2006, 4:e423.
    • (2006) PLoS Biol. , vol.4
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 7
    • 84899622427 scopus 로고    scopus 로고
    • Unravelling mechanisms of p53-mediated tumour suppression
    • Bieging K.T., Mello S.S., Attardi L.D. Unravelling mechanisms of p53-mediated tumour suppression. Nat. Rev. Cancer 2014, 14:359-370.
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 359-370
    • Bieging, K.T.1    Mello, S.S.2    Attardi, L.D.3
  • 8
    • 0015592534 scopus 로고
    • A morphometric study of the removal of phenobarbital-induced membranes from hepatocytes after cessation of threatment
    • Bolender R.P., Weibel E.R. A morphometric study of the removal of phenobarbital-induced membranes from hepatocytes after cessation of threatment. J. Cell Biol. 1973, 56:746-761.
    • (1973) J. Cell Biol. , vol.56 , pp. 746-761
    • Bolender, R.P.1    Weibel, E.R.2
  • 9
    • 84919829116 scopus 로고    scopus 로고
    • Netrin-1 improves post-injury cardiac function in vivo via DCC/NO-dependent preservation of mitochondrial integrity, while attenuating autophagy
    • Bouhidel J.O., Wang P., Siu K.L., Li H., Youn J.Y., Cai H. Netrin-1 improves post-injury cardiac function in vivo via DCC/NO-dependent preservation of mitochondrial integrity, while attenuating autophagy. Biochim. Biophys. Acta 2015, 1852:277-289.
    • (2015) Biochim. Biophys. Acta , vol.1852 , pp. 277-289
    • Bouhidel, J.O.1    Wang, P.2    Siu, K.L.3    Li, H.4    Youn, J.Y.5    Cai, H.6
  • 10
    • 84866358168 scopus 로고    scopus 로고
    • The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance
    • Bouwman P., Jonkers J. The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance. Nat. Rev. Cancer 2012, 12:587-598.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 587-598
    • Bouwman, P.1    Jonkers, J.2
  • 11
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • Brandizzi F., Barlowe C. Organization of the ER-Golgi interface for membrane traffic control. Nat. Rev. Mol. Cell Biol. 2013, 14:382-392.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 12
    • 84925776380 scopus 로고    scopus 로고
    • Peroxisomal Pex3 activates selective autophagy of peroxisomes via interaction with the pexophagy receptor Atg30
    • Burnett S.F., Farré J.C., Nazarko T.Y., Subramani S. Peroxisomal Pex3 activates selective autophagy of peroxisomes via interaction with the pexophagy receptor Atg30. J. Biol. Chem. 2015, 290:8623-8631.
    • (2015) J. Biol. Chem. , vol.290 , pp. 8623-8631
    • Burnett, S.F.1    Farré, J.C.2    Nazarko, T.Y.3    Subramani, S.4
  • 13
    • 84928926952 scopus 로고    scopus 로고
    • IRGM governs the core autophagy machinery to conduct antimicrobial defense
    • Chauhan S., Mandell M.A., Deretic V. IRGM governs the core autophagy machinery to conduct antimicrobial defense. Mol. Cell 2015, 58:507-521.
    • (2015) Mol. Cell , vol.58 , pp. 507-521
    • Chauhan, S.1    Mandell, M.A.2    Deretic, V.3
  • 14
    • 84899912073 scopus 로고    scopus 로고
    • A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy
    • Chen G., Han Z., Feng D., Chen Y., Chen L., Wu H., Huang L., Zhou C., Cai X., Fu C., et al. A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy. Mol. Cell 2014, 54:362-377.
    • (2014) Mol. Cell , vol.54 , pp. 362-377
    • Chen, G.1    Han, Z.2    Feng, D.3    Chen, Y.4    Chen, L.5    Wu, H.6    Huang, L.7    Zhou, C.8    Cai, X.9    Fu, C.10
  • 15
    • 84930516235 scopus 로고    scopus 로고
    • ATM-mediated PTEN phosphorylation promotes PTEN nuclear translocation and autophagy in response to DNA-damaging agents in cancer cells
    • Chen J.H., Zhang P., Chen W.D., Li D.D., Wu X.Q., Deng R., Jiao L., Li X., Ji J., Feng G.K., et al. ATM-mediated PTEN phosphorylation promotes PTEN nuclear translocation and autophagy in response to DNA-damaging agents in cancer cells. Autophagy 2015, 11:239-252.
    • (2015) Autophagy , vol.11 , pp. 239-252
    • Chen, J.H.1    Zhang, P.2    Chen, W.D.3    Li, D.D.4    Wu, X.Q.5    Deng, R.6    Jiao, L.7    Li, X.8    Ji, J.9    Feng, G.K.10
  • 16
    • 84355162283 scopus 로고    scopus 로고
    • Canonical and non-canonical autophagy: variations on a common theme of self-eating?
    • Codogno P., Mehrpour M., Proikas-Cezanne T. Canonical and non-canonical autophagy: variations on a common theme of self-eating?. Nat. Rev. Mol. Cell Biol. 2012, 13:7-12.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 7-12
    • Codogno, P.1    Mehrpour, M.2    Proikas-Cezanne, T.3
  • 17
    • 0031056002 scopus 로고    scopus 로고
    • DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • Cohen O., Feinstein E., Kimchi A. DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. EMBO J. 1997, 16:998-1008.
    • (1997) EMBO J. , vol.16 , pp. 998-1008
    • Cohen, O.1    Feinstein, E.2    Kimchi, A.3
  • 28
    • 84877788725 scopus 로고    scopus 로고
    • Elevated autophagic sequestration of mitochondria and lipid droplets in steatotic hepatocytes of chronic ethanol-treated rats: an immunohistochemical and electron microscopic study
    • Eid N., Ito Y., Maemura K., Otsuki Y. Elevated autophagic sequestration of mitochondria and lipid droplets in steatotic hepatocytes of chronic ethanol-treated rats: an immunohistochemical and electron microscopic study. J. Mol. Histol. 2013, 44:311-326.
    • (2013) J. Mol. Histol. , vol.44 , pp. 311-326
    • Eid, N.1    Ito, Y.2    Maemura, K.3    Otsuki, Y.4
  • 30
    • 84868118383 scopus 로고    scopus 로고
    • PARP-1 modulation of mTOR signaling in response to a DNA alkylating agent
    • Ethier C., Tardif M., Arul L., Poirier G.G. PARP-1 modulation of mTOR signaling in response to a DNA alkylating agent. PLoS ONE 2012, 7:e47978.
    • (2012) PLoS ONE , vol.7 , pp. e47978
    • Ethier, C.1    Tardif, M.2    Arul, L.3    Poirier, G.G.4
  • 31
  • 35
    • 84870206960 scopus 로고    scopus 로고
    • Mitochondria: master regulators of danger signalling
    • Galluzzi L., Kepp O., Kroemer G. Mitochondria: master regulators of danger signalling. Nat. Rev. Mol. Cell Biol. 2012, 13:780-788.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 780-788
    • Galluzzi, L.1    Kepp, O.2    Kroemer, G.3
  • 36
    • 84867691699 scopus 로고    scopus 로고
    • Mitochondrial control of cellular life, stress, and death
    • Galluzzi L., Kepp O., Trojel-Hansen C., Kroemer G. Mitochondrial control of cellular life, stress, and death. Circ. Res. 2012, 111:1198-1207.
    • (2012) Circ. Res. , vol.111 , pp. 1198-1207
    • Galluzzi, L.1    Kepp, O.2    Trojel-Hansen, C.3    Kroemer, G.4
  • 42
    • 84905050462 scopus 로고    scopus 로고
    • Assembly and localization of Toll-like receptor signalling complexes
    • Gay N.J., Symmons M.F., Gangloff M., Bryant C.E. Assembly and localization of Toll-like receptor signalling complexes. Nat. Rev. Immunol. 2014, 14:546-558.
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 546-558
    • Gay, N.J.1    Symmons, M.F.2    Gangloff, M.3    Bryant, C.E.4
  • 44
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson B.A., Kraus W.L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell Biol. 2012, 13:411-424.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 45
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes L.C., Di Benedetto G., Scorrano L. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 2011, 13:589-598.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 46
    • 55149097659 scopus 로고    scopus 로고
    • The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes
    • Hara-Kuge S., Fujiki Y. The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes. Exp. Cell Res. 2008, 314:3531-3541.
    • (2008) Exp. Cell Res. , vol.314 , pp. 3531-3541
    • Hara-Kuge, S.1    Fujiki, Y.2
  • 47
    • 84857058225 scopus 로고    scopus 로고
    • Control of autophagy as a therapy for neurodegenerative disease
    • Harris H., Rubinsztein D.C. Control of autophagy as a therapy for neurodegenerative disease. Nat. Rev. Neurol. 2012, 8:108-117.
    • (2012) Nat. Rev. Neurol. , vol.8 , pp. 108-117
    • Harris, H.1    Rubinsztein, D.C.2
  • 50
    • 84870909002 scopus 로고    scopus 로고
    • Attenuation of TNFSF10/TRAIL-induced apoptosis by an autophagic survival pathway involving TRAF2- and RIPK1/RIP1-mediated MAPK8/JNK activation
    • He W., Wang Q., Xu J., Xu X., Padilla M.T., Ren G., Gou X., Lin Y. Attenuation of TNFSF10/TRAIL-induced apoptosis by an autophagic survival pathway involving TRAF2- and RIPK1/RIP1-mediated MAPK8/JNK activation. Autophagy 2012, 8:1811-1821.
    • (2012) Autophagy , vol.8 , pp. 1811-1821
    • He, W.1    Wang, Q.2    Xu, J.3    Xu, X.4    Padilla, M.T.5    Ren, G.6    Gou, X.7    Lin, Y.8
  • 51
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 2012, 13:89-102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 55
    • 84880108306 scopus 로고    scopus 로고
    • Spatiotemporally controlled induction of autophagy-mediated lysosome turnover
    • Hung Y.H., Chen L.M., Yang J.Y., Yang W.Y. Spatiotemporally controlled induction of autophagy-mediated lysosome turnover. Nat. Commun. 2013, 4:2111.
    • (2013) Nat. Commun. , vol.4 , pp. 2111
    • Hung, Y.H.1    Chen, L.M.2    Yang, J.Y.3    Yang, W.Y.4
  • 56
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki K., Li Y., Zhu T., Wu J., Guan K.L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 2002, 4:648-657.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 57
    • 84862908818 scopus 로고    scopus 로고
    • AMPK and mTOR in cellular energy homeostasis and drug targets
    • Inoki K., Kim J., Guan K.L. AMPK and mTOR in cellular energy homeostasis and drug targets. Annu. Rev. Pharmacol. Toxicol. 2012, 52:381-400.
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 381-400
    • Inoki, K.1    Kim, J.2    Guan, K.L.3
  • 61
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin S.M., Lazarou M., Wang C., Kane L.A., Narendra D.P., Youle R.J. 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
  • 65
    • 79251574964 scopus 로고    scopus 로고
    • Mitochondrial degradation by autophagy (mitophagy) in GFP-LC3 transgenic hepatocytes during nutrient deprivation
    • Kim I., Lemasters J.J. Mitochondrial degradation by autophagy (mitophagy) in GFP-LC3 transgenic hepatocytes during nutrient deprivation. Am. J. Physiol. Cell Physiol. 2011, 300:C308-C317.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300 , pp. C308-C317
    • Kim, I.1    Lemasters, J.J.2
  • 66
    • 84872586081 scopus 로고    scopus 로고
    • Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy
    • Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R., Zhong Q., Guan K.L. Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy. Cell 2013, 152:290-303.
    • (2013) Cell , vol.152 , pp. 290-303
    • Kim, J.1    Kim, Y.C.2    Fang, C.3    Russell, R.C.4    Kim, J.H.5    Fan, W.6    Liu, R.7    Zhong, Q.8    Guan, K.L.9
  • 67
    • 80051813164 scopus 로고    scopus 로고
    • Eating the strangers within: host control of intracellular bacteria via xenophagy
    • Knodler L.A., Celli J. Eating the strangers within: host control of intracellular bacteria via xenophagy. Cell. Microbiol. 2011, 13:1319-1327.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1319-1327
    • Knodler, L.A.1    Celli, J.2
  • 69
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft C., Deplazes A., Sohrmann M., Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 2008, 10:602-610.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 70
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G., Jäättelä M. Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 2005, 5:886-897.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jäättelä, M.2
  • 71
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer G., Mariño G., Levine B. Autophagy and the integrated stress response. Mol. Cell 2010, 40:280-293.
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 72
    • 84859736977 scopus 로고    scopus 로고
    • Aggrephagy: selective disposal of protein aggregates by macroautophagy
    • Lamark T., Johansen T. Aggrephagy: selective disposal of protein aggregates by macroautophagy. Int. J. Cell Biol. 2012, 2012:736905.
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 736905
    • Lamark, T.1    Johansen, T.2
  • 74
    • 84907996785 scopus 로고    scopus 로고
    • Dnase2a deficiency uncovers lysosomal clearance of damaged nuclear DNA via autophagy
    • Lan Y.Y., Londoño D., Bouley R., Rooney M.S., Hacohen N. Dnase2a deficiency uncovers lysosomal clearance of damaged nuclear DNA via autophagy. Cell Rep. 2014, 9:180-192.
    • (2014) Cell Rep. , vol.9 , pp. 180-192
    • Lan, Y.Y.1    Londoño, D.2    Bouley, R.3    Rooney, M.S.4    Hacohen, N.5
  • 75
    • 0030038488 scopus 로고    scopus 로고
    • Fas ligation induces apoptosis and Jun kinase activation independently of CD45 and Lck in human T cells
    • Latinis K.M., Koretzky G.A. Fas ligation induces apoptosis and Jun kinase activation independently of CD45 and Lck in human T cells. Blood 1996, 87:871-875.
    • (1996) Blood , vol.87 , pp. 871-875
    • Latinis, K.M.1    Koretzky, G.A.2
  • 78
    • 84861444859 scopus 로고    scopus 로고
    • Regulation of glucose transport by insulin: traffic control of GLUT4
    • Leto D., Saltiel A.R. Regulation of glucose transport by insulin: traffic control of GLUT4. Nat. Rev. Mol. Cell Biol. 2012, 13:383-396.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 383-396
    • Leto, D.1    Saltiel, A.R.2
  • 79
    • 84898619521 scopus 로고    scopus 로고
    • MicroRNA-137 is a novel hypoxia-responsive microRNA that inhibits mitophagy via regulation of two mitophagy receptors FUNDC1 and NIX
    • Li W., Zhang X., Zhuang H., Chen H.G., Chen Y., Tian W., Wu W., Li Y., Wang S., Zhang L., et al. MicroRNA-137 is a novel hypoxia-responsive microRNA that inhibits mitophagy via regulation of two mitophagy receptors FUNDC1 and NIX. J. Biol. Chem. 2014, 289:10691-10701.
    • (2014) J. Biol. Chem. , vol.289 , pp. 10691-10701
    • Li, W.1    Zhang, X.2    Zhuang, H.3    Chen, H.G.4    Chen, Y.5    Tian, W.6    Wu, W.7    Li, Y.8    Wang, S.9    Zhang, L.10
  • 81
    • 84903817207 scopus 로고    scopus 로고
    • Receptor-mediated mitophagy in yeast and mammalian systems
    • Liu L., Sakakibara K., Chen Q., Okamoto K. Receptor-mediated mitophagy in yeast and mammalian systems. Cell Res. 2014, 24:787-795.
    • (2014) Cell Res. , vol.24 , pp. 787-795
    • Liu, L.1    Sakakibara, K.2    Chen, Q.3    Okamoto, K.4
  • 82
    • 84883028352 scopus 로고    scopus 로고
    • β-adrenergic receptor-stimulated lipolysis requires the RAB7-mediated autolysosomal lipid degradation
    • Lizaso A., Tan K.T., Lee Y.H. β-adrenergic receptor-stimulated lipolysis requires the RAB7-mediated autolysosomal lipid degradation. Autophagy 2013, 9:1228-1243.
    • (2013) Autophagy , vol.9 , pp. 1228-1243
    • Lizaso, A.1    Tan, K.T.2    Lee, Y.H.3
  • 83
  • 87
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning B.D., Cantley L.C. AKT/PKB signaling: navigating downstream. Cell 2007, 129:1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 90
    • 69449107689 scopus 로고    scopus 로고
    • Atypical BH3-domains of BNIP3 and BNIP3L lead to autophagy in hypoxia
    • Mazure N.M., Pouysségur J. Atypical BH3-domains of BNIP3 and BNIP3L lead to autophagy in hypoxia. Autophagy 2009, 5:868-869.
    • (2009) Autophagy , vol.5 , pp. 868-869
    • Mazure, N.M.1    Pouysségur, J.2
  • 91
    • 79251468749 scopus 로고    scopus 로고
    • Dependence receptors: from basic research to drug development
    • Mehlen P., Bredesen D.E. Dependence receptors: from basic research to drug development. Sci. Signal. 2011, 4:mr2.
    • (2011) Sci. Signal. , vol.4 , pp. mr2
    • Mehlen, P.1    Bredesen, D.E.2
  • 92
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova M.M., Shaw R.J. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat. Cell Biol. 2011, 13:1016-1023.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 93
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., Levine B., Cuervo A.M., Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 95
    • 84934449988 scopus 로고    scopus 로고
    • Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
    • Mochida K., Oikawa Y., Kimura Y., Kirisako H., Hirano H., Ohsumi Y., Nakatogawa H. Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus. Nature 2015, 522:359-362.
    • (2015) Nature , vol.522 , pp. 359-362
    • Mochida, K.1    Oikawa, Y.2    Kimura, Y.3    Kirisako, H.4    Hirano, H.5    Ohsumi, Y.6    Nakatogawa, H.7
  • 96
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1 is 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/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 2010, 6:1090-1106.
    • (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
  • 98
    • 84901801108 scopus 로고    scopus 로고
    • Organellophagy: eliminating cellular building blocks via selective autophagy
    • Okamoto K. Organellophagy: eliminating cellular building blocks via selective autophagy. J. Cell Biol. 2014, 205:435-445.
    • (2014) J. Cell Biol. , vol.205 , pp. 435-445
    • Okamoto, K.1
  • 99
    • 84866072587 scopus 로고    scopus 로고
    • PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
    • Okatsu K., Oka T., Iguchi M., Imamura K., Kosako H., Tani N., Kimura M., Go E., Koyano F., Funayama M., et al. PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nat. Commun. 2012, 3:1016.
    • (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
  • 103
    • 0029898073 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) receptor activates NF-kappaB independently of its cytotoxic function
    • Ponton A., Clément M.V., Stamenkovic I. The CD95 (APO-1/Fas) receptor activates NF-kappaB independently of its cytotoxic function. J. Biol. Chem. 1996, 271:8991-8995.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8991-8995
    • Ponton, A.1    Clément, M.V.2    Stamenkovic, I.3
  • 104
    • 84925324049 scopus 로고    scopus 로고
    • Fatty acid trafficking in starved cells: regulation by lipid droplet lipolysis, autophagy, and mitochondrial fusion dynamics
    • Rambold A.S., Cohen S., Lippincott-Schwartz J. Fatty acid trafficking in starved cells: regulation by lipid droplet lipolysis, autophagy, and mitochondrial fusion dynamics. Dev. Cell 2015, 32:678-692.
    • (2015) Dev. Cell , vol.32 , pp. 678-692
    • Rambold, A.S.1    Cohen, S.2    Lippincott-Schwartz, J.3
  • 110
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mitochondria contacts: function of the junction
    • Rowland A.A., Voeltz G.K. Endoplasmic reticulum-mitochondria contacts: function of the junction. Nat. Rev. Mol. Cell Biol. 2012, 13:607-625.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 111
    • 47249157360 scopus 로고    scopus 로고
    • Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum
    • Sakaki K., Wu J., Kaufman R.J. Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum. J. Biol. Chem. 2008, 283:15370-15380.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15370-15380
    • Sakaki, K.1    Wu, J.2    Kaufman, R.J.3
  • 112
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 2010, 141:290-303.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 114
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R., Shvets E., Fass E., Shorer H., Gil L., Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 2007, 26:1749-1760.
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 115
    • 84907042769 scopus 로고    scopus 로고
    • ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery
    • Schuck S., Gallagher C.M., Walter P. ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery. J. Cell Sci. 2014, 127:4078-4088.
    • (2014) J. Cell Sci. , vol.127 , pp. 4078-4088
    • Schuck, S.1    Gallagher, C.M.2    Walter, P.3
  • 118
    • 57749100267 scopus 로고    scopus 로고
    • MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages
    • Shi C.S., Kehrl J.H. MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages. J. Biol. Chem. 2008, 283:33175-33182.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33175-33182
    • Shi, C.S.1    Kehrl, J.H.2
  • 119
    • 84894523716 scopus 로고    scopus 로고
    • Making new contacts: the mTOR network in metabolism and signalling crosstalk
    • Shimobayashi M., Hall M.N. Making new contacts: the mTOR network in metabolism and signalling crosstalk. Nat. Rev. Mol. Cell Biol. 2014, 15:155-162.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 155-162
    • Shimobayashi, M.1    Hall, M.N.2
  • 132
    • 77953482819 scopus 로고    scopus 로고
    • The p53 response element and transcriptional repression
    • Wang B., Xiao Z., Ko H.L., Ren E.C. The p53 response element and transcriptional repression. Cell Cycle 2010, 9:870-879.
    • (2010) Cell Cycle , vol.9 , pp. 870-879
    • Wang, B.1    Xiao, Z.2    Ko, H.L.3    Ren, E.C.4
  • 133
    • 84869147050 scopus 로고    scopus 로고
    • Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation
    • Wang R.C., Wei Y., An Z., Zou Z., Xiao G., Bhagat G., White M., Reichelt J., Levine B. Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation. Science 2012, 338:956-959.
    • (2012) Science , vol.338 , pp. 956-959
    • Wang, R.C.1    Wei, Y.2    An, Z.3    Zou, Z.4    Xiao, G.5    Bhagat, G.6    White, M.7    Reichelt, J.8    Levine, B.9
  • 138
    • 84905582805 scopus 로고    scopus 로고
    • RNF2 is recruited by WASH to ubiquitinate AMBRA1 leading to downregulation of autophagy
    • Xia P., Wang S., Huang G., Du Y., Zhu P., Li M., Fan Z. RNF2 is recruited by WASH to ubiquitinate AMBRA1 leading to downregulation of autophagy. Cell Res. 2014, 24:943-958.
    • (2014) Cell Res. , vol.24 , pp. 943-958
    • Xia, P.1    Wang, S.2    Huang, G.3    Du, Y.4    Zhu, P.5    Li, M.6    Fan, Z.7
  • 140
    • 84925775785 scopus 로고    scopus 로고
    • The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy
    • Yamashita S., Abe K., Tatemichi Y., Fujiki Y. The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy. Autophagy 2014, 10:1549-1564.
    • (2014) Autophagy , vol.10 , pp. 1549-1564
    • Yamashita, S.1    Abe, K.2    Tatemichi, Y.3    Fujiki, Y.4
  • 143
    • 84907519033 scopus 로고    scopus 로고
    • The lysosomal v-ATPase-Ragulator complex is a common activator for AMPK and mTORC1, acting as a switch between catabolism and anabolism
    • Zhang C.S., Jiang B., Li M., Zhu M., Peng Y., Zhang Y.L., Wu Y.Q., Li T.Y., Liang Y., Lu Z., et al. The lysosomal v-ATPase-Ragulator complex is a common activator for AMPK and mTORC1, acting as a switch between catabolism and anabolism. Cell Metab. 2014, 20:526-540.
    • (2014) Cell Metab. , vol.20 , pp. 526-540
    • Zhang, C.S.1    Jiang, B.2    Li, M.3    Zhu, M.4    Peng, Y.5    Zhang, Y.L.6    Wu, Y.Q.7    Li, T.Y.8    Liang, Y.9    Lu, Z.10
  • 144
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • Zoncu R., Bar-Peled L., Efeyan A., Wang S., Sancak Y., Sabatini D.M. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 2011, 334:678-683.
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.