메뉴 건너뛰기




Volumn 15, Issue 10, 2013, Pages 1186-1196

A tuberous sclerosis complex signalling node at the peroxisome regulates mTORC1 and autophagy in response to ROS

Author keywords

[No Author keywords available]

Indexed keywords

HAMARTIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PEROXIN; PEROXIN 19; PEROXIN 5; REACTIVE OXYGEN METABOLITE; RHEB PROTEIN; TUBERIN; UNCLASSIFIED DRUG;

EID: 84885105969     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2822     Document Type: Article
Times cited : (222)

References (56)
  • 3
    • 3142546236 scopus 로고    scopus 로고
    • The Rheb family of GTP-binding proteins
    • Aspuria, P. J. & Tamanoi, F. The Rheb family of GTP-binding proteins. Cell Signal. 16, 1105-1112 (2004).
    • (2004) Cell Signal , vol.16 , pp. 1105-1112
    • Aspuria, P.J.1    Tamanoi, F.2
  • 4
    • 44449161481 scopus 로고    scopus 로고
    • The TSC1-TSC2 complex: A molecular switchboard controlling cell growth
    • Huang, J. & Manning, B. D. The TSC1-TSC2 complex: a molecular switchboard controlling cell growth. Biochem. J. 412, 179-190 (2008).
    • (2008) Biochem. J. , vol.412 , pp. 179-190
    • Huang, J.1    Manning, B.D.2
  • 5
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C. & Klionsky, D. J. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43, 67-93 (2009).
    • (2009) Annu. Rev. Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 6
    • 65249119430 scopus 로고    scopus 로고
    • Nutrient-dependent mTORC1 association with the ULK1-Atg13- FIP200 complex required for autophagy
    • Hosokawa, N. et al. Nutrient-dependent mTORC1 association with the ULK1-Atg13- FIP200 complex required for autophagy. Mol. Biol. Cell 20, 1981-1991 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1981-1991
    • Hosokawa, N.1
  • 7
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • Jung, C. H. et al. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol. Biol. Cell 20, 1992-2003 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1
  • 8
    • 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. Nat. Cell Biol. 13, 132-141 (2011).
    • (2011) Nat. Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 9
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • Klionsky, D. J. et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 8, 445-544 (2012).
    • (2012) Autophagy , vol.8 , pp. 445-544
    • Klionsky, D.J.1
  • 10
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima, N., Yoshimori, T. & Levine, B. Methods in mammalian autophagy research. Cell 140, 313-326 (2010).
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 11
    • 84876488191 scopus 로고    scopus 로고
    • MTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6
    • Nazio, F. et al. mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6. Nat. Cell Biol. 15, 406-416 (2013).
    • (2013) Nat. Cell Biol , vol.15 , pp. 406-416
    • Nazio, F.1
  • 12
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • Yu, L. et al. Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature 465, 942-946 (2010).
    • (2010) Nature , vol.465 , pp. 942-946
    • Yu, L.1
  • 13
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • Sancak, Y. et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320, 1496-1501 (2008).
    • (2008) Science , vol.320 , pp. 1496-1501
    • Sancak, Y.1
  • 14
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mtor complex 1 pathway by nutrients growth factors and stress
    • Sengupta, S., Peterson, T. R. & Sabatini, D. M. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol. Cell 40, 310-322 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 310-322
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 17
    • 79953316595 scopus 로고    scopus 로고
    • Lysosomal positioning coordinates cellular nutrient responses
    • Korolchuk, V. I. et al. Lysosomal positioning coordinates cellular nutrient responses. Nat. Cell Biol. 13, 453-460 (2011).
    • (2011) Nat. Cell Biol , vol.13 , pp. 453-460
    • Korolchuk, V.I.1
  • 18
    • 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. et al. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290-303 (2010).
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1
  • 19
    • 77749233738 scopus 로고    scopus 로고
    • ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS
    • Alexander, A. et al. ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS. Proc. Natl Acad. Sci. USA 107, 4153-4158 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4153-4158
    • Alexander, A.1
  • 20
    • 33845292901 scopus 로고    scopus 로고
    • Peroxisomes and oxidative stress
    • Schrader, M. & Fahimi, H. D. Peroxisomes and oxidative stress. Biochim. Biophys. Acta 1763, 1755-1766 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1755-1766
    • Schrader, M.1    Fahimi, H.D.2
  • 21
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders, R. J. & Waterham, H. R. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 75, 295-332 (2006).
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 22
    • 79955505833 scopus 로고    scopus 로고
    • Peroxisome assembly: Matrix and membrane protein biogenesis
    • Ma, C., Agrawal, G. & Subramani, S. Peroxisome assembly: matrix and membrane protein biogenesis. J. Cell Biol. 193, 7-16 (2011).
    • (2011) J. Cell Biol , vol.193 , pp. 7-16
    • Ma, C.1    Agrawal, G.2    Subramani, S.3
  • 23
    • 84865371057 scopus 로고    scopus 로고
    • TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1
    • Dibble, C. C. et al. TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1. Mol. Cell 47, 535-546 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 535-546
    • Dibble, C.C.1
  • 24
    • 33646111903 scopus 로고    scopus 로고
    • Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning
    • Cai, S. L. et al. Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning. J. Cell Biol. 173, 279-289 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 279-289
    • Cai, S.L.1
  • 25
    • 63149136365 scopus 로고    scopus 로고
    • Tuberous sclerosis complex, implication from a rare genetic disease to common cancer treatment
    • Inoki, K. & Guan, K. L. Tuberous sclerosis complex, implication from a rare genetic disease to common cancer treatment. Hum. Mol. Genet. 18, R94-R100 (2009).
    • (2009) Hum. Mol. Genet , vol.18
    • Inoki, K.1    Guan, K.L.2
  • 26
    • 0032213545 scopus 로고    scopus 로고
    • The product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles
    • Plank, T. L., Yeung, R. S. & Henske, E. P. Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles. Cancer Res. 58, 4766-4770 (1998).
    • (1998) Cancer Res , vol.58 , pp. 4766-4770
    • Plank, T.L.1    Yeung, R.S.2    Henske3    Hamartin, E.P.4
  • 27
    • 67549084381 scopus 로고    scopus 로고
    • Superoxide is the major reactive oxygen species regulating autophagy
    • Chen, Y., Azad, M. B. & Gibson, S. B. Superoxide is the major reactive oxygen species regulating autophagy. Cell Death Differ. 16, 1040-1052 (2009).
    • (2009) Cell Death Differ , vol.16 , pp. 1040-1052
    • Chen, Y.1    Azad, M.B.2    Gibson, S.B.3
  • 28
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and Specifically regulate the activity of Atg4
    • Scherz-Shouval, R. et al. Reactive oxygen species are essential for autophagy and Specifically regulate the activity of Atg4. EMBO J. 26, 1749-1760 (2007).
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1
  • 29
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma, A. et al. The role of autophagy during the early neonatal starvation period. Nature 432, 1032-1036 (2004).
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1
  • 30
    • 0030896007 scopus 로고    scopus 로고
    • Peroxisome proliferation and beta- oxidation in fao and mh1c1 rat hepatoma cells, hepg2 human hepatoblastoma cells and cultured human hepatocytes: Effect of ciprofibrate
    • Duclos, S., Bride, J., Ramirez, L. C. & Bournot, P. Peroxisome proliferation and beta- oxidation in Fao and MH1C1 rat hepatoma cells, HepG2 human hepatoblastoma cells and cultured human hepatocytes: effect of ciprofibrate. Eur. J. Cell Biol. 72, 314-323 (1997).
    • (1997) Eur. J. Cell Biol , vol.72 , pp. 314-323
    • Duclos, S.1    Bride, J.2    Ramirez, L.C.3    Bournot, P.4
  • 31
    • 0028933657 scopus 로고
    • Comparative effects of clofibrate on peroxisomal enzymes of human (Hep EBNA2) and rat FaO) hepatoma cell lines
    • Scotto, C., Keller, J. M., Schohn, H. & Dauca, M. Comparative effects of clofibrate on peroxisomal enzymes of human (Hep EBNA2) and rat (FaO) hepatoma cell lines. Eur. J. Cell Biol. 66, 375-381 (1995).
    • (1995) Eur. J. Cell Biol , vol.66 , pp. 375-381
    • Scotto, C.1    Keller, J.M.2    Schohn, H.3    Dauca, M.4
  • 33
    • 11844304072 scopus 로고    scopus 로고
    • Restraining PI3K: MTOR signalling goes back to the membrane
    • Harrington, L. S., Findlay, G. M. & Lamb, R. F. Restraining PI3K: mTOR signalling goes back to the membrane. Trends Biochem. Sci. 30, 35-42 (2005).
    • (2005) Trends Biochem. Sci , vol.30 , pp. 35-42
    • Harrington, L.S.1    Findlay, G.M.2    Lamb, R.F.3
  • 35
    • 81755181731 scopus 로고    scopus 로고
    • PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14
    • Freitas, M. O. et al. PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14. J. Biol. Chem. 286, 40509-40519 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 40509-40519
    • Freitas, M.O.1
  • 36
    • 33845321747 scopus 로고    scopus 로고
    • Dynamic architecture of the peroxisomal import receptor Pex5p
    • Stanley, W. A. & Wilmanns, M. Dynamic architecture of the peroxisomal import receptor Pex5p. Biochim. Biophys. Acta 1763, 1592-1598 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1592-1598
    • Stanley, W.A.1    Wilmanns, M.2
  • 37
    • 33947501298 scopus 로고    scopus 로고
    • PTS1-independent sorting of peroxisomal matrix proteins by Pex5p
    • Van der Klei, I. J. & Veenhuis, M. PTS1-independent sorting of peroxisomal matrix proteins by Pex5p. Biochim. Biophys. Acta 1763, 1794-1800 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1794-1800
    • Van Der Klei, I.J.1    Veenhuis, M.2
  • 38
    • 0037102523 scopus 로고    scopus 로고
    • Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin
    • Yamamoto, Y., Jones, K. A., Mak, B. C., Muehlenbachs, A. & Yeung, R. S. Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin. Arch. Biochem. Biophys. 404, 210-217 (2002).
    • (2002) Arch. Biochem. Biophys , vol.404 , pp. 210-217
    • Yamamoto, Y.1    Jones, K.A.2    Mak, B.C.3    Muehlenbachs, A.4    Yeung, R.S.5
  • 39
    • 0035667191 scopus 로고    scopus 로고
    • Pathological mutations in TSC1 and TSC2 disrupt the interaction between hamartin and tuberin
    • Hodges, A. K. et al. Pathological mutations in TSC1 and TSC2 disrupt the interaction between hamartin and tuberin. Hum. Mol. Genet. 10, 2899-2905 (2001).
    • (2001) Hum. Mol. Genet , vol.10 , pp. 2899-2905
    • Hodges, A.K.1
  • 40
    • 51949094890 scopus 로고    scopus 로고
    • Tuberous sclerosis complex proteins control axon formation
    • Choi, Y. J. et al. Tuberous sclerosis complex proteins control axon formation. Genes Dev. 22, 2485-2495 (2008).
    • (2008) Genes Dev , vol.22 , pp. 2485-2495
    • Choi, Y.J.1
  • 41
    • 60749095458 scopus 로고    scopus 로고
    • A reliable cell-based assay for testing unclassified TSC2 gene variants
    • Coevoets, R. et al. A reliable cell-based assay for testing unclassified TSC2 gene variants. Eur. J. Hum. Genet. 17, 301-310 (2009).
    • (2009) Eur. J. Hum. Genet , vol.17 , pp. 301-310
    • Coevoets, R.1
  • 42
    • 0033365408 scopus 로고    scopus 로고
    • Comprehensive mutation analysis of TSC1 and TSC2-and phenotypic correlations in 150 families with tuberous sclerosis
    • Jones, A. C. et al. Comprehensive mutation analysis of TSC1 and TSC2-and phenotypic correlations in 150 families with tuberous sclerosis. Am. J. Hum. Genet. 64, 1305-1315 (1999).
    • (1999) Am. J. Hum. Genet , vol.64 , pp. 1305-1315
    • Jones, A.C.1
  • 43
    • 0035813120 scopus 로고    scopus 로고
    • A single gene produces mitochondrial, cytoplasmic, and peroxisomal NADP-dependent isocitrate dehydrogenase in Aspergillus nidulans
    • Szewczyk, E., Andrianopoulos, A., Davis, M. A. & Hynes, M. J. A single gene produces mitochondrial, cytoplasmic, and peroxisomal NADP-dependent isocitrate dehydrogenase in Aspergillus nidulans. J. Biol. Chem. 276, 37722-37729 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 37722-37729
    • Szewczyk, E.1    Andrianopoulos, A.2    Davis, M.A.3    Hynes, M.J.4
  • 44
    • 75149165986 scopus 로고    scopus 로고
    • Efficient targeting of polyhydroxybutyrate biosynthetic enzymes to plant peroxisomes requires more than three amino acids in the carboxyl-terminal signal
    • Tilbrook, K., Gnanasambandam, A., Schenk, P. M. & Brumbley, S. M. efficient targeting of polyhydroxybutyrate biosynthetic enzymes to plant peroxisomes requires more than three amino acids in the carboxyl-terminal signal. J. Plant Physiol. 167, 329-332 (2010).
    • (2010) J. Plant Physiol , vol.167 , pp. 329-332
    • Tilbrook, K.1    Gnanasambandam, A.2    Schenk, P.M.3    Brumbley, S.M.4
  • 45
    • 0037067768 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxi- somes that is dependent on Pex5p
    • Klein, A. T., van den Berg, M., Bottger, G., Tabak, H. F. & Distel, B. Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxi- somes that is dependent on Pex5p. J. Biol. Chem. 277, 25011-25019 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 25011-25019
    • Klein, A.T.1    Van Den Berg, M.2    Bottger, G.3    Tabak, H.F.4    Distel, B.5
  • 46
    • 80051800850 scopus 로고    scopus 로고
    • Viruses exploiting peroxisomes
    • Lazarow, P. B. Viruses exploiting peroxisomes. Curr. Opin. Microbiol. 14, 458-469 (2011).
    • (2011) Curr. Opin. Microbiol , vol.14 , pp. 458-469
    • Lazarow, P.B.1
  • 47
    • 0036173070 scopus 로고    scopus 로고
    • Identification of a type 1 peroxisomal targeting signal in a viral protein and demonstration of its targeting to the organelle
    • Mohan, K. V., Som, I. & Atreya, C. D. Identification of a type 1 peroxisomal targeting signal in a viral protein and demonstration of its targeting to the organelle. J. Virol. 76, 2543-2547 (2002).
    • (2002) J. Virol , vol.76 , pp. 2543-2547
    • Mohan, K.V.1    Som, I.2    Atreya, C.D.3
  • 48
    • 33846475008 scopus 로고    scopus 로고
    • Akt regulates nuclear/cytoplasmic localization of tuberin
    • Rosner, M., Freilinger, A. & Hengstschlager, M. Akt regulates nuclear/cytoplasmic localization of tuberin. Oncogene 26, 521-531 (2007).
    • (2007) Oncogene , vol.26 , pp. 521-531
    • Rosner, M.1    Freilinger, A.2    Hengstschlager, M.3
  • 49
    • 7144255533 scopus 로고    scopus 로고
    • Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products
    • Van Slegtenhorst, M. et al. Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products. Hum. Mol. Genet. 7, 1053-1057 (1998).
    • (1998) Hum. Mol. Genet , vol.7 , pp. 1053-1057
    • Van Slegtenhorst, M.1
  • 50
    • 1842337009 scopus 로고    scopus 로고
    • Co-localization of the TSC2 product tuberin with its target Rap1 in the Golgi apparatus
    • Wienecke, R. et al. Co-localization of the TSC2 product tuberin with its target Rap1 in the Golgi apparatus. Oncogene 13, 913-923 (1996).
    • (1996) Oncogene , vol.13 , pp. 913-923
    • Wienecke, R.1
  • 51
    • 0037008730 scopus 로고    scopus 로고
    • Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture
    • Zhang, X., Shu, L., Hosoi, H., Murti, K. G. & Houghton, P. J. Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture. J. Biol. Chem. 277, 28127-28134 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 28127-28134
    • Zhang, X.1    Shu, L.2    Hosoi, H.3    Murti, K.G.4    Houghton, P.J.5
  • 52
    • 84877578621 scopus 로고    scopus 로고
    • Rheb regulates mitophagy induced by mitochondrial energetic status
    • Melser, S. et al. Rheb regulates mitophagy induced by mitochondrial energetic status. Cell Metab. 17, 719-730 (2013).
    • (2013) Cell Metab , vol.17 , pp. 719-730
    • Melser, S.1
  • 53
    • 0033607810 scopus 로고    scopus 로고
    • Localization of a portion of extranuclear ATM to peroxisomes
    • Watters, D. et al. Localization of a portion of extranuclear ATM to peroxisomes. J. Biol. Chem. 274, 34277-34282 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 34277-34282
    • Watters, D.1
  • 55
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C. & Blenis, J. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13, 1259-1268 (2003).
    • (2003) Curr. Biol , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 56
    • 21744440266 scopus 로고    scopus 로고
    • Retinoic acid isomers protect hippocampal neurons from amyloid-beta induced neurodegeneration
    • Sahin, M., Karauzum, S. B., Perry, G., Smith, M. A. & Aliciguzel, Y. Retinoic acid isomers protect hippocampal neurons from amyloid-beta induced neurodegeneration. Neurotox Res. 7, 243-250 (2005).
    • (2005) Neurotox Res , vol.7 , pp. 243-250
    • Sahin, M.1    Karauzum, S.B.2    Perry, G.3    Smith, M.A.4    Aliciguzel, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.