메뉴 건너뛰기




Volumn 18, Issue 3, 2013, Pages 380-391

The REGγ proteasome regulates hepatic lipid metabolism through inhibition of autophagy

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; PROTEASOME ACTIVATOR REG GAMMA; SIRTUIN 1; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84883486073     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2013.08.012     Document Type: Article
Times cited : (77)

References (44)
  • 4
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • W.Y. Chen, D.H. Wang, R.C. Yen, J. Luo, W. Gu, and S.B. Baylin Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses Cell 123 2005 437 448
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1    Wang, D.H.2    Yen, R.C.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 5
    • 77951464621 scopus 로고    scopus 로고
    • Autophagy in health and disease. 2. Regulation of lipid metabolism and storage by autophagy: Pathophysiological implications
    • M.J. Czaja Autophagy in health and disease. 2. Regulation of lipid metabolism and storage by autophagy: pathophysiological implications Am. J. Physiol. Cell Physiol. 298 2010 C973 C978
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298
    • Czaja, M.J.1
  • 7
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • W.X. Ding, H.M. Ni, W. Gao, T. Yoshimori, D.B. Stolz, D. Ron, and X.M. Yin Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability Am. J. Pathol. 171 2007 513 524
    • (2007) Am. J. Pathol. , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 8
    • 0026498493 scopus 로고
    • Purification of an 11 S regulator of the multicatalytic protease
    • W. Dubiel, G. Pratt, K. Ferrell, and M. Rechsteiner Purification of an 11 S regulator of the multicatalytic protease J. Biol. Chem. 267 1992 22369 22377
    • (1992) J. Biol. Chem. , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 10
    • 84866184236 scopus 로고    scopus 로고
    • Polysome profiling in liver identifies dynamic regulation of endoplasmic reticulum translatome by obesity and fasting
    • S. Fu, J. Fan, J. Blanco, A. Gimenez-Cassina, N.N. Danial, S.M. Watkins, and G.S. Hotamisligil Polysome profiling in liver identifies dynamic regulation of endoplasmic reticulum translatome by obesity and fasting PLoS Genet. 8 2012 e1002902
    • (2012) PLoS Genet. , vol.8 , pp. 1002902
    • Fu, S.1    Fan, J.2    Blanco, J.3    Gimenez-Cassina, A.4    Danial, N.N.5    Watkins, S.M.6    Hotamisligil, G.S.7
  • 11
    • 79959355078 scopus 로고    scopus 로고
    • Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity
    • Z. Gao, J. Zhang, I. Kheterpal, N. Kennedy, R.J. Davis, and J. Ye Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity J. Biol. Chem. 286 2011 22227 22234
    • (2011) J. Biol. Chem. , vol.286 , pp. 22227-22234
    • Gao, Z.1    Zhang, J.2    Kheterpal, I.3    Kennedy, N.4    Davis, R.J.5    Ye, J.6
  • 12
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • L. Guarente Sir2 links chromatin silencing, metabolism, and aging Genes Dev. 14 2000 1021 1026
    • (2000) Genes Dev. , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 13
    • 84861748047 scopus 로고    scopus 로고
    • Roles of Kruppel-associated Box (KRAB)-associated Co-repressor KAP1 Ser-473 Phosphorylation in DNA Damage Response
    • C. Hu, S. Zhang, X. Gao, X. Gao, X. Xu, Y. Lv, Y. Zhang, Z. Zhu, C. Zhang, and Q. Li Roles of Kruppel-associated Box (KRAB)-associated Co-repressor KAP1 Ser-473 Phosphorylation in DNA Damage Response J. Biol. Chem. 287 2012 18937 18952
    • (2012) J. Biol. Chem. , vol.287 , pp. 18937-18952
    • Hu, C.1    Zhang, S.2    Gao, X.3    Gao, X.4    Xu, X.5    Lv, Y.6    Zhang, Y.7    Zhu, Z.8    Zhang, C.9    Li, Q.10
  • 14
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • V.I. Korolchuk, A. Mansilla, F.M. Menzies, and D.C. Rubinsztein Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates Mol. Cell 33 2009 517 527
    • (2009) Mol. Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 15
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • G. Kroemer, G. Mariño, and B. Levine Autophagy and the integrated stress response Mol. Cell 40 2010 280 293
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 16
    • 65249106104 scopus 로고    scopus 로고
    • Regulation of autophagy by the p300 acetyltransferase
    • I.H. Lee, and T. Finkel Regulation of autophagy by the p300 acetyltransferase J. Biol. Chem. 284 2009 6322 6328
    • (2009) J. Biol. Chem. , vol.284 , pp. 6322-6328
    • Lee, I.H.1    Finkel, T.2
  • 18
    • 31044449824 scopus 로고    scopus 로고
    • The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome
    • X. Li, D.M. Lonard, S.Y. Jung, A. Malovannaya, Q. Feng, J. Qin, S.Y. Tsai, M.J. Tsai, and B.W. O'Malley The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome Cell 124 2006 381 392
    • (2006) Cell , vol.124 , pp. 381-392
    • Li, X.1    Lonard, D.M.2    Jung, S.Y.3    Malovannaya, A.4    Feng, Q.5    Qin, J.6    Tsai, S.Y.7    Tsai, M.J.8    O'Malley, B.W.9
  • 19
    • 34250339984 scopus 로고    scopus 로고
    • Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway
    • X. Li, L. Amazit, W. Long, D.M. Lonard, J.J. Monaco, and B.W. O'Malley Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway Mol. Cell 26 2007 831 842
    • (2007) Mol. Cell , vol.26 , pp. 831-842
    • Li, X.1    Amazit, L.2    Long, W.3    Lonard, D.M.4    Monaco, J.J.5    O'Malley, B.W.6
  • 22
    • 84863268084 scopus 로고    scopus 로고
    • Liver Patt1 deficiency protects male mice from age-associated but not high-fat diet-induced hepatic steatosis
    • Y. Liu, D. Zhou, F. Zhang, Y. Tu, Y. Xia, H. Wang, B. Zhou, Y. Zhang, J. Wu, and X. Gao Liver Patt1 deficiency protects male mice from age-associated but not high-fat diet-induced hepatic steatosis J. Lipid Res. 53 2012 358 367
    • (2012) J. Lipid Res. , vol.53 , pp. 358-367
    • Liu, Y.1    Zhou, D.2    Zhang, F.3    Tu, Y.4    Xia, Y.5    Wang, H.6    Zhou, B.7    Zhang, Y.8    Wu, J.9    Gao, X.10
  • 23
    • 84878746494 scopus 로고    scopus 로고
    • Site-specific acetylation of the proteasome activator REGγ directs its heptameric structure and functions
    • J. Liu, Y. Wang, L. Li, L. Zhou, H. Wei, Q. Zhou, J. Liu, W. Wang, L. Ji, and P. Shan Site-specific acetylation of the proteasome activator REGγ directs its heptameric structure and functions J. Biol. Chem. 288 2013 16567 16578
    • (2013) J. Biol. Chem. , vol.288 , pp. 16567-16578
    • Liu, J.1    Wang, Y.2    Li, L.3    Zhou, L.4    Wei, H.5    Zhou, Q.6    Liu, J.7    Wang, W.8    Ji, L.9    Shan, P.10
  • 24
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • J. Luo, A.Y. Nikolaev, S. Imai, D. Chen, F. Su, A. Shiloh, L. Guarente, and W. Gu Negative control of p53 by Sir2alpha promotes cell survival under stress Cell 107 2001 137 148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 25
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain)
    • C.P. Ma, C.A. Slaughter, and G.N. DeMartino Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain) J. Biol. Chem. 267 1992 10515 10523
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Ma, C.P.1    Slaughter, C.A.2    Demartino, G.N.3
  • 26
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • N. Mizushima Autophagy: process and function Genes Dev. 21 2007 2861 2873
    • (2007) Genes Dev. , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 29
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • S. Nemoto, M.M. Fergusson, and T. Finkel Nutrient availability regulates SIRT1 through a forkhead-dependent pathway Science 306 2004 2105 2108
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 33
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • A. Purushotham, T.T. Schug, Q. Xu, S. Surapureddi, X.M. Guo, and X.L. Li Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation Cell Metab. 9 2009 327 338
    • (2009) Cell Metab. , vol.9 , pp. 327-338
    • Purushotham, A.1    Schug, T.T.2    Xu, Q.3    Surapureddi, S.4    Guo, X.M.5    Li, X.L.6
  • 35
    • 35448999693 scopus 로고    scopus 로고
    • Effect of starvation on global gene expression and proteolysis in rainbow trout (Oncorhynchus mykiss)
    • M. Salem, J. Silverstein, C.E. Rexroad 3rd, and J. Yao Effect of starvation on global gene expression and proteolysis in rainbow trout (Oncorhynchus mykiss) BMC Genomics 8 2007 328
    • (2007) BMC Genomics , vol.8 , pp. 328
    • Salem, M.1    Silverstein, J.2    Rexroad III, C.E.3    Yao, J.4
  • 36
    • 84859768059 scopus 로고    scopus 로고
    • Lipophagy: Connecting autophagy and lipid metabolism
    • R. Singh, and A.M. Cuervo Lipophagy: connecting autophagy and lipid metabolism Int. J. Cell Biol. 2012 2012 282041
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 282041
    • Singh, R.1    Cuervo, A.M.2
  • 40
    • 0344528638 scopus 로고    scopus 로고
    • Proteasome activator subunit PA28 alpha and related Ki antigen (PA28 gamma) are absent from the nuclear fraction purified by sucrose gradient centrifugation
    • C. Wójcik Proteasome activator subunit PA28 alpha and related Ki antigen (PA28 gamma) are absent from the nuclear fraction purified by sucrose gradient centrifugation Int. J. Biochem. Cell Biol. 31 1999 273 276
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 273-276
    • Wójcik, C.1
  • 41
    • 77956400005 scopus 로고    scopus 로고
    • Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance
    • L. Yang, P. Li, S.N. Fu, E.S. Calay, and G.S. Hotamisligil Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance Cell Metab. 11 2010 467 478
    • (2010) Cell Metab. , vol.11 , pp. 467-478
    • Yang, L.1    Li, P.2    Fu, S.N.3    Calay, E.S.4    Hotamisligil, G.S.5
  • 43
    • 73949124173 scopus 로고    scopus 로고
    • Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis
    • Y. Zhang, S. Goldman, R. Baerga, Y. Zhao, M. Komatsu, and S.K. Jin Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis Proc. Natl. Acad. Sci. USA 106 2009 19860 19865
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19860-19865
    • Zhang, Y.1    Goldman, S.2    Baerga, R.3    Zhao, Y.4    Komatsu, M.5    Jin, S.K.6
  • 44
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • W. Zhao, J.P. Kruse, Y. Tang, S.Y. Jung, J. Qin, and W. Gu Negative regulation of the deacetylase SIRT1 by DBC1 Nature 451 2008 587 590
    • (2008) Nature , vol.451 , pp. 587-590
    • Zhao, W.1    Kruse, J.P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.