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Volumn 20, Issue 3, 2014, Pages 458-470

The ER-associated degradation adaptor protein sel1l regulates LPL secretion and lipid metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; LIPASE MATURATION FACTOR 1; LIPID; LIPOPROTEIN LIPASE; MEMBRANE PROTEIN; SEL 1 SUPPRESSOR OF LIN 12 LIKE PROTEIN; UNCLASSIFIED DRUG; LMF1 PROTEIN, MOUSE; PROTEIN; PROTEIN AGGREGATE; SEL1H PROTEIN, MOUSE;

EID: 84913536702     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2014.06.015     Document Type: Article
Times cited : (96)

References (47)
  • 1
    • 0026697404 scopus 로고
    • Maturation of lipoprotein lipase. Expression of full catalytic activity requires glucose trimming but not translocation to the cis-Golgi compartment
    • O. Ben-Zeev, M.H. Doolittle, R.C. Davis, J. Elovson, and M.C. Schotz Maturation of lipoprotein lipase. Expression of full catalytic activity requires glucose trimming but not translocation to the cis-Golgi compartment J. Biol. Chem. 267 1992 6219 6227
    • (1992) J. Biol. Chem. , vol.267 , pp. 6219-6227
    • Ben-Zeev, O.1    Doolittle, M.H.2    Davis, R.C.3    Elovson, J.4    Schotz, M.C.5
  • 2
    • 0037155921 scopus 로고    scopus 로고
    • Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates
    • O. Ben-Zeev, H.Z. Mao, and M.H. Doolittle Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates J. Biol. Chem. 277 2002 10727 10738
    • (2002) J. Biol. Chem. , vol.277 , pp. 10727-10738
    • Ben-Zeev, O.1    Mao, H.Z.2    Doolittle, M.H.3
  • 3
    • 76149098224 scopus 로고    scopus 로고
    • Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates
    • R. Bernasconi, C. Galli, V. Calanca, T. Nakajima, and M. Molinari Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates J. Cell Biol. 188 2010 223 235
    • (2010) J. Cell Biol. , vol.188 , pp. 223-235
    • Bernasconi, R.1    Galli, C.2    Calanca, V.3    Nakajima, T.4    Molinari, M.5
  • 4
    • 0032622210 scopus 로고    scopus 로고
    • Determining lipoprotein lipase and hepatic lipase activity using radiolabeled substrates
    • V. Briquet-Laugier, O. Ben-Zeev, and M.H. Doolittle Determining lipoprotein lipase and hepatic lipase activity using radiolabeled substrates Methods Mol. Biol. 109 1999 81 94
    • (1999) Methods Mol. Biol. , vol.109 , pp. 81-94
    • Briquet-Laugier, V.1    Ben-Zeev, O.2    Doolittle, M.H.3
  • 5
    • 84872483502 scopus 로고    scopus 로고
    • Postprandial hypertriglyceridemia and cardiovascular disease: Current and future therapies
    • D.C. Chan, J. Pang, G. Romic, and G.F. Watts Postprandial hypertriglyceridemia and cardiovascular disease: current and future therapies Curr. Atheroscler. Rep. 15 2013 309
    • (2013) Curr. Atheroscler. Rep. , vol.15 , pp. 309
    • Chan, D.C.1    Pang, J.2    Romic, G.3    Watts, G.F.4
  • 6
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 84894387971 scopus 로고    scopus 로고
    • Regulation of lipoprotein lipase by Angptl4
    • W. Dijk, and S. Kersten Regulation of lipoprotein lipase by Angptl4 Trends Endocrinol. Metab. 25 2014 146 155
    • (2014) Trends Endocrinol. Metab. , vol.25 , pp. 146-155
    • Dijk, W.1    Kersten, S.2
  • 8
  • 10
    • 77951564358 scopus 로고    scopus 로고
    • Deficiency of suppressor enhancer Lin12 1 like (SEL1L) in mice leads to systemic endoplasmic reticulum stress and embryonic lethality
    • A.B. Francisco, R. Singh, S. Li, A.K. Vani, L. Yang, R.J. Munroe, G. Diaferia, M. Cardano, I. Biunno, and L. Qi Deficiency of suppressor enhancer Lin12 1 like (SEL1L) in mice leads to systemic endoplasmic reticulum stress and embryonic lethality J. Biol. Chem. 285 2010 13694 13703
    • (2010) J. Biol. Chem. , vol.285 , pp. 13694-13703
    • Francisco, A.B.1    Singh, R.2    Li, S.3    Vani, A.K.4    Yang, L.5    Munroe, R.J.6    Diaferia, G.7    Cardano, M.8    Biunno, I.9    Qi, L.10
  • 11
    • 34247113888 scopus 로고    scopus 로고
    • Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: Ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II)
    • E. Fujita, Y. Kouroku, A. Isoai, H. Kumagai, A. Misutani, C. Matsuda, Y.K. Hayashi, and T. Momoi Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II) Hum. Mol. Genet. 16 2007 618 629
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 618-629
    • Fujita, E.1    Kouroku, Y.2    Isoai, A.3    Kumagai, H.4    Misutani, A.5    Matsuda, C.6    Hayashi, Y.K.7    Momoi, T.8
  • 14
    • 0029666010 scopus 로고    scopus 로고
    • The Caenorhabditis elegans sel-1 gene, a negative regulator of lin-12 and glp-1, encodes a predicted extracellular protein
    • B. Grant, and I. Greenwald The Caenorhabditis elegans sel-1 gene, a negative regulator of lin-12 and glp-1, encodes a predicted extracellular protein Genetics 143 1996 237 247
    • (1996) Genetics , vol.143 , pp. 237-247
    • Grant, B.1    Greenwald, I.2
  • 15
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • R.Y. Hampton, R.G. Gardner, and J. Rine Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein Mol. Biol. Cell 7 1996 2029 2044
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 17
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • C. Hetz The unfolded protein response: controlling cell fate decisions under ER stress and beyond Nat. Rev. Mol. Cell Biol. 13 2012 89 102
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 19
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • G.S. Hotamisligil Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Cell 140 2010 900 917
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 20
    • 84863253136 scopus 로고    scopus 로고
    • Cellular responses to misfolded proteins and protein aggregates
    • S.A. Houck, S. Singh, and D.M. Cyr Cellular responses to misfolded proteins and protein aggregates Methods Mol. Biol. 832 2012 455 461
    • (2012) Methods Mol. Biol. , vol.832 , pp. 455-461
    • Houck, S.A.1    Singh, S.2    Cyr, D.M.3
  • 21
    • 84897986050 scopus 로고    scopus 로고
    • Quality control autophagy degrades soluble ERAD-resistant conformers of the misfolded membrane protein GnRHR
    • S.A. Houck, H.Y. Ren, V.J. Madden, J.N. Bonner, M.P. Conlin, J.A. Janovick, P.M. Conn, and D.M. Cyr Quality control autophagy degrades soluble ERAD-resistant conformers of the misfolded membrane protein GnRHR Mol. Cell 54 2014 166 179
    • (2014) Mol. Cell , vol.54 , pp. 166-179
    • Houck, S.A.1    Ren, H.Y.2    Madden, V.J.3    Bonner, J.N.4    Conlin, M.P.5    Janovick, J.A.6    Conn, P.M.7    Cyr, D.M.8
  • 23
    • 0027232560 scopus 로고
    • Assembly of lipoprotein lipase in perfused guinea-pig hearts
    • G. Liu, G. Bengtsson-Olivecrona, and T. Olivecrona Assembly of lipoprotein lipase in perfused guinea-pig hearts Biochem. J. 292 1993 277 282
    • (1993) Biochem. J. , vol.292 , pp. 277-282
    • Liu, G.1    Bengtsson-Olivecrona, G.2    Olivecrona, T.3
  • 24
    • 84864684825 scopus 로고    scopus 로고
    • Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis
    • T.F. Liu, J.J. Tang, P.S. Li, Y. Shen, J.G. Li, H.H. Miao, B.L. Li, and B.L. Song Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis Cell Metab. 16 2012 213 225
    • (2012) Cell Metab. , vol.16 , pp. 213-225
    • Liu, T.F.1    Tang, J.J.2    Li, P.S.3    Shen, Y.4    Li, J.G.5    Miao, H.H.6    Li, B.L.7    Song, B.L.8
  • 25
    • 33750359201 scopus 로고    scopus 로고
    • SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
    • B. Mueller, B.N. Lilley, and H.L. Ploegh SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER J. Cell Biol. 175 2006 261 270
    • (2006) J. Cell Biol. , vol.175 , pp. 261-270
    • Mueller, B.1    Lilley, B.N.2    Ploegh, H.L.3
  • 26
  • 27
    • 33744755382 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B
    • Y. Ohsaki, J. Cheng, A. Fujita, T. Tokumoto, and T. Fujimoto Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B Mol. Biol. Cell 17 2006 2674 2683
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2674-2683
    • Ohsaki, Y.1    Cheng, J.2    Fujita, A.3    Tokumoto, T.4    Fujimoto, T.5
  • 29
    • 84859159989 scopus 로고    scopus 로고
    • Lipase maturation factor 1: A lipase chaperone involved in lipid metabolism
    • M. Péterfy Lipase maturation factor 1: a lipase chaperone involved in lipid metabolism Biochim. Biophys. Acta 1821 2012 790 794
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 790-794
    • Péterfy, M.1
  • 31
    • 79955111850 scopus 로고    scopus 로고
    • Hepatic autophagy mediates endoplasmic reticulum stress-induced degradation of misfolded apolipoprotein B
    • W. Qiu, J. Zhang, M.J. Dekker, H. Wang, J. Huang, J.H. Brumell, and K. Adeli Hepatic autophagy mediates endoplasmic reticulum stress-induced degradation of misfolded apolipoprotein B Hepatology 53 2011 1515 1525
    • (2011) Hepatology , vol.53 , pp. 1515-1525
    • Qiu, W.1    Zhang, J.2    Dekker, M.J.3    Wang, H.4    Huang, J.5    Brumell, J.H.6    Adeli, K.7
  • 32
    • 35348827324 scopus 로고    scopus 로고
    • That which does not kill me makes me stronger: Adapting to chronic ER stress
    • D.T. Rutkowski, and R.J. Kaufman That which does not kill me makes me stronger: adapting to chronic ER stress Trends Biochem. Sci. 32 2007 469 476
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 469-476
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 33
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • A. Sakakibara, M. Furuse, M. Saitou, Y. Ando-Akatsuka, and S. Tsukita Possible involvement of phosphorylation of occludin in tight junction formation J. Cell Biol. 137 1997 1393 1401
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 34
    • 84894429746 scopus 로고    scopus 로고
    • Adipocyte spliced form of X-box-binding protein 1 promotes adiponectin multimerization and systemic glucose homeostasis
    • H. Sha, L. Yang, M. Liu, S. Xia, Y. Liu, F. Liu, S. Kersten, and L. Qi Adipocyte spliced form of X-box-binding protein 1 promotes adiponectin multimerization and systemic glucose homeostasis Diabetes 63 2014 867 879
    • (2014) Diabetes , vol.63 , pp. 867-879
    • Sha, H.1    Yang, L.2    Liu, M.3    Xia, S.4    Liu, Y.5    Liu, F.6    Kersten, S.7    Qi, L.8
  • 35
    • 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
  • 36
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • M.H. Smith, H.L. Ploegh, and J.S. Weissman Road to ruin: targeting proteins for degradation in the endoplasmic reticulum Science 334 2011 1086 1090
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 37
    • 84861869574 scopus 로고    scopus 로고
    • The ATP-P2X7 signaling axis is dispensable for obesity-associated inflammasome activation in adipose tissue
    • S. Sun, S. Xia, Y. Ji, S. Kersten, and L. Qi The ATP-P2X7 signaling axis is dispensable for obesity-associated inflammasome activation in adipose tissue Diabetes 61 2012 1471 1478
    • (2012) Diabetes , vol.61 , pp. 1471-1478
    • Sun, S.1    Xia, S.2    Ji, Y.3    Kersten, S.4    Qi, L.5
  • 39
    • 0027435169 scopus 로고
    • Suppressors of a lin-12 hypomorph define genes that interact with both lin-12 and glp-1 in Caenorhabditis elegans
    • M. Sundaram, and I. Greenwald Suppressors of a lin-12 hypomorph define genes that interact with both lin-12 and glp-1 in Caenorhabditis elegans Genetics 135 1993 765 783
    • (1993) Genetics , vol.135 , pp. 765-783
    • Sundaram, M.1    Greenwald, I.2
  • 40
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • J.H. Teckman, and D.H. Perlmutter Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response Am. J. Physiol. Gastrointest. Liver Physiol. 279 2000 G961 G974
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279 , pp. 961-G974
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 41
    • 0024368843 scopus 로고
    • Biosynthesis of lipoprotein lipase in cultured mouse adipocytes. II. Processing, subunit assembly, and intracellular transport
    • C. Vannier, and G. Ailhaud Biosynthesis of lipoprotein lipase in cultured mouse adipocytes. II. Processing, subunit assembly, and intracellular transport J. Biol. Chem. 264 1989 13206 13216
    • (1989) J. Biol. Chem. , vol.264 , pp. 13206-13216
    • Vannier, C.1    Ailhaud, G.2
  • 43
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Q. Wang, Y. Liu, N. Soetandyo, K. Baek, R. Hegde, and Y. Ye A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation Mol. Cell 42 2011 758 770
    • (2011) Mol. Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 45
    • 55849135236 scopus 로고    scopus 로고
    • Molecular processes that handle - And mishandle - Dietary lipids
    • K.J. Williams Molecular processes that handle - and mishandle - dietary lipids J. Clin. Invest. 118 2008 3247 3259
    • (2008) J. Clin. Invest. , vol.118 , pp. 3247-3259
    • Williams, K.J.1
  • 47
    • 77449096697 scopus 로고    scopus 로고
    • Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance
    • R. Ye, D.Y. Jung, J.Y. Jun, J. Li, S. Luo, H.J. Ko, J.K. Kim, and A.S. Lee Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance Diabetes 59 2010 6 16
    • (2010) Diabetes , vol.59 , pp. 6-16
    • Ye, R.1    Jung, D.Y.2    Jun, J.Y.3    Li, J.4    Luo, S.5    Ko, H.J.6    Kim, J.K.7    Lee, A.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.