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Volumn 20, Issue 3, 2013, Pages 391-402

Discovery of oxysterol-derived pharmacological chaperones for NPC1: Implication for the existence of second sterol-binding site

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; MEMBRANE PROTEIN; MUTANT PROTEIN; NIEMANN PICK TYPE C1 PROTEIN; OXYSTEROL; UNCLASSIFIED DRUG;

EID: 84875448226     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2013.02.009     Document Type: Article
Times cited : (59)

References (56)
  • 1
    • 79959654327 scopus 로고    scopus 로고
    • Unesterified cholesterol accumulation in late endosomes/lysosomes causes neurodegeneration and is prevented by driving cholesterol export from this compartment
    • A. Aqul, B. Liu, C.M. Ramirez, A.A. Pieper, S.J. Estill, D.K. Burns, B. Liu, J.J. Repa, S.D. Turley, and J.M. Dietschy Unesterified cholesterol accumulation in late endosomes/lysosomes causes neurodegeneration and is prevented by driving cholesterol export from this compartment J. Neurosci. 31 2011 9404 9413
    • (2011) J. Neurosci. , vol.31 , pp. 9404-9413
    • Aqul, A.1    Liu, B.2    Ramirez, C.M.3    Pieper, A.A.4    Estill, S.J.5    Burns, D.K.6    Liu, B.7    Repa, J.J.8    Turley, S.D.9    Dietschy, J.M.10
  • 2
    • 77956093932 scopus 로고    scopus 로고
    • Identification of HSP60 as a primary target of o- carboranylphenoxyacetanilide, an HIF-1alpha inhibitor
    • H.S. Ban, K. Shimizu, H. Minegishi, and H. Nakamura Identification of HSP60 as a primary target of o-carboranylphenoxyacetanilide, an HIF-1alpha inhibitor J. Am. Chem. Soc. 132 2010 11870 11871
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11870-11871
    • Ban, H.S.1    Shimizu, K.2    Minegishi, H.3    Nakamura, H.4
  • 3
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • S. Bolte, and F.P. Cordelières A guided tour into subcellular colocalization analysis in light microscopy J. Microsc. 224 2006 213 232
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 6
    • 70349190528 scopus 로고    scopus 로고
    • Chronic cyclodextrin treatment of murine Niemann-Pick C disease ameliorates neuronal cholesterol and glycosphingolipid storage and disease progression
    • C.D. Davidson, N.F. Ali, M.C. Micsenyi, G. Stephney, S. Renault, K. Dobrenis, D.S. Ory, M.T. Vanier, and S.U. Walkley Chronic cyclodextrin treatment of murine Niemann-Pick C disease ameliorates neuronal cholesterol and glycosphingolipid storage and disease progression PLoS ONE 4 2009 e6951
    • (2009) PLoS ONE , vol.4 , pp. 6951
    • Davidson, C.D.1    Ali, N.F.2    Micsenyi, M.C.3    Stephney, G.4    Renault, S.5    Dobrenis, K.6    Ory, D.S.7    Vanier, M.T.8    Walkley, S.U.9
  • 7
    • 0034637440 scopus 로고    scopus 로고
    • Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein
    • J.P. Davies, and Y.A. Ioannou Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein J. Biol. Chem. 275 2000 24367 24374
    • (2000) J. Biol. Chem. , vol.275 , pp. 24367-24374
    • Davies, J.P.1    Ioannou, Y.A.2
  • 8
    • 0034704244 scopus 로고    scopus 로고
    • Transmembrane molecular pump activity of Niemann-Pick C1 protein
    • J.P. Davies, F.W. Chen, and Y.A. Ioannou Transmembrane molecular pump activity of Niemann-Pick C1 protein Science 290 2000 2295 2298
    • (2000) Science , vol.290 , pp. 2295-2298
    • Davies, J.P.1    Chen, F.W.2    Ioannou, Y.A.3
  • 9
    • 82755197370 scopus 로고    scopus 로고
    • Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding
    • M.S. Deffieu, and S.R. Pfeffer Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding Proc. Natl. Acad. Sci. USA 108 2011 18932 18936
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18932-18936
    • Deffieu, M.S.1    Pfeffer, S.R.2
  • 10
    • 0043235841 scopus 로고    scopus 로고
    • A contradictory treatment for lysosomal storage disorders: Inhibitors enhance mutant enzyme activity
    • J.Q. Fan A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity Trends Pharmacol. Sci. 24 2003 355 360
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 355-360
    • Fan, J.Q.1
  • 11
    • 43749115379 scopus 로고    scopus 로고
    • Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding
    • M.E. Gelsthorpe, N. Baumann, E. Millard, S.E. Gale, S.J. Langmade, J.E. Schaffer, and D.S. Ory Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding J. Biol. Chem. 283 2008 8229 8236
    • (2008) J. Biol. Chem. , vol.283 , pp. 8229-8236
    • Gelsthorpe, M.E.1    Baumann, N.2    Millard, E.3    Gale, S.E.4    Langmade, S.J.5    Schaffer, J.E.6    Ory, D.S.7
  • 12
    • 3142774112 scopus 로고    scopus 로고
    • Niemann-Pick type C disease involves disrupted neurosteroidogenesis and responds to allopregnanolone
    • L.D. Griffin, W. Gong, L. Verot, and S.H. Mellon Niemann-Pick type C disease involves disrupted neurosteroidogenesis and responds to allopregnanolone Nat. Med. 10 2004 704 711
    • (2004) Nat. Med. , vol.10 , pp. 704-711
    • Griffin, L.D.1    Gong, W.2    Verot, L.3    Mellon, S.H.4
  • 13
    • 12144289185 scopus 로고    scopus 로고
    • Novel bifunctional probe for radioisotope-free photoaffinity labeling: Compact structure comprised of photospecific ligand ligation and detectable tag anchoring units
    • T. Hosoya, T. Hiramatsu, T. Ikemoto, M. Nakanishi, H. Aoyama, A. Hosoya, T. Iwata, K. Maruyama, M. Endo, and M. Suzuki Novel bifunctional probe for radioisotope-free photoaffinity labeling: compact structure comprised of photospecific ligand ligation and detectable tag anchoring units Org. Biomol. Chem. 2 2004 637 641
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 637-641
    • Hosoya, T.1    Hiramatsu, T.2    Ikemoto, T.3    Nakanishi, M.4    Aoyama, H.5    Hosoya, A.6    Iwata, T.7    Maruyama, K.8    Endo, M.9    Suzuki, M.10
  • 14
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein
    • X. Hua, A. Nohturfft, J.L. Goldstein, and M.S. Brown Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein Cell 87 1996 415 426
    • (1996) Cell , vol.87 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 15
    • 38149069055 scopus 로고    scopus 로고
    • Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein
    • R.E. Infante, L. Abi-Mosleh, A. Radhakrishnan, J.D. Dale, M.S. Brown, and J.L. Goldstein Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein J. Biol. Chem. 283 2008 1052 1063
    • (2008) J. Biol. Chem. , vol.283 , pp. 1052-1063
    • Infante, R.E.1    Abi-Mosleh, L.2    Radhakrishnan, A.3    Dale, J.D.4    Brown, M.S.5    Goldstein, J.L.6
  • 17
    • 55749083068 scopus 로고    scopus 로고
    • NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes
    • R.E. Infante, M.L. Wang, A. Radhakrishnan, H.J. Kwon, M.S. Brown, and J.L. Goldstein NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes Proc. Natl. Acad. Sci. USA 105 2008 15287 15292
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15287-15292
    • Infante, R.E.1    Wang, M.L.2    Radhakrishnan, A.3    Kwon, H.J.4    Brown, M.S.5    Goldstein, J.L.6
  • 18
    • 0035458847 scopus 로고    scopus 로고
    • Multidrug permeases and subcellular cholesterol transport
    • Y.A. Ioannou Multidrug permeases and subcellular cholesterol transport Nat. Rev. Mol. Cell Biol. 2 2001 657 668
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 657-668
    • Ioannou, Y.A.1
  • 19
    • 0027787898 scopus 로고
    • Characterization of a mutant alpha-galactosidase gene product for the late-onset cardiac form of Fabry disease
    • S. Ishii, R. Kase, H. Sakuraba, and Y. Suzuki Characterization of a mutant alpha-galactosidase gene product for the late-onset cardiac form of Fabry disease Biochem. Biophys. Res. Commun. 197 1993 1585 1589
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1585-1589
    • Ishii, S.1    Kase, R.2    Sakuraba, H.3    Suzuki, Y.4
  • 20
    • 0035163949 scopus 로고    scopus 로고
    • Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events
    • D.C. Ko, M.D. Gordon, J.Y. Jin, and M.P. Scott Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events Mol. Biol. Cell 12 2001 601 614
    • (2001) Mol. Biol. Cell , vol.12 , pp. 601-614
    • Ko, D.C.1    Gordon, M.D.2    Jin, J.Y.3    Scott, M.P.4
  • 21
    • 0036534286 scopus 로고    scopus 로고
    • The sterol-sensing domain: Multiple families, a unique role?
    • P.E. Kuwabara, and M. Labouesse The sterol-sensing domain: multiple families, a unique role? Trends Genet. 18 2002 193 201
    • (2002) Trends Genet. , vol.18 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 22
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • H.J. Kwon, L. Abi-Mosleh, M.L. Wang, J. Deisenhofer, J.L. Goldstein, M.S. Brown, and R.E. Infante Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol Cell 137 2009 1213 1224
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6    Infante, R.E.7
  • 23
    • 59449095489 scopus 로고    scopus 로고
    • Characterization of fluorescent sterol binding to purified human NPC1
    • R. Liu, P. Lu, J.W. Chu, and F.J. Sharom Characterization of fluorescent sterol binding to purified human NPC1 J. Biol. Chem. 284 2009 1840 1852
    • (2009) J. Biol. Chem. , vol.284 , pp. 1840-1852
    • Liu, R.1    Lu, P.2    Chu, J.W.3    Sharom, F.J.4
  • 24
    • 60549084168 scopus 로고    scopus 로고
    • Reversal of defective lysosomal transport in NPC disease ameliorates liver dysfunction and neurodegeneration in the npc1-/- mouse
    • B. Liu, S.D. Turley, D.K. Burns, A.M. Miller, J.J. Repa, and J.M. Dietschy Reversal of defective lysosomal transport in NPC disease ameliorates liver dysfunction and neurodegeneration in the npc1-/- mouse Proc. Natl. Acad. Sci. USA 106 2009 2377 2382
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2377-2382
    • Liu, B.1    Turley, S.D.2    Burns, D.K.3    Miller, A.M.4    Repa, J.J.5    Dietschy, J.M.6
  • 26
    • 0031021804 scopus 로고    scopus 로고
    • Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators
    • T.W. Loo, and D.M. Clarke Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators J. Biol. Chem. 272 1997 709 712
    • (1997) J. Biol. Chem. , vol.272 , pp. 709-712
    • Loo, T.W.1    Clarke, D.M.2
  • 27
    • 34547105186 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones as new therapeutic agents
    • T.W. Loo, and D.M. Clarke Chemical and pharmacological chaperones as new therapeutic agents Expert Rev. Mol. Med. 9 2007 1 18
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-18
    • Loo, T.W.1    Clarke, D.M.2
  • 28
    • 0030473469 scopus 로고    scopus 로고
    • Inverse agonist-induced up-regulation of the human beta2-adrenoceptor in transfected neuroblastoma X glioma hybrid cells
    • D.J. MacEwan, and G. Milligan Inverse agonist-induced up-regulation of the human beta2-adrenoceptor in transfected neuroblastoma X glioma hybrid cells Mol. Pharmacol. 50 1996 1479 1486
    • (1996) Mol. Pharmacol. , vol.50 , pp. 1479-1486
    • MacEwan, D.J.1    Milligan, G.2
  • 29
    • 36749047362 scopus 로고    scopus 로고
    • Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation
    • A.L. MacKinnon, J.L. Garrison, R.S. Hegde, and J. Taunton Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation J. Am. Chem. Soc. 129 2007 14560 14561
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14560-14561
    • MacKinnon, A.L.1    Garrison, J.L.2    Hegde, R.S.3    Taunton, J.4
  • 32
    • 79955973156 scopus 로고    scopus 로고
    • Identification of luminal Loop 1 of Scap protein as the sterol sensor that maintains cholesterol homeostasis
    • M. Motamed, Y. Zhang, M.L. Wang, J. Seemann, H.J. Kwon, J.L. Goldstein, and M.S. Brown Identification of luminal Loop 1 of Scap protein as the sterol sensor that maintains cholesterol homeostasis J. Biol. Chem. 286 2011 18002 18012
    • (2011) J. Biol. Chem. , vol.286 , pp. 18002-18012
    • Motamed, M.1    Zhang, Y.2    Wang, M.L.3    Seemann, J.4    Kwon, H.J.5    Goldstein, J.L.6    Brown, M.S.7
  • 35
    • 84868139156 scopus 로고    scopus 로고
    • Intracellular cholesterol transport by NPC1/NPC2: Mysteries of Niemann-Pick disease type C
    • K. Morikawa, S. Tate, Transworld Research Network Kerala, India
    • H. Ninomiya Intracellular cholesterol transport by NPC1/NPC2: Mysteries of Niemann-Pick disease type C K. Morikawa, S. Tate, Functional and Structural Biology on the Lipo-Network 2006 Transworld Research Network Kerala, India 1 15
    • (2006) Functional and Structural Biology on the Lipo-Network , pp. 1-15
    • Ninomiya, H.1
  • 36
    • 4344637102 scopus 로고    scopus 로고
    • Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain
    • N. Ohgami, D.C. Ko, M. Thomas, M.P. Scott, C.C. Chang, and T.Y. Chang Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain Proc. Natl. Acad. Sci. USA 101 2004 12473 12478
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12473-12478
    • Ohgami, N.1    Ko, D.C.2    Thomas, M.3    Scott, M.P.4    Chang, C.C.5    Chang, T.Y.6
  • 38
    • 0034672696 scopus 로고    scopus 로고
    • Niemann-Pick type C: A disorder of cellular cholesterol trafficking
    • D.S. Ory Niemann-Pick type C: a disorder of cellular cholesterol trafficking Biochim. Biophys. Acta 1529 2000 331 339
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 331-339
    • Ory, D.S.1
  • 40
    • 34547753513 scopus 로고    scopus 로고
    • Miglustat for treatment of Niemann-Pick C disease: A randomised controlled study
    • M.C. Patterson, D. Vecchio, H. Prady, L. Abel, and J.E. Wraith Miglustat for treatment of Niemann-Pick C disease: a randomised controlled study Lancet Neurol. 6 2007 765 772
    • (2007) Lancet Neurol. , vol.6 , pp. 765-772
    • Patterson, M.C.1    Vecchio, D.2    Prady, H.3    Abel, L.4    Wraith, J.E.5
  • 43
    • 0034986205 scopus 로고    scopus 로고
    • Detection of receptor ligands by monitoring selective stabilization of a Renilla luciferase-tagged, constitutively active mutant, G-protein-coupled receptor
    • D. Ramsay, N. Bevan, S. Rees, and G. Milligan Detection of receptor ligands by monitoring selective stabilization of a Renilla luciferase-tagged, constitutively active mutant, G-protein-coupled receptor Br. J. Pharmacol. 133 2001 315 323
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 315-323
    • Ramsay, D.1    Bevan, N.2    Rees, S.3    Milligan, G.4
  • 44
    • 79851476221 scopus 로고    scopus 로고
    • Niemann-Pick type C disease: Molecular mechanisms and potential therapeutic approaches
    • A.I. Rosenbaum, and F.R. Maxfield Niemann-Pick type C disease: molecular mechanisms and potential therapeutic approaches J. Neurochem. 116 2011 789 795
    • (2011) J. Neurochem. , vol.116 , pp. 789-795
    • Rosenbaum, A.I.1    Maxfield, F.R.2
  • 45
    • 9144244897 scopus 로고    scopus 로고
    • Targeting of NPC1 to late endosomes involves multiple signals, including one residing within the putative sterol-sensing domain
    • C. Scott, M.E. Higgins, J.P. Davies, and Y.A. Ioannou Targeting of NPC1 to late endosomes involves multiple signals, including one residing within the putative sterol-sensing domain J. Biol. Chem. 279 2004 48214 48223
    • (2004) J. Biol. Chem. , vol.279 , pp. 48214-48223
    • Scott, C.1    Higgins, M.E.2    Davies, J.P.3    Ioannou, Y.A.4
  • 47
  • 48
    • 78649916808 scopus 로고    scopus 로고
    • Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes
    • M.L. Wang, M. Motamed, R.E. Infante, L. Abi-Mosleh, H.J. Kwon, M.S. Brown, and J.L. Goldstein Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes Cell Metab. 12 2010 166 173
    • (2010) Cell Metab. , vol.12 , pp. 166-173
    • Wang, M.L.1    Motamed, M.2    Infante, R.E.3    Abi-Mosleh, L.4    Kwon, H.J.5    Brown, M.S.6    Goldstein, J.L.7
  • 51
    • 0034714439 scopus 로고    scopus 로고
    • Determinants of NPC1 expression and action: Key promoter regions, posttranscriptional control, and the importance of a "cysteine-rich" loop
    • H. Watari, E.J. Blanchette-Mackie, N.K. Dwyer, M. Watari, C.G. Burd, S. Patel, P.G. Pentchev, and J.F. Strauss 3rd Determinants of NPC1 expression and action: key promoter regions, posttranscriptional control, and the importance of a "cysteine-rich" loop Exp. Cell Res. 259 2000 247 256
    • (2000) Exp. Cell Res. , vol.259 , pp. 247-256
    • Watari, H.1    Blanchette-Mackie, E.J.2    Dwyer, N.K.3    Watari, M.4    Burd, C.G.5    Patel, S.6    Pentchev, P.G.7    Strauss III, J.F.8
  • 52
    • 80053085866 scopus 로고    scopus 로고
    • Amino acid substitution in NPC1 that abolishes cholesterol binding reproduces phenotype of complete NPC1 deficiency in mice
    • X. Xie, M.S. Brown, J.M. Shelton, J.A. Richardson, J.L. Goldstein, and G. Liang Amino acid substitution in NPC1 that abolishes cholesterol binding reproduces phenotype of complete NPC1 deficiency in mice Proc. Natl. Acad. Sci. USA 108 2011 15330 15335
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 15330-15335
    • Xie, X.1    Brown, M.S.2    Shelton, J.M.3    Richardson, J.A.4    Goldstein, J.L.5    Liang, G.6
  • 53
    • 0033832873 scopus 로고    scopus 로고
    • Genotype-phenotype relationship of Niemann-Pick disease type C: A possible correlation between clinical onset and levels of NPC1 protein in isolated skin fibroblasts
    • T. Yamamoto, H. Ninomiya, M. Matsumoto, Y. Ohta, E. Nanba, Y. Tsutsumi, K. Yamakawa, G. Millat, M.T. Vanier, P.G. Pentchev, and K. Ohno Genotype-phenotype relationship of Niemann-Pick disease type C: a possible correlation between clinical onset and levels of NPC1 protein in isolated skin fibroblasts J. Med. Genet. 37 2000 707 712
    • (2000) J. Med. Genet. , vol.37 , pp. 707-712
    • Yamamoto, T.1    Ninomiya, H.2    Matsumoto, M.3    Ohta, Y.4    Nanba, E.5    Tsutsumi, Y.6    Yamakawa, K.7    Millat, G.8    Vanier, M.T.9    Pentchev, P.G.10    Ohno, K.11


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