메뉴 건너뛰기




Volumn 6, Issue 6, 2010, Pages 424-432

Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALNEXIN; CHAPERONE; DANTROLENE; DILTIAZEM; GLUCOSYLCERAMIDASE; LYSOSOME ENZYME; RYANODINE RECEPTOR; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 2B; UNCLASSIFIED DRUG; VERAPAMIL; ATP2A2 PROTEIN, HUMAN; CALCIUM; CALCIUM CHANNEL BLOCKING AGENT; VASODILATOR AGENT;

EID: 77952501011     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.368     Document Type: Article
Times cited : (78)

References (50)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916-919 (2008).
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling, E. & Bukau, B. Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit. Rev. Biochem. Mol. Biol. 39, 261-277 (2004).
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 3
  • 4
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J. & Horwich, A. Molecular chaperones and protein quality control. Cell 125, 443-451 (2006).
    • (2006) Cell. , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 5
    • 64949099855 scopus 로고    scopus 로고
    • Protein homeostasis and aging: Taking care of proteins from the cradle to the grave
    • Morimoto, R. I. & Cuervo, A. M. Protein homeostasis and aging: taking care of proteins from the cradle to the grave. J. Gerontol. Ser. A Biol. Sci. Med. Sci. 64A, 167-170 (2009).
    • (2009) J. Gerontol. Ser. A Biol. Sci. Med. Sci. , vol.64 , pp. 167-170
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 6
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide, S. D., Anckar, J., Stevens, S. M., Sistonen, L. & Morimoto, R. I. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323, 1063-1066 (2009).
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 7
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
    • Dai, C., Whitesell, L., Rogers, A. B. & Lindquist, S. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 130, 1005-1018 (2007).
    • (2007) Cell. , vol.130 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 8
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D. & Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529 (2007).
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 9
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M. & Kaufman, R. J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789 (2005).
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 10
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R. & Morimoto, R. I. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311, 1471-1474 (2006).
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 11
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fbrosis
    • Wang, X. et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fbrosis. Cell 127, 803-815 (2006).
    • (2006) Cell. , vol.127 , pp. 803-815
    • Wang, X.1
  • 12
    • 40149095757 scopus 로고    scopus 로고
    • Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis
    • Mu, T. W., Fowler, D. M. & Kelly, J. W. Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis. PLoS Biol. 6, e26 (2008).
    • (2008) PLoS Biol. , vol.6
    • Mu, T.W.1    Fowler, D.M.2    Kelly, J.W.3
  • 13
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • Mu, T. W. et al. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134, 769-781 (2008).
    • (2008) Cell. , vol.134 , pp. 769-781
    • Mu, T.W.1
  • 14
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W. & Dillin, A. Opposing activities protect against age-onset proteotoxicity. Science 313, 1604-1610 (2006).
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 15
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley, J. F., Brignull, H. R., Weyers, J. J. & Morimoto, R. I. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 99, 10417-10422 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 16
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman, A. H. & van Meer, G. The cell biology of lysosomal storage disorders. Nat. Rev. Mol. Cell Biol. 5, 554-565 (2004).
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 17
    • 0037180511 scopus 로고    scopus 로고
    • Chemical chaperones increase the cellular activity of N370S beta-glucosidase: A therapeutic strategy for Gaucher disease
    • Sawkar, A. R. et al. Chemical chaperones increase the cellular activity of N370S beta-glucosidase: a therapeutic strategy for Gaucher disease. Proc. Natl. Acad. Sci. USA 99, 15428-15433 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15428-15433
    • Sawkar, A.R.1
  • 18
    • 33745293617 scopus 로고    scopus 로고
    • Therapeutic strategies to ameliorate lysosomal storage disorders-a focus on Gaucher disease
    • Sawkar, A. R., D'Haeze, W. & Kelly, J. W. Therapeutic strategies to ameliorate lysosomal storage disorders-a focus on Gaucher disease. Cell. Mol. Life Sci. 63, 1179-1192 (2006).
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1179-1192
    • Sawkar, A.R.1    D'Haeze, W.2    Kelly, J.W.3
  • 19
    • 23944477827 scopus 로고    scopus 로고
    • Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease
    • Schmitz, M., Alfalah, M., Aerts, J., Naim, H. Y. & Zimmer, K. P. Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease. Int. J. Biochem. Cell Biol. 37, 2310-2320 (2005).
    • (2005) Int. J. Biochem. Cell. Biol. , vol.37 , pp. 2310-2320
    • Schmitz, M.1    Alfalah, M.2    Aerts, J.3    Naim, H.Y.4    Zimmer, K.P.5
  • 20
    • 26444609722 scopus 로고    scopus 로고
    • ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity
    • Ron, I. & Horowitz, M. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum. Mol. Genet. 14, 2387-2398 (2005).
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2387-2398
    • Ron, I.1    Horowitz, M.2
  • 21
    • 4644224470 scopus 로고    scopus 로고
    • Correlation between enzyme activity and substrate storage in a cell culture model system for Gaucher disease
    • Schueler, U. H. et al. Correlation between enzyme activity and substrate storage in a cell culture model system for Gaucher disease. J. Inherit. Metab. Dis. 27, 649-658 (2004).
    • (2004) J. Inherit. Metab. Dis. , vol.27 , pp. 649-658
    • Schueler, U.H.1
  • 22
    • 0032798194 scopus 로고    scopus 로고
    • Intracellular transport of acid β-glucosidase and lysosome-associated membrane proteins is affected in Gaucher's disease (G202R mutation)
    • Zimmer, K.-P. et al. Intracellular transport of acid β-glucosidase and lysosome-associated membrane proteins is affected in Gaucher's disease (G202R mutation). J. Pathol. 188, 407-414 (1999).
    • (1999) J. Pathol. , vol.188 , pp. 407-414
    • Zimmer, K.-P.1
  • 23
    • 33845240108 scopus 로고    scopus 로고
    • Chemical chaperones and permissive temperatures alter the cellular localization of Gaucher disease associated glucocerebrosidase variants
    • Sawkar, A. R. et al. Chemical chaperones and permissive temperatures alter the cellular localization of Gaucher disease associated glucocerebrosidase variants. ACS Chem. Biol. 1, 235-251 (2006).
    • (2006) ACS Chem. Biol. , vol.1 , pp. 235-251
    • Sawkar, A.R.1
  • 24
    • 0036895451 scopus 로고    scopus 로고
    • Enzyme replacement and enhancement therapies: Lessons from lysosomal disorders
    • Desnick, R. J. & Schuchman, E. H. Enzyme replacement and enhancement therapies: Lessons from lysosomal disorders. Nat. Rev. Genet. 3, 954-966 (2002).
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 954-966
    • Desnick, R.J.1    Schuchman, E.H.2
  • 25
    • 0025727902 scopus 로고
    • Characterization of human glucocerebrosidase from different mutant alleles
    • Ohashi, T. et al. Characterization of human glucocerebrosidase from different mutant alleles. J. Biol. Chem. 266, 3661-3667 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 3661-3667
    • Ohashi, T.1
  • 26
    • 0033618336 scopus 로고    scopus 로고
    • Elevation of intracellular glucosylceramide levels results in an increase in endoplasmic reticulum density and in functional calcium stores in cultured neurons
    • Korkotian, E. et al. Elevation of intracellular glucosylceramide levels results in an increase in endoplasmic reticulum density and in functional calcium stores in cultured neurons. J. Biol. Chem. 274, 21673-21678 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21673-21678
    • Korkotian, E.1
  • 27
    • 0038607434 scopus 로고    scopus 로고
    • Glucosylceramide and glucosylsphingosine modulate calcium mobilization from brain microsomes via different mechanisms
    • Lloyd-Evans, E. et al. Glucosylceramide and glucosylsphingosine modulate calcium mobilization from brain microsomes via different mechanisms. J. Biol. Chem. 278, 23594-23599 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 23594-23599
    • Lloyd-Evans, E.1
  • 28
    • 11844278539 scopus 로고    scopus 로고
    • Enhanced calcium release in the acute neuronopathic form of Gaucher disease
    • Pelled, D. et al. Enhanced calcium release in the acute neuronopathic form of Gaucher disease. Neurobiol. Dis. 18, 83-88 (2005).
    • (2005) Neurobiol. Dis. , vol.18 , pp. 83-88
    • Pelled, D.1
  • 29
    • 0025040546 scopus 로고
    • Direct binding of verapamil to the ryanodine receptor channel of sarcoplasmic-reticulum
    • Valdivia, H. H., Valdivia, C., Ma, J. J. & Coronado, R. Direct binding of verapamil to the ryanodine receptor channel of sarcoplasmic- reticulum. Biophys. J. 58, 471-481 (1990).
    • (1990) Biophys. J. , vol.58 , pp. 471-481
    • Valdivia, H.H.1    Valdivia, C.2    Ma, J.J.3    Coronado, R.4
  • 30
    • 0025764306 scopus 로고
    • Characterization of high-affinity ryanodine-binding sites of rat liver endoplasmic-reticulum-differences between liver and skeletal-muscle
    • Shoshan-Barmatz, V., Pressley, T. A., Higham, S. & Kraus-Friedmann, N. Characterization of high-affinity ryanodine-binding sites of rat liver endoplasmic-reticulum-differences between liver and skeletal-muscle. Biochem. J. 276, 41-46 (1991).
    • (1991) Biochem. J. , vol.276 , pp. 41-46
    • Shoshan-Barmatz, V.1    Pressley, T.A.2    Higham, S.3    Kraus-Friedmann, N.4
  • 31
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk, R., Lehnart, S. E. & Marks, A. R. Modulation of the ryanodine receptor and intracellular calcium. Annu. Rev. Biochem. 76, 367-385 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3
  • 32
    • 0022529046 scopus 로고
    • Dantrolene-a review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in malignant hyperthermia, the neuroleptic malignant syndrome and an update of its use in muscle spasticity
    • Ward, A., Chaffman, M. O. & Sorkin, E. M. Dantrolene-a review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in malignant hyperthermia, the neuroleptic malignant syndrome and an update of its use in muscle spasticity. Drugs 32, 130-168 (1986).
    • (1986) Drugs , vol.32 , pp. 130-168
    • Ward, A.1    Chaffman, M.O.2    Sorkin, E.M.3
  • 33
    • 0028101231 scopus 로고
    • Effects of bipyridylium compounds on calcium-release from triadic vesicles isolated from rabbit skeletal-muscle
    • Kang, J. J., Hsu, K. S. & Linshiau, S. Y. Effects of bipyridylium compounds on calcium-release from triadic vesicles isolated from rabbit skeletal-muscle. Br. J. Pharmacol. 112, 1216-1222 (1994).
    • (1994) Br. J. Pharmacol. , vol.112 , pp. 1216-1222
    • Kang, J.J.1    Hsu, K.S.2    Linshiau, S.Y.3
  • 34
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signaling
    • Berridge, M. J. Inositol trisphosphate and calcium signaling. Nature 361, 315-325 (1993).
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 37
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32, 269-278 (2002).
    • (2002) Cell. Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Parker, J.M.R.2    Opas, M.3
  • 38
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J. D. et al. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644 (2001).
    • (2001) Mol. Cell. , vol.8 , pp. 633-644
    • Schrag, J.D.1
  • 39
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic-reticulum suggests a chaperone function for human integral membrane-protein IP90 (calnexin)
    • David, V., Hochstenbach, F., Rajagopalan, S. & Brenner, M. B. Interaction with newly synthesized and retained proteins in the endoplasmic-reticulum suggests a chaperone function for human integral membrane-protein IP90 (calnexin). J. Biol. Chem. 268, 9585-9592 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 9585-9592
    • David, V.1    Hochstenbach, F.2    Rajagopalan, S.3    Brenner, M.B.4
  • 40
    • 33646844964 scopus 로고    scopus 로고
    • 2+ binding site on GRP78 is differentially enhanced by ADP and ATP
    • 2+ binding site on GRP78 is differentially enhanced by ADP and ATP. J. Biol. Chem. 281, 8796-8805 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8796-8805
    • Lamb, H.K.1
  • 42
    • 0034647539 scopus 로고    scopus 로고
    • Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain
    • Wilson, C. M., Farmery, M. R. & Bulleid, N. J. Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain. J. Biol. Chem. 275, 21224-21232 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 21224-21232
    • Wilson, C.M.1    Farmery, M.R.2    Bulleid, N.J.3
  • 43
    • 0032479290 scopus 로고    scopus 로고
    • Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor
    • Keller, S. H., Lindstrom, J. & Taylor, P. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 273, 17064-17072 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 17064-17072
    • Keller, S.H.1    Lindstrom, J.2    Taylor, P.3
  • 44
    • 0034254433 scopus 로고    scopus 로고
    • Role of calnexin, calreticulin, and endoplasmic reticulum mannosidase I in apolipoprotein (a) intracellular targeting
    • Wang, J. & White, A. L. Role of calnexin, calreticulin, and endoplasmic reticulum mannosidase I in apolipoprotein (a) intracellular targeting. Biochemistry 39, 8993-9000 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8993-9000
    • Wang, J.1    White, A.L.2
  • 45
    • 33750340637 scopus 로고    scopus 로고
    • Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum
    • Brockmeier, A. & Williams, D. B. Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum. Biochemistry 45, 12906-12916 (2006).
    • (2006) Biochemistry , vol.45 , pp. 12906-12916
    • Brockmeier, A.1    Williams, D.B.2
  • 46
    • 25844474620 scopus 로고    scopus 로고
    • Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein
    • Tammavongsa, V., Mancino, L. & Raghavan, M. Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein. J. Biol. Chem. 280, 33497-33505 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 33497-33505
    • Tammavongsa, V.1    Mancino, L.2    Raghavan, M.3
  • 47
    • 0028205240 scopus 로고
    • Human, mouse and rat calreticulin cDNA cloning-identification of potential calcium-binding motifs and gene localization to human-chromosome-5
    • Tjoelker, L. W. et al. Human, mouse and rat calreticulin cDNA cloning-identification of potential calcium-binding motifs and gene localization to human-chromosome-5. Biochemistry 33, 3229-3236 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3229-3236
    • Tjoelker, L.W.1
  • 48
    • 0034282386 scopus 로고    scopus 로고
    • The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment
    • Corbett, E. F. et al. The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment. J. Biol. Chem. 275, 27177-27185 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27177-27185
    • Corbett, E.F.1
  • 49


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.