메뉴 건너뛰기




Volumn 112, Issue 4, 2015, Pages 1137-1142

Mutant glucocerebrosidase in Gaucher disease recruits Hsp27 to the Hsp90 chaperone complex for proteasomal degradation

Author keywords

Gaucher disease; Heat shock protein; Hsp27; Hsp90; Molecular chaperone

Indexed keywords

CHAPERONE; GLUCOSYLCERAMIDASE; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 90; PEPTIDE; PROTEASOME; ATP DEPENDENT 26S PROTEASE; CDC37 PROTEIN, HUMAN; CELL CYCLE PROTEIN; CHAPERONIN; HOMEODOMAIN PROTEIN; HOP PROTEIN, HUMAN; HSPB1 PROTEIN, HUMAN; TUMOR SUPPRESSOR PROTEIN;

EID: 84921717897     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1424288112     Document Type: Article
Times cited : (18)

References (26)
  • 1
    • 0028054985 scopus 로고
    • Mutations causing Gaucher disease
    • Horowitz M, Zimran A (1994) Mutations causing Gaucher disease. Hum Mutat 3(1):1-11.
    • (1994) Hum Mutat , vol.3 , Issue.1 , pp. 1-11
    • Horowitz, M.1    Zimran, A.2
  • 2
    • 42949118684 scopus 로고    scopus 로고
    • Gaucher disease: Mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA)
    • Hruska KS, LaMarca ME, Scott CR, Sidransky E (2008) Gaucher disease: mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA). Hum Mutat 29(5):567-583.
    • (2008) Hum Mutat , vol.29 , Issue.5 , pp. 567-583
    • Hruska, K.S.1    LaMarca, M.E.2    Scott, C.R.3    Sidransky, E.4
  • 3
    • 84862965909 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher disease
    • Lu J, et al. (2011) Histone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher disease. Proc Natl Acad Sci USA 108(52):21200-21205.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.52 , pp. 21200-21205
    • Lu, J.1
  • 4
    • 78650750313 scopus 로고    scopus 로고
    • Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl
    • Lu J, et al. (2010) Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl. Proc Natl Acad Sci USA 107(50):21665-21670.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.50 , pp. 21665-21670
    • Lu, J.1
  • 5
    • 84862585334 scopus 로고    scopus 로고
    • Pharmacological chaperones facilitate the post-ER transport of recombinant N370Smutant β-glucocerebrosidase in plant cells: Evidence that N370S is a folding mutant
    • Babajani G, Tropak MB, Mahuran DJ, Kermode AR (2012) Pharmacological chaperones facilitate the post-ER transport of recombinant N370Smutant β-glucocerebrosidase in plant cells: evidence that N370S is a folding mutant. Mol Genet Metab 106(3):323-329.
    • (2012) Mol Genet Metab , vol.106 , Issue.3 , pp. 323-329
    • Babajani, G.1    Tropak, M.B.2    Mahuran, D.J.3    Kermode, A.R.4
  • 6
    • 26444609722 scopus 로고    scopus 로고
    • ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity
    • Ron I, Horowitz M (2005) ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum Mol Genet 14(16):2387-2398.
    • (2005) Hum Mol Genet , vol.14 , Issue.16 , pp. 2387-2398
    • Ron, I.1    Horowitz, M.2
  • 7
    • 77956537090 scopus 로고    scopus 로고
    • Interaction between parkin and mutant glucocerebrosidase variants: A possible link between Parkinson disease and Gaucher disease
    • Ron I, Rapaport D, Horowitz M (2010) Interaction between parkin and mutant glucocerebrosidase variants: a possible link between Parkinson disease and Gaucher disease. Hum Mol Genet 19(19):3771-3781.
    • (2010) Hum Mol Genet , vol.19 , Issue.19 , pp. 3771-3781
    • Ron, I.1    Rapaport, D.2    Horowitz, M.3
  • 8
    • 84875249831 scopus 로고    scopus 로고
    • ITCH regulates degradation of mutant glucocerebrosidase: Implications to Gaucher disease
    • Maor G, Filocamo M, Horowitz M (2013) ITCH regulates degradation of mutant glucocerebrosidase: implications to Gaucher disease. Hum Mol Genet 22(7):1316-1327.
    • (2013) Hum Mol Genet , vol.22 , Issue.7 , pp. 1316-1327
    • Maor, G.1    Filocamo, M.2    Horowitz, M.3
  • 10
    • 0043133793 scopus 로고    scopus 로고
    • HSP27 is a ubiquitin-binding protein involved in I-kappa-Balpha proteasomal degradation
    • Parcellier A, et al. (2003) HSP27 is a ubiquitin-binding protein involved in I-kappa-Balpha proteasomal degradation. Mol Cell Biol 23(16):5790-5802.
    • (2003) Mol Cell Biol , vol.23 , Issue.16 , pp. 5790-5802
    • Parcellier, A.1
  • 11
    • 33845623275 scopus 로고    scopus 로고
    • HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells
    • Parcellier A, et al. (2006) HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells. FASEB J 20(8):1179-1181.
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1179-1181
    • Parcellier, A.1
  • 12
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415(6868):180-183.
    • (2002) Nature , vol.415 , Issue.6868 , pp. 180-183
    • Ho, Y.1
  • 13
    • 84872541302 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones
    • Yang C, et al. (2013) Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones. Proc Natl Acad Sci USA 110(3):966-971.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.3 , pp. 966-971
    • Yang, C.1
  • 14
    • 84891929380 scopus 로고    scopus 로고
    • Celastrol increases glucocerebrosidase activity in Gaucher disease by modulating molecular chaperones
    • Yang C, et al. (2014) Celastrol increases glucocerebrosidase activity in Gaucher disease by modulating molecular chaperones. Proc Natl Acad Sci USA 111(1):249-254.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.1 , pp. 249-254
    • Yang, C.1
  • 15
    • 84920439211 scopus 로고    scopus 로고
    • ERdj3 is an endoplasmic reticulum degradation factor for mutant glucocerebrosidase variants linked to Gaucher's disease
    • Tan YL, et al. (2014) ERdj3 is an endoplasmic reticulum degradation factor for mutant glucocerebrosidase variants linked to Gaucher's disease. Chem Biol 21(8):967-976.
    • (2014) Chem Biol , vol.21 , Issue.8 , pp. 967-976
    • Tan, Y.L.1
  • 17
    • 84891820046 scopus 로고    scopus 로고
    • The Hsp90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin increases cisplatin antitumor activity by inducing p53-mediated apoptosis in head and neck cancer
    • Roh JL, Kim EH, Park HB, Park JY (2013) The Hsp90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin increases cisplatin antitumor activity by inducing p53-mediated apoptosis in head and neck cancer. Cell Death Dis 4:e956.
    • (2013) Cell Death Dis , vol.4 , pp. e956
    • Roh, J.L.1    Kim, E.H.2    Park, H.B.3    Park, J.Y.4
  • 18
    • 84890215177 scopus 로고    scopus 로고
    • Mode of cell death induced by the HSP90 inhibitor 17-AAG (tanespimycin) is dependent on the expression of pro-apoptotic BAX
    • Powers MV, et al. (2013) Mode of cell death induced by the HSP90 inhibitor 17-AAG (tanespimycin) is dependent on the expression of pro-apoptotic BAX. Oncotarget 4(11):1963-1975.
    • (2013) Oncotarget , vol.4 , Issue.11 , pp. 1963-1975
    • Powers, M.V.1
  • 19
    • 84903788086 scopus 로고    scopus 로고
    • Parkin-mediated ubiquitination of mutant glucocerebrosidase leads to competition with its substrates PARIS and ARTS
    • Bendikov-Bar I, Rapaport D, Larisch S, Horowitz M (2014) Parkin-mediated ubiquitination of mutant glucocerebrosidase leads to competition with its substrates PARIS and ARTS. Orphanet J Rare Dis 9:86.
    • (2014) Orphanet J Rare Dis , vol.9 , pp. 86
    • Bendikov-Bar, I.1    Rapaport, D.2    Larisch, S.3    Horowitz, M.4
  • 20
    • 84886303330 scopus 로고    scopus 로고
    • Treatment of Niemann-pick type C disease by histone deacetylase inhibitors
    • Helquist P, Maxfield FR, Wiech NL, Wiest O (2013) Treatment of Niemann-pick type C disease by histone deacetylase inhibitors. Neurotherapeutics 10(4):688-697.
    • (2013) Neurotherapeutics , vol.10 , Issue.4 , pp. 688-697
    • Helquist, P.1    Maxfield, F.R.2    Wiech, N.L.3    Wiest, O.4
  • 21
    • 84868298330 scopus 로고    scopus 로고
    • Missense mutations in the human SDHB gene increase protein degradation without altering intrinsic enzymatic function
    • Yang C, et al. (2012) Missense mutations in the human SDHB gene increase protein degradation without altering intrinsic enzymatic function. FASEB J 26(11):4506-4516.
    • (2012) FASEB J , vol.26 , Issue.11 , pp. 4506-4516
    • Yang, C.1
  • 22
    • 79953217085 scopus 로고    scopus 로고
    • Missense mutations in the NF2 gene result in the quantitative loss of merlin protein and minimally affect protein intrinsic function
    • Yang C, et al. (2011) Missense mutations in the NF2 gene result in the quantitative loss of merlin protein and minimally affect protein intrinsic function. Proc Natl Acad Sci USA 108(12):4980-4985.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.12 , pp. 4980-4985
    • Yang, C.1
  • 23
    • 84866278220 scopus 로고    scopus 로고
    • Gaucher disease paradigm: From ERAD to comorbidity
    • Bendikov-Bar I, Horowitz M (2012) Gaucher disease paradigm: from ERAD to comorbidity. Hum Mutat 33(10):1398-1407.
    • (2012) Hum Mutat , vol.33 , Issue.10 , pp. 1398-1407
    • Bendikov-Bar, I.1    Horowitz, M.2
  • 24
    • 78650805237 scopus 로고    scopus 로고
    • Characterization of the ERAD process of the L444P mutant glucocerebrosidase variant
    • Bendikov-Bar I, Ron I, Filocamo M, HorowitzM(2011) Characterization of the ERAD process of the L444P mutant glucocerebrosidase variant. Blood Cells Mol Dis 46(1):4-10.
    • (2011) Blood Cells Mol Dis , vol.46 , Issue.1 , pp. 4-10
    • Bendikov-Bar, I.1    Ron, I.2    Filocamo, M.3    Horowitz, M.4
  • 25
    • 79953798740 scopus 로고    scopus 로고
    • Chaperone Hsp27 modulates AUF1 proteolysis and AUrich element-mediated mRNA degradation
    • Knapinska AM, et al. (2011) Chaperone Hsp27 modulates AUF1 proteolysis and AUrich element-mediated mRNA degradation. Mol Cell Biol 31(7):1419-1431.
    • (2011) Mol Cell Biol , vol.31 , Issue.7 , pp. 1419-1431
    • Knapinska, A.M.1
  • 26
    • 84860792637 scopus 로고    scopus 로고
    • β-Catenin signaling initiates the activation of astrocytes and its dysregulation contributes to the pathogenesis of astrocytomas
    • Yang C, et al. (2012) β-Catenin signaling initiates the activation of astrocytes and its dysregulation contributes to the pathogenesis of astrocytomas. Proc Natl Acad Sci USA 109(18):6963-6968.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.18 , pp. 6963-6968
    • Yang, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.