메뉴 건너뛰기




Volumn 15, Issue 11, 2016, Pages 3348-3360

The primary effect on the proteome of ARID1A-mutated ovarian clear cell carcinoma is downregulation of the mevalonate pathway at the post-transcriptional level

Author keywords

[No Author keywords available]

Indexed keywords

ARID1A PROTEIN; CHOLESTEROL; GLYCOGEN; ISOPRENOID; MEVALONIC ACID; PROTEOME; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; ARID1A PROTEIN, HUMAN; NUCLEAR PROTEIN;

EID: 84995426673     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M116.062539     Document Type: Article
Times cited : (23)

References (54)
  • 2
    • 41349083323 scopus 로고    scopus 로고
    • Mechanisms of chemoresistance and poor prognosis in ovarian clear cell carcinoma
    • Itamochi, H., Kigawa, J., and Terakawa, N. (2008) Mechanisms of chemoresistance and poor prognosis in ovarian clear cell carcinoma. Cancer Sci. 99, 653-658
    • (2008) Cancer Sci. , vol.99 , pp. 653-658
    • Itamochi, H.1    Kigawa, J.2    Terakawa, N.3
  • 3
    • 33751248513 scopus 로고    scopus 로고
    • Treatment issues in clear cell carcinoma of the ovary: A different entity?
    • Pectasides, D., Pectasides, E., Psyrri, A., and Economopoulos, T. (2006) Treatment issues in clear cell carcinoma of the ovary: a different entity? Oncologist 11, 1089-1094
    • (2006) Oncologist , vol.11 , pp. 1089-1094
    • Pectasides, D.1    Pectasides, E.2    Psyrri, A.3    Economopoulos, T.4
  • 4
    • 41349100528 scopus 로고    scopus 로고
    • Pathogenesis of ovarian cancer: Lessons from morphology and molecular biology and their clinical implications
    • Kurman, R. J., and Shih Ie, M. (2008) Pathogenesis of ovarian cancer: lessons from morphology and molecular biology and their clinical implications. Int. J. Gynecol. Pathol. 27, 151-160
    • (2008) Int. J. Gynecol. Pathol. , vol.27 , pp. 151-160
    • Kurman, R.J.1    Shih Ie, M.2
  • 5
    • 77950087106 scopus 로고    scopus 로고
    • Identification of an ovarian clear cell carcinoma gene signature that reflects inherent disease biology and the carcinogenic processes
    • Yamaguchi, K., Mandai, M., Oura, T., Matsumura, N., Hamanishi, J., Baba, T., Matsui, S., Murphy, S. K., and Konishi, I. (2010) Identification of an ovarian clear cell carcinoma gene signature that reflects inherent disease biology and the carcinogenic processes. Oncogene 29, 1741-1752
    • (2010) Oncogene , vol.29 , pp. 1741-1752
    • Yamaguchi, K.1    Mandai, M.2    Oura, T.3    Matsumura, N.4    Hamanishi, J.5    Baba, T.6    Matsui, S.7    Murphy, S.K.8    Konishi, I.9
  • 11
    • 84908693041 scopus 로고    scopus 로고
    • Vulnerabilities of mutant SWI/SNF complexes in cancer
    • Helming, K. C., Wang, X., and Roberts, C. W. (2014) Vulnerabilities of mutant SWI/SNF complexes in cancer. Cancer Cell. 26, 309-317
    • (2014) Cancer Cell. , vol.26 , pp. 309-317
    • Helming, K.C.1    Wang, X.2    Roberts, C.W.3
  • 12
    • 85041801996 scopus 로고    scopus 로고
    • Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic insights gained from human genomics
    • Kadoch, C., and Crabtree, G. R. (2015) Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic insights gained from human genomics. Sci. Adv. 1, e1500447
    • (2015) Sci. Adv. , vol.1 , pp. e1500447
    • Kadoch, C.1    Crabtree, G.R.2
  • 14
    • 13744250058 scopus 로고    scopus 로고
    • DNA-binding properties of ARID family proteins
    • Patsialou, A., Wilsker, D., and Moran, E. (2005) DNA-binding properties of ARID family proteins. Nucleic Acids Res. 33, 66-80
    • (2005) Nucleic Acids Res. , vol.33 , pp. 66-80
    • Patsialou, A.1    Wilsker, D.2    Moran, E.3
  • 15
    • 0034002033 scopus 로고    scopus 로고
    • The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity
    • Dallas, P. B., Pacchione, S., Wilsker, D., Bowrin, V., Kobayashi, R., and Moran, E. (2000) The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity. Mol. Cell. Biol. 20, 3137-3146
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3137-3146
    • Dallas, P.B.1    Pacchione, S.2    Wilsker, D.3    Bowrin, V.4    Kobayashi, R.5    Moran, E.6
  • 16
    • 0034461148 scopus 로고    scopus 로고
    • A specificity and targeting subunit of a human SWI/SNF family-related chromatin-remodeling complex
    • Nie, Z., Xue, Y., Yang, D., Zhou, S., Deroo, B. J., Archer, T. K., and Wang, W. (2000) A specificity and targeting subunit of a human SWI/SNF family-related chromatin-remodeling complex. Mol. Cell. Biol. 20, 8879-8888
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8879-8888
    • Nie, Z.1    Xue, Y.2    Yang, D.3    Zhou, S.4    Deroo, B.J.5    Archer, T.K.6    Wang, W.7
  • 17
    • 80155131218 scopus 로고    scopus 로고
    • ARID1A, a factor that promotes formation of SWI/SNF-mediated chromatin remodeling, is a tumor suppressor in gynecologic cancers
    • Guan, B., Wang, T. L., and Shih Ie, M. (2011) ARID1A, a factor that promotes formation of SWI/SNF-mediated chromatin remodeling, is a tumor suppressor in gynecologic cancers. Cancer Res. 71, 6718-6727
    • (2011) Cancer Res. , vol.71 , pp. 6718-6727
    • Guan, B.1    Wang, T.L.2    Shih Ie, M.3
  • 19
    • 84953240912 scopus 로고    scopus 로고
    • Genome-Wide Transcriptional Regulation Mediated by Biochemically Distinct SWI/SNF Complexes
    • Raab, J. R., Resnick, S., and Magnuson, T. (2015) Genome-Wide Transcriptional Regulation Mediated by Biochemically Distinct SWI/SNF Complexes. PLoS Genet. 11, e1005748
    • (2015) PLoS Genet. , vol.11 , pp. e1005748
    • Raab, J.R.1    Resnick, S.2    Magnuson, T.3
  • 21
    • 84955210237 scopus 로고    scopus 로고
    • Arid1a inactivation in an Apc-and Pten-defective mouse ovarian cancer model enhances epithelial differ-entiation and prolongs survival
    • Zhai, Y., Kuick, R., Tipton, C., Wu, R., Sessine, M., Wang, Z., Baker, S. J., Fearon, E. R., and Cho, K. R. (2016) Arid1a inactivation in an Apc-and Pten-defective mouse ovarian cancer model enhances epithelial differ-entiation and prolongs survival. J. Pathol. 238, 21-30
    • (2016) J. Pathol. , vol.238 , pp. 21-30
    • Zhai, Y.1    Kuick, R.2    Tipton, C.3    Wu, R.4    Sessine, M.5    Wang, Z.6    Baker, S.J.7    Fearon, E.R.8    Cho, K.R.9
  • 22
    • 84858439862 scopus 로고    scopus 로고
    • Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
    • Vogel, C., and Marcotte, E. M. (2012) Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat. Rev. Genet. 13, 227-232
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 227-232
    • Vogel, C.1    Marcotte, E.M.2
  • 23
    • 84895086287 scopus 로고    scopus 로고
    • A functional proteogenomic analysis of endometrioid and clear cell carcinomas using reverse phase protein array and mutation analysis: Protein expression is histotype-specific and loss of ARID1A/BAF250a is associated with AKT phosphorylation
    • Wiegand, K. C., Hennessy, B. T., Leung, S., Wang, Y., Ju, Z., McGahren, M., Kalloger, S. E., Finlayson, S., Stemke-Hale, K., Lu, Y., Zhang, F., Anglesio, M. S., Gilks, B., Mills, G. B., Huntsman, D. G., and Carey, M. S. (2014) A functional proteogenomic analysis of endometrioid and clear cell carcinomas using reverse phase protein array and mutation analysis: protein expression is histotype-specific and loss of ARID1A/BAF250a is associated with AKT phosphorylation. BMC Cancer 14, 120
    • (2014) BMC Cancer , vol.14 , pp. 120
    • Wiegand, K.C.1    Hennessy, B.T.2    Leung, S.3    Wang, Y.4    Ju, Z.5    McGahren, M.6    Kalloger, S.E.7    Finlayson, S.8    Stemke-Hale, K.9    Lu, Y.10    Zhang, F.11    Anglesio, M.S.12    Gilks, B.13    Mills, G.B.14    Huntsman, D.G.15    Carey, M.S.16
  • 24
    • 79952437118 scopus 로고    scopus 로고
    • Systematic discovery of ectopic pregnancy serum biomarkers using 3-D protein profiling coupled with label-free quantitation
    • Beer, L. A., Tang, H. Y., Sriswasdi, S., Barnhart, K. T., and Speicher, D. W. (2011) Systematic discovery of ectopic pregnancy serum biomarkers using 3-D protein profiling coupled with label-free quantitation. J. Pro-teome Res. 10, 1126-1138
    • (2011) J. Pro-teome Res. , vol.10 , pp. 1126-1138
    • Beer, L.A.1    Tang, H.Y.2    Sriswasdi, S.3    Barnhart, K.T.4    Speicher, D.W.5
  • 25
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 27
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox, J., Hein, M. Y., Luber, C. A., Paron, I., Nagaraj, N., and Mann, M. (2014) Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol. Cell. Proteomics 13, 2513-2526
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2513-2526
    • Cox, J.1    Hein, M.Y.2    Luber, C.A.3    Paron, I.4    Nagaraj, N.5    Mann, M.6
  • 29
    • 84963706086 scopus 로고    scopus 로고
    • Accounting for the Multiple Natures of Missing Values in Label-Free Quantitative Proteomics Data Sets to Compare Imputation Strategies
    • Lazar, C., Gatto, L., Ferro, M., Bruley, C., and Burger, T. (2016) Accounting for the Multiple Natures of Missing Values in Label-Free Quantitative Proteomics Data Sets to Compare Imputation Strategies. J. Proteome Res. 15, 1116-1125
    • (2016) J. Proteome Res. , vol.15 , pp. 1116-1125
    • Lazar, C.1    Gatto, L.2    Ferro, M.3    Bruley, C.4    Burger, T.5
  • 32
    • 84857938446 scopus 로고    scopus 로고
    • Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins
    • Geiger, T., Wehner, A., Schaab, C., Cox, J., and Mann, M. (2012) Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins. Mol. Cell. Proteomics 11, M111 014050
    • (2012) Mol. Cell. Proteomics , vol.11
    • Geiger, T.1    Wehner, A.2    Schaab, C.3    Cox, J.4    Mann, M.5
  • 34
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., and Brown, M. S. (1990) Regulation of the mevalonate pathway. Nature 343, 425-430
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 35
    • 34249685010 scopus 로고    scopus 로고
    • Mevalonate pathway: A review of clinical and therapeutical implications
    • Buhaescu, I., and Izzedine, H. (2007) Mevalonate pathway: a review of clinical and therapeutical implications. Clin. Biochem. 40, 575-584
    • (2007) Clin. Biochem. , vol.40 , pp. 575-584
    • Buhaescu, I.1    Izzedine, H.2
  • 36
    • 58149488988 scopus 로고    scopus 로고
    • The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development
    • Morrison, D. K. (2009) The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development. Trends Cell Biol. 19, 16-23
    • (2009) Trends Cell Biol. , vol.19 , pp. 16-23
    • Morrison, D.K.1
  • 38
    • 0028900265 scopus 로고
    • Establishment and characterization of two human ovarian clear cell adenocarcinoma lines from metastatic lesions with different properties
    • Gorai, I., Nakazawa, T., Miyagi, E., Hirahara, F., Nagashima, Y., and Minaguchi, H. (1995) Establishment and characterization of two human ovarian clear cell adenocarcinoma lines from metastatic lesions with different properties. Gynecol. Oncol. 57, 33-46
    • (1995) Gynecol. Oncol. , vol.57 , pp. 33-46
    • Gorai, I.1    Nakazawa, T.2    Miyagi, E.3    Hirahara, F.4    Nagashima, Y.5    Minaguchi, H.6
  • 39
    • 80054866000 scopus 로고    scopus 로고
    • Targeting protein prenylation for cancer therapy
    • Berndt, N., Hamilton, A. D., and Sebti, S. M. (2011) Targeting protein prenylation for cancer therapy. Nat. Rev. Cancer 11, 775-791
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 775-791
    • Berndt, N.1    Hamilton, A.D.2    Sebti, S.M.3
  • 41
    • 84863317657 scopus 로고    scopus 로고
    • Novel aspects of mevalonate pathway inhibitors as antitumor agents
    • Thurnher, M., Nussbaumer, O., and Gruenbacher, G. (2012) Novel aspects of mevalonate pathway inhibitors as antitumor agents. Clin. Cancer Res. 18, 3524-3531
    • (2012) Clin. Cancer Res. , vol.18 , pp. 3524-3531
    • Thurnher, M.1    Nussbaumer, O.2    Gruenbacher, G.3
  • 43
    • 84920688856 scopus 로고    scopus 로고
    • Statin use and risk for ovarian cancer: A Danish nationwide case-control study
    • Baandrup, L., Dehlendorff, C., Friis, S., Olsen, J. H., and Kjaer, S. K. (2015) Statin use and risk for ovarian cancer: a Danish nationwide case-control study. Br. J. Cancer 112, 157-161
    • (2015) Br. J. Cancer , vol.112 , pp. 157-161
    • Baandrup, L.1    Dehlendorff, C.2    Friis, S.3    Olsen, J.H.4    Kjaer, S.K.5
  • 45
    • 84922931260 scopus 로고    scopus 로고
    • Global quantitative proteomics reveals novel factors in the ecdysone signaling pathway in Drosophila melanogaster
    • Sap, K. A., Bezstarosti, K., Dekkers, D. H., van den Hout, M., van Ijcken, W., Rijkers, E., and Demmers, J. A. (2015) Global quantitative proteomics reveals novel factors in the ecdysone signaling pathway in Drosophila melanogaster. Proteomics 15, 725-738
    • (2015) Proteomics , vol.15 , pp. 725-738
    • Sap, K.A.1    Bezstarosti, K.2    Dekkers, D.H.3    Van Den Hout, M.4    Van Ijcken, W.5    Rijkers, E.6    Demmers, J.A.7
  • 46
    • 79961118496 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase in mammals and yeast
    • Burg, J. S., and Espenshade, P. J. (2011) Regulation of HMG-CoA reductase in mammals and yeast. Prog. Lipid Res. 50, 403-410
    • (2011) Prog. Lipid Res. , vol.50 , pp. 403-410
    • Burg, J.S.1    Espenshade, P.J.2
  • 47
    • 77952860536 scopus 로고    scopus 로고
    • Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase
    • Jo, Y., and Debose-Boyd, R. A. (2010) Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase. Crit. Rev. Biochem. Mol. Biol. 45, 185-198
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 185-198
    • Jo, Y.1    Debose-Boyd, R.A.2
  • 48
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Hampton, R. Y., and Bhakta, H. (1997) Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. U.S.A. 94, 12944-12948
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 49
    • 0034680918 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Ravid, T., Doolman, R., Avner, R., Harats, D., and Roitelman, J. (2000) The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 275, 35840-35847
    • (2000) J. Biol. Chem. , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 50
    • 79952174597 scopus 로고    scopus 로고
    • Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase
    • Gill, S., Stevenson, J., Kristiana, I., and Brown, A. J. (2011) Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab. 13, 260-273
    • (2011) Cell Metab. , vol.13 , pp. 260-273
    • Gill, S.1    Stevenson, J.2    Kristiana, I.3    Brown, A.J.4
  • 52
    • 84879588228 scopus 로고    scopus 로고
    • Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)
    • Sharpe, L. J., and Brown, A. J. (2013) Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR). J. Biol. Chem. 288, 18707-18715
    • (2013) J. Biol. Chem. , vol.288 , pp. 18707-18715
    • Sharpe, L.J.1    Brown, A.J.2
  • 53
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • Ciechanover, A. (2005) Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat. Rev. Mol. Cell Biol. 6, 79-87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.