메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

A novel mechanism of post-translational modulation of HMGA functions by the histone chaperone nucleophosmin

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DNA; HIGH MOBILITY GROUP A PROTEIN; IGFBP1 PROTEIN, HUMAN; INSULIN RECEPTOR; NUCLEAR PROTEIN; NUCLEOPHOSMIN; PROTEIN BINDING; SMALL INTERFERING RNA; SOMATOMEDIN BINDING PROTEIN 1;

EID: 84923641991     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep08552     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 4444288119 scopus 로고    scopus 로고
    • Nuclear phosphoproteins HMGA and their relationship with chromatin structure and cancer
    • Sgarra, R. et al. Nuclear phosphoproteins HMGA and their relationship with chromatin structure and cancer. FEBS Lett. 574, 1-8 (2004).
    • (2004) FEBS Lett. , vol.574 , pp. 1-8
    • Sgarra, R.1
  • 2
    • 0037385239 scopus 로고    scopus 로고
    • A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription
    • Foti, D., Iuliano, R., Chiefari, E. & Brunetti, A. A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription. Mol. Cell. Biol. 23, 2720-2732 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2720-2732
    • Foti, D.1    Iuliano, R.2    Chiefari, E.3    Brunetti, A.4
  • 3
    • 22544482628 scopus 로고    scopus 로고
    • Lack of the architectural factor HMGA1 causes insulin resistance and diabetes in humans and mice
    • Foti, D. et al. Lack of the architectural factor HMGA1 causes insulin resistance and diabetes in humans and mice. Nat. Med. 11, 765-773 (2005).
    • (2005) Nat. Med. , vol.11 , pp. 765-773
    • Foti, D.1
  • 4
    • 84859735682 scopus 로고    scopus 로고
    • HMGA1 is a novel downstream nuclear target of the insulin receptor signaling pathway
    • Chiefari, E. et al. HMGA1 is a novel downstream nuclear target of the insulin receptor signaling pathway. Sci Rep. 2, 251; DOI:10.1038/srep00251 (2012).
    • (2012) Sci Rep. , vol.2 , pp. 251
    • Chiefari, E.1
  • 5
    • 0029617947 scopus 로고
    • Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome
    • Thanos, D. & Maniatis, T. Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome. Cell 83, 1091-1100 (1995).
    • (1995) Cell , vol.83 , pp. 1091-1100
    • Thanos, D.1    Maniatis, T.2
  • 6
    • 0033152497 scopus 로고    scopus 로고
    • The role of HMG I(Y) in the assembly and function of the IFN-beta enhanceosome
    • Yie, J., Merika, M., Munshi, N., Chen, G. & Thanos, D. The role of HMG I(Y) in the assembly and function of the IFN-beta enhanceosome. EMBO J. 18, 3074-3089 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3074-3089
    • Yie, J.1    Merika, M.2    Munshi, N.3    Chen, G.4    Thanos, D.5
  • 7
    • 0035164289 scopus 로고    scopus 로고
    • Architectural transcription factor HMGI(Y) promotes tumor progression and mesenchymal transition of human epithelial cells
    • Reeves, R., Edberg, D. D. & Li, Y. Architectural transcription factor HMGI(Y) promotes tumor progression and mesenchymal transition of human epithelial cells. Mol. Cell. Biol. 21, 575-594 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 575-594
    • Reeves, R.1    Edberg, D.D.2    Li, Y.3
  • 8
    • 84877071501 scopus 로고    scopus 로고
    • HMGA1: A master regulator of tumor progression in triple-negative breast cancer cells
    • Shah, S. N. et al. HMGA1: a master regulator of tumor progression in triple-negative breast cancer cells. Plos One 8, e63419 (2012).
    • (2012) Plos One , vol.8 , pp. e63419
    • Shah, S.N.1
  • 9
    • 84884313879 scopus 로고    scopus 로고
    • HMGA1 promotes metastatic processes in basal-like breast cancer regulating EMT and stemness
    • Pegoraro, S. et al. HMGA1 promotes metastatic processes in basal-like breast cancer regulating EMT and stemness. Oncotarget 4, 1293-1308 (2013).
    • (2013) Oncotarget , vol.4 , pp. 1293-1308
    • Pegoraro, S.1
  • 10
    • 33746034613 scopus 로고    scopus 로고
    • Transforming growth factor-beta employs HMGA2 to elicit epithelial-mesenchymal transition
    • Thuault, S. et al. Transforming growth factor-beta employs HMGA2 to elicit epithelial-mesenchymal transition. J. Cell Biol. 174, 175-183 (2006).
    • (2006) J. Cell Biol. , vol.174 , pp. 175-183
    • Thuault, S.1
  • 11
    • 34250330247 scopus 로고    scopus 로고
    • Transcriptional control of the human high mobility group A1 gene: Basal and oncogenic Ras-regulated expression
    • Cleynen, I. et al. Transcriptional control of the human high mobility group A1 gene: basal and oncogenic Ras-regulated expression. Cancer Res. 67, 4620-4629 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 4620-4629
    • Cleynen, I.1
  • 12
    • 73549090376 scopus 로고    scopus 로고
    • HMGA1 is induced by Wnt/beta-catenin pathway and maintains cell proliferation in gastric cancer
    • Akaboshi, S. et al. HMGA1 is induced by Wnt/beta-catenin pathway and maintains cell proliferation in gastric cancer. Am. J. Pathol. 175, 1675-1685 (2009).
    • (2009) Am. J. Pathol. , vol.175 , pp. 1675-1685
    • Akaboshi, S.1
  • 13
    • 34247565615 scopus 로고    scopus 로고
    • The tumor suppressor microRNA let-7 represses the HMGA2 oncogene
    • Lee, Y. S. & Dutta, A. The tumor suppressor microRNA let-7 represses the HMGA2 oncogene. Genes Dev. 21, 1025-1030 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1025-1030
    • Lee, Y.S.1    Dutta, A.2
  • 14
    • 78651359790 scopus 로고    scopus 로고
    • Histone deacetylase regulates high mobility group A2-targeting microRNAs in human cord blood-derived multipotent stem cell aging
    • Lee, S. et al. Histone deacetylase regulates high mobility group A2-targeting microRNAs in human cord blood-derived multipotent stem cell aging. Cell. Mol. Life Sci. 68, 325-336 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 325-336
    • Lee, S.1
  • 15
    • 84880699142 scopus 로고    scopus 로고
    • miR-26a inhibits proliferation and motility in bladder cancer by targeting HMGA1
    • Lin, Y. et al. miR-26a inhibits proliferation and motility in bladder cancer by targeting HMGA1. FEBS Lett. 587, 2467-2473 (2013).
    • (2013) FEBS Lett. , vol.587 , pp. 2467-2473
    • Lin, Y.1
  • 16
    • 84899519555 scopus 로고    scopus 로고
    • MicroRNA-26a acts as a tumor suppressor inhibiting gallbladder cancer cell proliferation by directly targeting HMGA2
    • Zhou, H. et al. MicroRNA-26a acts as a tumor suppressor inhibiting gallbladder cancer cell proliferation by directly targeting HMGA2. Int. J. Oncol. 44, 2050-2058 (2014).
    • (2014) Int. J. Oncol. , vol.44 , pp. 2050-2058
    • Zhou, H.1
  • 17
    • 84856793694 scopus 로고    scopus 로고
    • Pseudogene-mediated posttranscriptional silencing of HMGA1 can result in insulin resistance and type 2 diabetes
    • Chiefari, E. et al. Pseudogene-mediated posttranscriptional silencing of HMGA1 can result in insulin resistance and type 2 diabetes. Nat. Commun, 1, 40, DOI:10.1038/ncomms1040 (2010).
    • (2010) Nat. Commun , vol.1 , pp. 40
    • Chiefari, E.1
  • 18
    • 74549129403 scopus 로고    scopus 로고
    • HMG modifications and nuclear function
    • Zhang, Q. & Wang, Y. HMG modifications and nuclear function. Biochim. Biophys. Acta 1799, 28-36 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 28-36
    • Zhang, Q.1    Wang, Y.2
  • 19
    • 17844403529 scopus 로고    scopus 로고
    • Discovering high mobility group A molecular partners in tumour cells
    • Sgarra, R. et al. Discovering high mobility group A molecular partners in tumour cells. Proteomics 5, 1494-1506 (2005).
    • (2005) Proteomics , vol.5 , pp. 1494-1506
    • Sgarra, R.1
  • 20
    • 55849141307 scopus 로고    scopus 로고
    • Interaction proteomics of the HMGA chromatin architectural factors
    • Sgarra, R. et al. Interaction proteomics of the HMGA chromatin architectural factors. Proteomics 8, 4721-4732 (2008).
    • (2008) Proteomics , vol.8 , pp. 4721-4732
    • Sgarra, R.1
  • 21
    • 79955370375 scopus 로고    scopus 로고
    • HMGA Interactome: New insights from phage display technology
    • Malini, E. et al. HMGA Interactome: new insights from phage display technology. Biochemistry 50, 3462-3468 (2011).
    • (2011) Biochemistry , vol.50 , pp. 3462-3468
    • Malini, E.1
  • 22
    • 67049117516 scopus 로고    scopus 로고
    • Macroscopic differences in HMGA oncoproteins post-translational modifications: C-terminal phosphorylation of HMGA2 affects its DNA binding properties
    • Sgarra, R. et al. Macroscopic differences in HMGA oncoproteins post-translational modifications: C-terminal phosphorylation of HMGA2 affects its DNA binding properties. J. Proteome Res. 8, 2978-2989 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 2978-2989
    • Sgarra, R.1
  • 23
    • 0035128347 scopus 로고    scopus 로고
    • Transcriptional regulation of human insulin receptor gene by the high-mobility group protein HMGI(Y)
    • Brunetti, A.,Manfioletti, G., Chiefari, E. & Goldfine, I. D., Foti, D. 'Transcriptional regulation of human insulin receptor gene by the high-mobility group protein HMGI(Y). FASEB, 15, 492-500 (2001).
    • (2001) FASEB , vol.15 , pp. 492-500
    • Brunetti, A.1    Manfioletti, G.2    Chiefari, E.3    Goldfine, I.D.4    Foti, D.5
  • 24
    • 0035985191 scopus 로고    scopus 로고
    • The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype
    • Okuwaki, M., Tsujimoto, M. & Nagata, K. The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype. Mol. Biol. Cell 13, 2016-2030 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2016-2030
    • Okuwaki, M.1    Tsujimoto, M.2    Nagata, K.3
  • 26
    • 41349111453 scopus 로고    scopus 로고
    • The structure and functions of NPM1/Nucleophosmin/B23, a multifunctional nucleolar acidic protein
    • Okuwaki, M. The structure and functions of NPM1/Nucleophosmin/B23, a multifunctional nucleolar acidic protein. J. Biochem. 143, 441-448 (2008).
    • (2008) J. Biochem. , vol.143 , pp. 441-448
    • Okuwaki, M.1
  • 27
    • 0035850837 scopus 로고    scopus 로고
    • Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone
    • Okuwaki, M., Matsumoto, K., Tsujimoto, M. & Nagata, K. Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone. FEBS Lett. 506, 272-276 (2001).
    • (2001) FEBS Lett. , vol.506 , pp. 272-276
    • Okuwaki, M.1    Matsumoto, K.2    Tsujimoto, M.3    Nagata, K.4
  • 28
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani, K., Szebeni, A. & Olson, M. O. Mapping the functional domains of nucleolar protein B23. J Biol Chem. 275, 24451-24457 (2000).
    • (2000) J Biol Chem. , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 29
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • Lai, J. S. & Herr, W. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad. Sci. USA 89, 6958-6962 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6958-6962
    • Lai, J.S.1    Herr, W.2
  • 30
    • 33745829795 scopus 로고    scopus 로고
    • Molecular chaperones: Assisting assembly in addition to folding
    • Ellis, R. J. Molecular chaperones: assisting assembly in addition to folding. Trends Biochem. Sci. 31, 395-401 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 395-401
    • Ellis, R.J.1
  • 31
    • 44949119317 scopus 로고    scopus 로고
    • Histone chaperones in nucleosome eviction and histone exchange
    • Park, Y. J. & Luger, K. Histone chaperones in nucleosome eviction and histone exchange. Curr. Opin. Struct. Biol. 18, 282-289 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 282-289
    • Park, Y.J.1    Luger, K.2
  • 32
    • 34250806536 scopus 로고    scopus 로고
    • Physical and functional interaction between a nucleolar protein nucleophosmin/B23 and adenovirus basic core proteins
    • Samad, M. A., Okuwaki, M., Haruki, H. & Nagata, K. Physical and functional interaction between a nucleolar protein nucleophosmin/B23 and adenovirus basic core proteins. FEBS Lett. 581, 3283-3288 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 3283-3288
    • Samad, M.A.1    Okuwaki, M.2    Haruki, H.3    Nagata, K.4
  • 33
    • 0030721536 scopus 로고    scopus 로고
    • High mobility group I proteins interfere with the homeodomains binding to DNA
    • Arlotta, P. et al. High mobility group I proteins interfere with the homeodomains binding to DNA. J. Biol. Chem. 272, 29904-29910 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 29904-29910
    • Arlotta, P.1
  • 34
    • 79953720878 scopus 로고    scopus 로고
    • The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone
    • Gadad, S. S. et al. The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone. Biochemistry 50, 2780-2789 (2011).
    • (2011) Biochemistry , vol.50 , pp. 2780-2789
    • Gadad, S.S.1
  • 35
    • 23844472662 scopus 로고    scopus 로고
    • Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription
    • Swaminathan, V., Kishore, A. H., Febitha, K. K. & Kundu, T. K. Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription. Mol. Cell. Biol. 25, 7534-7545 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7534-7545
    • Swaminathan, V.1    Kishore, A.H.2    Febitha, K.K.3    Kundu, T.K.4
  • 36
    • 0030930058 scopus 로고    scopus 로고
    • Identification and characterization of nucleophosmin/B23/numatrin which binds the anti-oncogenic transcription factor IRF-1 and manifests oncogenic activity
    • Kondo, T. et al. Identification and characterization of nucleophosmin/B23/numatrin which binds the anti-oncogenic transcription factor IRF-1 and manifests oncogenic activity. Oncogene 15, 1275-1281 (1997).
    • (1997) Oncogene , vol.15 , pp. 1275-1281
    • Kondo, T.1
  • 37
    • 0028335152 scopus 로고
    • Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23
    • Inouye, C. J. & Seto, E. Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23. J. Biol. Chem. 269, 6506-6510 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 6506-6510
    • Inouye, C.J.1    Seto, E.2
  • 38
    • 3543023310 scopus 로고    scopus 로고
    • Evidence for nucleosome depletion at active regulatory regions genome-wide
    • Lee, C. K., Shibata, Y., Rao, B., Strahl, B. D. & Lieb, J. D. Evidence for nucleosome depletion at active regulatory regions genome-wide. Nat. Genet. 36, 900-905 (2004).
    • (2004) Nat. Genet. , vol.36 , pp. 900-905
    • Lee, C.K.1    Shibata, Y.2    Rao, B.3    Strahl, B.D.4    Lieb, J.D.5
  • 39
    • 79952231642 scopus 로고    scopus 로고
    • Functional variants of the HMGA1 gene and type 2 diabetes mellitus
    • Chiefari, E. et al. Functional variants of the HMGA1 gene and type 2 diabetes mellitus. JAMA 305, 903-912 (2011).
    • (2011) JAMA , vol.305 , pp. 903-912
    • Chiefari, E.1
  • 40
    • 84865442111 scopus 로고    scopus 로고
    • Polymorphism of HMGA1 is associated with increased risk of type 2 diabetes among Chinese individuals
    • Liu, L. et al. Polymorphism of HMGA1 is associated with increased risk of type 2 diabetes among Chinese individuals. Diabetologia 55, 1685-1688 (2012).
    • (2012) Diabetologia , vol.55 , pp. 1685-1688
    • Liu, L.1
  • 41
    • 84875795546 scopus 로고    scopus 로고
    • A polymorphism of HMGA1 is associated with increased risk of metabolic syndrome and related components
    • Chiefari, E. et al. A polymorphism of HMGA1 is associated with increased risk of metabolic syndrome and related components. Sci. Rep. 3, 1491; DOI: 10.1038/srep01491 (2013).
    • (2013) Sci. Rep. , vol.3 , pp. 1491
    • Chiefari, E.1
  • 42
    • 84863666187 scopus 로고    scopus 로고
    • Insulin resistance and cancer risk: An overview of the pathogenetic mechanisms
    • Arcidiacono, B. et al. Insulin resistance and cancer risk: an overview of the pathogenetic mechanisms. Exp. Diabetes Res. 2012, 789174 (2012).
    • (2012) Exp. Diabetes Res. , vol.2012 , pp. 789174
    • Arcidiacono, B.1
  • 43
    • 58249092146 scopus 로고    scopus 로고
    • Insulin, the insulin-like growth factor axis, and mortality in patients with nonmetastatic colorectal cancer
    • Wolpin, B. M. et al. Insulin, the insulin-like growth factor axis, and mortality in patients with nonmetastatic colorectal cancer. J. Clin. Oncol. 27, 176-85 (2009).
    • (2009) J. Clin. Oncol. , vol.27 , pp. 176-185
    • Wolpin, B.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.