메뉴 건너뛰기




Volumn 30, Issue 8, 2010, Pages 1898-1909

The chaperone-like protein HYPK acts together with natA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GREEN FLUORESCENT PROTEIN; HUNTINGTIN; HYBRID PROTEIN; HYPK PROTEIN; NALPHA TERMINAL ACETYLTRANSFERASE PROTEIN; POLYGLUTAMINE; UNCLASSIFIED DRUG;

EID: 77950667600     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01199-09     Document Type: Article
Times cited : (106)

References (46)
  • 2
    • 57649114878 scopus 로고    scopus 로고
    • Implication of human N-alpha-acetyltransferase 5 in cellular proliferation and carcinogenesis
    • Ametzazurra, A., E. Larrea, M. P. Civeira, J. Prieto, and R. Aldabe. 2008. Implication of human N-alpha-acetyltransferase 5 in cellular proliferation and carcinogenesis. Oncogene 27:7296-7306.
    • (2008) Oncogene , vol.27 , pp. 7296-7306
    • Ametzazurra, A.1    Larrea, E.2    Civeira, M.P.3    Prieto, J.4    Aldabe, R.5
  • 3
    • 0042972838 scopus 로고    scopus 로고
    • A new algorithm for the evaluation of shotgun peptide sequencing in proteomics: Support vector machine classification of peptide MS/MS spectra and SEQUEST scores
    • Anderson, D. C., W. Li, D. G. Payan, and W. S. Noble. 2003. A new algorithm for the evaluation of shotgun peptide sequencing in proteomics: support vector machine classification of peptide MS/MS spectra and SEQUEST scores. J. Proteome Res. 2:137-146.
    • (2003) J. Proteome Res. , vol.2 , pp. 137-146
    • Anderson, D.C.1    Li, W.2    Payan, D.G.3    Noble, W.S.4
  • 4
    • 15944413192 scopus 로고    scopus 로고
    • Identification and characterization of the human ARD1-NATH protein acetyltransferase complex
    • DOI 10.1042/BJ20041071
    • Arnesen, T., D. Anderson, C. Baldersheim, M. Lanotte, J. E. Varhaug, and J. R. Lillehaug. 2005. Identification and characterization of the human ARD1-NATH protein acetyltransferase complex. Biochem. J. 386:433-443. (Pubitemid 40445867)
    • (2005) Biochemical Journal , vol.386 , Issue.3 , pp. 433-443
    • Arnesen, T.1    Anderson, D.2    Baldersheim, C.3    Lanotte, M.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 5
    • 33645757829 scopus 로고    scopus 로고
    • Cloning and characterization of hNAT5/hSAN: An evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex
    • Arnesen, T., D. Anderson, J. Torsvik, H. B. Halseth, J. E. Varhaug, and J. R. Lillehaug. 2006. Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex. Gene 371:291-295.
    • (2006) Gene , vol.371 , pp. 291-295
    • Arnesen, T.1    Anderson, D.2    Torsvik, J.3    Halseth, H.B.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 7
    • 27744441053 scopus 로고    scopus 로고
    • Expression of N-acetyl transferase human and human arrest defective 1 proteins in thyroid neoplasms
    • DOI 10.1089/thy.2005.15.1131
    • Arnesen, T., D. Gromyko, O. Horvli, O. Fluge, J. Lillehaug, and J. E. Varhaug. 2005. Expression of N-acetyl transferase human and human Arrest defective 1 proteins in thyroid neoplasms. Thyroid 15:1131-1136. (Pubitemid 41720719)
    • (2005) Thyroid , vol.15 , Issue.10 , pp. 1131-1136
    • Arnesen, T.1    Gromyko, D.2    Horvli, O.3    Fluge, O.4    Lillehaug, J.5    Varhaug, J.E.6
  • 9
    • 33744971921 scopus 로고    scopus 로고
    • Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex
    • DOI 10.1038/sj.onc.1209469, PII 1209469
    • Arnesen, T., D. Gromyko, F. Pendino, A. Ryningen, J. E. Varhaug, and J. R. Lillehaug. 2006. Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex. Oncogene 25:4350-4360. (Pubitemid 44100505)
    • (2006) Oncogene , vol.25 , Issue.31 , pp. 4350-4360
    • Arnesen, T.1    Gromyko, D.2    Pendino, F.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 10
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1alpha
    • DOI 10.1016/j.febslet.2005.10.036, PII S0014579305012962
    • Arnesen, T., X. Kong, R. Evjenth, D. Gromyko, J. E. Varhaug, Z. Lin, N. Sang, J. Caro, and J. R. Lillehaug. 2005. Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha. FEBS Lett. 579:6428-6432. (Pubitemid 41612163)
    • (2005) FEBS Letters , vol.579 , Issue.28 , pp. 6428-6432
    • Arnesen, T.1    Kong, X.2    Evjenth, R.3    Gromyko, D.4    Varhaug, J.E.5    Lin, Z.6    Sang, N.7    Caro, J.8    Lillehaug, J.R.9
  • 14
    • 77950633355 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 15
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • Edgar, R. C. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32:1792-1797. (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 16
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng. J. K., A. L. McCormack, and J. R. Yates. 1994. An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database. J. Am. Soc. Mass Spectrom. 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 17
    • 0001037808 scopus 로고
    • Cycloheximide: Aspects of inhibition of protein synthesis in mammalian cells
    • Ennis, H. L., and M. Lubin. 1964. Cycloheximide: aspects of inhibition of protein synthesis in mammalian cells. Science 146:1474-1476.
    • (1964) Science , vol.146 , pp. 1474-1476
    • Ennis, H.L.1    Lubin, M.2
  • 18
    • 71449101084 scopus 로고    scopus 로고
    • Human Naa50p (Nat5/San) displays both protein N alphaand N epsilon-acetyltransferase activity
    • Evjenth, R., K. Hole, O. A. Karlsen, M. Ziegler, T. Arnesen, and J. R. Lillehaug. 2009. Human Naa50p (Nat5/San) displays both protein N alphaand N epsilon-acetyltransferase activity. J. Biol. Chem. 284:31122-31129.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31122-31129
    • Evjenth, R.1    Hole, K.2    Karlsen, O.A.3    Ziegler, M.4    Arnesen, T.5    Lillehaug, J.R.6
  • 20
    • 20544431636 scopus 로고    scopus 로고
    • Analysis of ARD1 function in hypoxia response using retroviral RNA interference
    • Fisher, T. S., S. D. Etages, L. Hayes, K. Crimin, and B. Li. 2005. Analysis of ARD1 function in hypoxia response using retroviral RNA interference. J. Biol. Chem. 280:17749-17757.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17749-17757
    • Fisher, T.S.1    Etages, S.D.2    Hayes, L.3    Crimin, K.4    Li, B.5
  • 21
    • 0141640821 scopus 로고    scopus 로고
    • The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
    • Gautschi, M., S. Just, A. Mun, S. Ross, P. Rucknagel, Y. Dubaquie, A. Ehrenhofer-Murray, and S. Rospert. 2003. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 23:7403-7414.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7403-7414
    • Gautschi, M.1    Just, S.2    Mun, A.3    Ross, S.4    Rucknagel, P.5    Dubaquie, Y.6    Ehrenhofer-Murray, A.7    Rospert, S.8
  • 22
    • 0036589853 scopus 로고    scopus 로고
    • Use of MEDUSA-based data analysis and capillary HPLC - Ion-trap mass spectrometry to examine complex immunoaffinity extracts of RbAp48
    • DOI 10.1021/pr0255147
    • Gururaja, T., W. Li, J. Bernstein, D. G. Payan, and D. C. Anderson. 2002. Use of MEDUSA-based data analysis and capillary HPLC-ion-trap mass spectrometry to examine complex immunoaffinity extracts of RBAp48. J. Proteome Res. 1:253-261. (Pubitemid 36050255)
    • (2002) Journal of Proteome Research , vol.1 , Issue.3 , pp. 253-261
    • Gururaja, T.1    Li, W.2    Bernstein, J.3    Payan, D.G.4    Anderson, D.C.5
  • 24
    • 34548290480 scopus 로고    scopus 로고
    • Cellular prion protein (PrPC) protects neuronal cells from the effect of huntingtin aggregation
    • Lee, K. J., A. Panzera, D. Rogawski, L. E. Greene, and E. Eisenberg. 2007. Cellular prion protein (PrPC) protects neuronal cells from the effect of huntingtin aggregation. J. Cell Sci. 120:2663-2671.
    • (2007) J. Cell Sci. , vol.120 , pp. 2663-2671
    • Lee, K.J.1    Panzera, A.2    Rogawski, D.3    Greene, L.E.4    Eisenberg, E.5
  • 25
    • 33845293454 scopus 로고    scopus 로고
    • Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation
    • Lim, J. H., J. W. Park, and Y. S. Chun. 2006. Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation. Cancer Res. 66:10677-10682.
    • (2006) Cancer Res. , vol.66 , pp. 10677-10682
    • Lim, J.H.1    Park, J.W.2    Chun, Y.S.3
  • 28
    • 0026605888 scopus 로고
    • ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity
    • Park, E. C., and J. W. Szostak. 1992. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 11:2087-2093.
    • (1992) EMBO J. , vol.11 , pp. 2087-2093
    • Park, E.C.1    Szostak, J.W.2
  • 29
    • 0015949361 scopus 로고
    • N-terminal acetylation of histone-like nascent peptides on rat liver polyribosomes in vitro
    • Pestana, A., and H. C. Pitot. 1974. N-terminal acetylation of histone-like nascent peptides on rat liver polyribosomes in vitro. Nature 247:200-202.
    • (1974) Nature , vol.247 , pp. 200-202
    • Pestana, A.1    Pitot, H.C.2
  • 30
    • 0016691755 scopus 로고
    • Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro
    • Pestana, A., and H. C. Pitot. 1975. Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro. Biochemistry 14:1404-1412.
    • (1975) Biochemistry , vol.14 , pp. 1404-1412
    • Pestana, A.1    Pitot, H.C.2
  • 31
    • 0032528301 scopus 로고    scopus 로고
    • The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex
    • DOI 10.1093/emboj/17.14.3981
    • Pfund, C., N. Lopez-Hoyo, T. Ziegelhoffer, B. A. Schilke, P. Lopez-Buesa, W. A. Walter, M. Wiedmann, and E. A. Craig. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosomenascent chain complex. EMBO J. 17:3981-3989. (Pubitemid 28333983)
    • (1998) EMBO Journal , vol.17 , Issue.14 , pp. 3981-3989
    • Pfund, C.1    Lopez-Hoyo, N.2    Ziegelhoffer, T.3    Schilke, B.A.4    Lopez-Buesa, P.5    Walter, W.A.6    Wiedmann, M.7    Craig, E.A.8
  • 32
    • 71449089622 scopus 로고    scopus 로고
    • A synopsis of eukaryotic Nalpha-terminal acetyltransferases: Nomenclature, subunits and substrates
    • Polevoda, B., T. Arnesen, and F. Sherman. 2009. A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proc. 3(Suppl. 6):S2.
    • (2009) BMC Proc. , vol.3 , Issue.SUPPL. 6
    • Polevoda, B.1    Arnesen, T.2    Sherman, F.3
  • 33
    • 66349135032 scopus 로고    scopus 로고
    • Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4
    • Polevoda, B., J. Hoskins, and F. Sherman. 2009. Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4. Mol. Cell. Biol. 29:2913-2924.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2913-2924
    • Polevoda, B.1    Hoskins, J.2    Sherman, F.3
  • 34
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • Polevoda, B., and F. Sherman. 2003. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J. Mol. Biol. 325:595-622.
    • (2003) J. Mol. Biol. , vol.325 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 35
    • 34247281027 scopus 로고    scopus 로고
    • Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence
    • Raue, U., S. Oellerer, and S. Rospert. 2007. Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence. J. Biol. Chem. 282:7809-7816.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7809-7816
    • Raue, U.1    Oellerer, S.2    Rospert, S.3
  • 36
    • 37849012236 scopus 로고    scopus 로고
    • HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity
    • Raychaudhuri, S., M. Sinha, D. Mukhopadhyay, and N. P. Bhattacharyya. 2008. HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Hum. Mol. Genet. 17:240-255.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 240-255
    • Raychaudhuri, S.1    Sinha, M.2    Mukhopadhyay, D.3    Bhattacharyya, N.P.4
  • 37
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • DOI 10.1093/bioinformatics/btg180
    • Ronquist, F., and J. P. Huelsenbeck. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574. (Pubitemid 37038874)
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 38
    • 0141755383 scopus 로고    scopus 로고
    • An Nalphaacetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A
    • Song, O. K., X. Wang, J. H. Waterborg, and R. Sternglanz. 2003. An Nalphaacetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J. Biol. Chem. 278:38109-38112.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38109-38112
    • Song, O.K.1    Wang, X.2    Waterborg, J.H.3    Sternglanz, R.4
  • 39
    • 54049149934 scopus 로고    scopus 로고
    • Identification of the human N(alpha)-acetyltransferase complex B (hNatB): A complex important for cell-cycle progression
    • Starheim, K. K., T. Arnesen, D. Gromyko, A. Ryningen, J. E. Varhaug, and J. R. Lillehaug. 2008. Identification of the human N(alpha)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression. Biochem. J. 415:325-331.
    • (2008) Biochem. J. , vol.415 , pp. 325-331
    • Starheim, K.K.1    Arnesen, T.2    Gromyko, D.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 40
    • 67650085001 scopus 로고    scopus 로고
    • Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization
    • Starheim, K. K., D. Gromyko, R. Evjenth, A. Ryningen, J. E. Varhaug, J. R. Lillehaug, and T. Arnesen. 2009. Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell. Biol. 29:3569-3581.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3569-3581
    • Starheim, K.K.1    Gromyko, D.2    Evjenth, R.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6    Arnesen, T.7
  • 41
  • 42
    • 0015845499 scopus 로고
    • Synthesis of lens protein in vitro. N-terminal acetylation of alpha-crystallin
    • Strous, G. J., H. van Westreenen, and H. Bloemendal. 1973. Synthesis of lens protein in vitro. N-terminal acetylation of alpha-crystallin. Eur. J. Biochem. 38:79-85.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 79-85
    • Strous, G.J.1    Van Westreenen, H.2    Bloemendal, H.3
  • 43
    • 0026098715 scopus 로고
    • The characterization of free, cytoskeletal and membrane-bound polysomes in Krebs II ascites and 3T3 cells
    • Vedeler, A., I. F. Pryme, and J. E. Hesketh. 1991. The characterization of free, cytoskeletal and membrane-bound polysomes in Krebs II ascites and 3T3 cells. Mol. Cell. Biochem. 100:183-193.
    • (1991) Mol. Cell. Biochem. , vol.100 , pp. 183-193
    • Vedeler, A.1    Pryme, I.F.2    Hesketh, J.E.3
  • 44
    • 0029112391 scopus 로고
    • NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center
    • Wang, S., H. Sakai, and M. Wiedmann. 1995. NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center. J. Cell Biol. 130:519-528.
    • (1995) J. Cell Biol. , vol.130 , pp. 519-528
    • Wang, S.1    Sakai, H.2    Wiedmann, M.3
  • 45
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach, A., J. Carmichael, J. Swartz, R. A. Furlong, Y. Narain, J. Rankin, and D. C. Rubinsztein. 2000. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl. Acad. Sci. USA 97:2898-2903.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5    Rankin, J.6    Rubinsztein, D.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.