메뉴 건너뛰기




Volumn 6, Issue , 2012, Pages 1-10

Endoplasmic Reticulum (ER) stress enhances Tip60 (A Histone Acetyltransferase) binding to the concanavalin A

Author keywords

Cell cycle; ER stress; HAT; N glycosylation; Tip60

Indexed keywords

CONCANAVALIN A; ETOPOSIDE; PROTEIN TIP60; TRANSACTIVATOR PROTEIN; TUNICAMYCIN; UNCLASSIFIED DRUG;

EID: 84859487144     PISSN: None     EISSN: 1874091X     Source Type: Journal    
DOI: 10.2174/1874091X01206010001     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 0029961534 scopus 로고    scopus 로고
    • Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator
    • Kamine, J.; Elangovan, B.; Subramanian, T.; Coleman, D.; Chinnadurai, G. Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology, 1996, 216, (2), 357-366.
    • (1996) Virology , vol.216 , Issue.2 , pp. 357-366
    • Kamine, J.1    Elangovan, B.2    Subramanian, T.3    Coleman, D.4    Chinnadurai, G.5
  • 2
    • 0030712311 scopus 로고    scopus 로고
    • Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60
    • Yamamoto, T.; Horikoshi, M. Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. J. Biol. Chem., 1997, 272, (49), 30595-30598.
    • (1997) J. Biol. Chem , vol.272 , Issue.49 , pp. 30595-30598
    • Yamamoto, T.1    Horikoshi, M.2
  • 3
    • 0033529253 scopus 로고    scopus 로고
    • Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein
    • Creaven, M.; Hans, F.; Mutskov, V.; Col, E.; Caron, C.; Dimitrov, S.; Khochbin, S. Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat. Biochemistry, 1999, 38, (27), 8826-8830.
    • (1999) Tat. Biochemistry , vol.38 , Issue.27 , pp. 8826-8830
    • Creaven, M.1    Hans, F.2    Mutskov, V.3    Col, E.4    Caron, C.5    Dimitrov, S.6    Khochbin, S.7
  • 6
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner, D. E.; Berger, S. L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev., 2000, 64, (2), 435-459.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , Issue.2 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 7
    • 33747882071 scopus 로고    scopus 로고
    • Tip60 in DNA damage response and growth control: Many tricks in one HAT
    • Squatrito, M.; Gorrini, C.; Amati, B. Tip60 in DNA damage response and growth control: many tricks in one HAT. Trends Cell Biol., 2006, 16, (9), 433-442.
    • (2006) Trends Cell Biol , vol.16 , Issue.9 , pp. 433-442
    • Squatrito, M.1    Gorrini, C.2    Amati, B.3
  • 8
    • 0033231984 scopus 로고    scopus 로고
    • Oligosaccharide transport: Pumping waste from the ER into lysosomes
    • Moore, S. E. Oligosaccharide transport: pumping waste from the ER into lysosomes. Trends Cell Biol., 1999, 9, (11), 441-446.
    • (1999) Trends Cell Biol , vol.9 , Issue.11 , pp. 441-446
    • Moore, S.E.1
  • 9
    • 0034657712 scopus 로고    scopus 로고
    • Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
    • Parodi, A. J. Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem. J., 2000, 348 Pt 1, 1-13.
    • (2000) Biochem. J , Issue.348 Pt 1 , pp. 1-13
    • Parodi, A.J.1
  • 10
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes, R. C. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochem. Biophys. Acta., 1999, 1473, (1), 172-185.
    • (1999) Biochem. Biophys. Acta , vol.1473 , Issue.1 , pp. 172-185
    • Hughes, R.C.1
  • 11
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A.; Aebi, M. Intracellular functions of N-linked glycans. Science, 2001, 291, (5512), 2364-2369.
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 12
    • 0020146990 scopus 로고
    • Conformational aspects of N-glycosylation of proteins. Studies with linear and cyclic peptides as probes
    • Bause, E.; Hettkamp, H.; Legler, G. Conformational aspects of N-glycosylation of proteins. Studies with linear and cyclic peptides as probes. Biochem. J. 1982, 203, (3), 761-768.
    • (1982) Biochem. J , vol.203 , Issue.3 , pp. 761-768
    • Bause, E.1    Hettkamp, H.2    Legler, G.3
  • 13
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause, E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem. J., 1983, 209, (2), 331-336.
    • (1983) Biochem. J , vol.209 , Issue.2 , pp. 331-336
    • Bause, E.1
  • 14
    • 75749134145 scopus 로고    scopus 로고
    • N-glycan structures: Recognition and processing in the ER
    • Aebi, M.; Bernasconi, R.; Clerc, S.; Molinari, M. N-glycan structures: recognition and processing in the ER. Trends Biochem. Sci., 2010, 35, (2), 74-82.
    • (2010) Trends Biochem. Sci , vol.35 , Issue.2 , pp. 74-82
    • Aebi, M.1    Bernasconi, R.2    Clerc, S.3    Molinari, M.4
  • 15
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C.; Braakman, I.; Helenius, A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA, 1994, 91, (3), 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.3 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 16
    • 0030667061 scopus 로고    scopus 로고
    • The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
    • Hebert, D. N.; Zhang, J. X.; Chen, W.; Foellmer, B.; Helenius, A. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol., 1997, 139, (3), 613-623.
    • (1997) J. Cell Biol , vol.139 , Issue.3 , pp. 613-623
    • Hebert, D.N.1    Zhang, J.X.2    Chen, W.3    Foellmer, B.4    Helenius, A.5
  • 17
    • 68149136657 scopus 로고    scopus 로고
    • Cellular responses to endoplasmic reticulum stress and apoptosis
    • Rasheva, V. I.; Domingos, P. M. Cellular responses to endoplasmic reticulum stress and apoptosis. Apoptosis, 2009, 14, (8), 996-1007.
    • (2009) Apoptosis , vol.14 , Issue.8 , pp. 996-1007
    • Rasheva, V.I.1    Domingos, P.M.2
  • 18
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski, D. T.; Hegde, R. S. Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell. Biol., 2010, 189, (5), 783-794.
    • (2010) J. Cell. Biol , vol.189 , Issue.5 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 19
    • 50249116184 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response in immunity and autoimmunity
    • Todd, D. J.; Lee, A. H.; Glimcher, L. H. The endoplasmic reticulum stress response in immunity and autoimmunity. Nat Rev. Immunol., 2008, 8, (9), 663-674.
    • (2008) Nat Rev. Immunol , vol.8 , Issue.9 , pp. 663-674
    • Todd, D.J.1    Lee, A.H.2    Glimcher, L.H.3
  • 20
    • 79958830569 scopus 로고    scopus 로고
    • Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates
    • Lee, E. J.; Shin, S. H.; Hyun, S.; Chun, J.; Kang, S. S. Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates. Animal Cells Syst. (Seoul,) 2011, 15, (2), 95-106.
    • (2011) Animal Cells Syst. (Seoul,) , vol.15 , Issue.2 , pp. 95-106
    • Lee, E.J.1    Shin, S.H.2    Hyun, S.3    Chun, J.4    Kang, S.S.5
  • 21
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg, J.; Pilch, B. J.; Podtelejnikov, A. V.; Wisniewski, J. R. Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics, 2004, 4, (2), 454-465.
    • (2004) Proteomics , vol.4 , Issue.2 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wisniewski, J.R.4
  • 22
    • 33747349486 scopus 로고    scopus 로고
    • Concanavalin A for in vivo glucose sensing: A biotoxicity review
    • Ballerstadt, R.; Evans, C.; McNichols, R.; Gowda, A. Concanavalin A for in vivo glucose sensing: a biotoxicity review. Biosens. Bioelectron, 2006, 22, (2), 275-284.
    • (2006) Biosens. Bioelectron , vol.22 , Issue.2 , pp. 275-284
    • Ballerstadt, R.1    Evans, C.2    McNichols, R.3    Gowda, A.4
  • 23
    • 63449123137 scopus 로고    scopus 로고
    • Lectin of Concanavalin A as an anti-hepatoma therapeutic agent
    • Lei, H. Y.; Chang, C. P. Lectin of Concanavalin A as an anti-hepatoma therapeutic agent. J. Biomed. Sci., 2009, 16, 10.
    • (2009) J. Biomed. Sci , vol.16 , pp. 10
    • Lei, H.Y.1    Chang, C.P.2
  • 24
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley, F.; Trimble, R. B.; Tarentino, A. L.; Plummer, T. H., Jr. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem., 1989, 180, (2), 195-204.
    • (1989) Anal. Biochem , vol.180 , Issue.2 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer Jr., T.H.4
  • 25
    • 0017369177 scopus 로고
    • Impaired conversion of procollagen to collagen by fibroblasts and bone treated with tunicamycin, an inhibitor of protein glycosylation
    • Duksin, D.; Bornstein, P. Impaired conversion of procollagen to collagen by fibroblasts and bone treated with tunicamycin, an inhibitor of protein glycosylation. J. Biol. Chem., 1977, 252, (3), 955-962.
    • (1977) J. Biol. Chem , vol.252 , Issue.3 , pp. 955-962
    • Duksin, D.1    Bornstein, P.2
  • 26
    • 13644267779 scopus 로고    scopus 로고
    • Effects of tunicamycin, mannosamine, and other inhibitors of glycoprotein processing on skeletal alkaline phosphatase in human osteoblast-like cells
    • Farley, J. R.; Magnusson, P. Effects of tunicamycin, mannosamine, and other inhibitors of glycoprotein processing on skeletal alkaline phosphatase in human osteoblast-like cells. Calcif. Tissue Int., 2005, 76, (1), 63-74.
    • (2005) Calcif. Tissue Int , vol.76 , Issue.1 , pp. 63-74
    • Farley, J.R.1    Magnusson, P.2
  • 27
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X.; Sudhof, T. C. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science, 2001, 293, (5527), 115-120.
    • (2001) Science , vol.293 , Issue.5527 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 28
    • 77950190270 scopus 로고    scopus 로고
    • Etoposide induces G2/M arrest and apoptosis in neural progenitor cells via DNA damage and an ATM/p53-related pathway
    • Nam, C.; Doi, K.; Nakayama, H. Etoposide induces G2/M arrest and apoptosis in neural progenitor cells via DNA damage and an ATM/p53-related pathway. Histol. Histopathol., 2010, 25, (4), 485-493.
    • (2010) Histol. Histopathol , vol.25 , Issue.4 , pp. 485-493
    • Nam, C.1    Doi, K.2    Nakayama, H.3
  • 29
    • 77949268266 scopus 로고    scopus 로고
    • Cellular responses to etoposide: Cell death despite cell cycle arrest and repair of DNA damage
    • Schonn, I.; Hennesen, J.; Dartsch, D. C. Cellular responses to etoposide: cell death despite cell cycle arrest and repair of DNA damage. Apoptosis, 2010, 15, (2), 162-172.
    • (2010) Apoptosis , vol.15 , Issue.2 , pp. 162-172
    • Schonn, I.1    Hennesen, J.2    Dartsch, D.C.3
  • 30
    • 0026611735 scopus 로고
    • Brefeldin A thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis
    • Price, B. D.; Mannheim-Rodman, L. A.; Calderwood, S. K. Brefeldin A, thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J. Cell. Physiol., 1992, 152, (3), 545-552.
    • (1992) J. Cell. Physiol , vol.152 , Issue.3 , pp. 545-552
    • Price, B.D.1    Mannheim-Rodman, L.A.2    Calderwood, S.K.3
  • 31
    • 0032942210 scopus 로고    scopus 로고
    • Brefeldin A (BFA) disrupts the organization of the microtubule and the actin cytoskeletons
    • Alvarez, C.; Sztul, E. S, Brefeldin A (BFA) disrupts the organization of the microtubule and the actin cytoskeletons. Eur. J. Cell. Biol., 1999, 78, (1), 1-14.
    • (1999) Eur. J. Cell. Biol , vol.78 , Issue.1 , pp. 1-14
    • Alvarez, C.1    Sztul, E.S.2
  • 32
    • 77952574173 scopus 로고    scopus 로고
    • ER stress in pancreatic beta cells: The thin red line between adaptation and failure
    • Eizirik, D. L.; Cnop, M. ER stress in pancreatic beta cells: the thin red line between adaptation and failure. Sci. Signal., 2010, 3, (110), pe7.
    • (2010) Sci. Signal , vol.3 , Issue.110
    • Eizirik, D.L.1    Cnop, M.2
  • 33
    • 0037047434 scopus 로고    scopus 로고
    • The gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein induces apoptosis via Tip60 in H4 cells
    • Kinoshita, A.; Whelan, C. M.; Berezovska, O.; Hyman, B. T. The gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein induces apoptosis via Tip60 in H4 cells. J. Biol. Chem., 2002, 277, (32), 28530-28536.
    • (2002) J. Biol. Chem , vol.277 , Issue.32 , pp. 28530-28536
    • Kinoshita, A.1    Whelan, C.M.2    Berezovska, O.3    Hyman, B.T.4
  • 34
    • 40549088942 scopus 로고    scopus 로고
    • The FE65 proteins and Alzheimer's disease
    • McLoughlin, D. M.; Miller, C. C. The FE65 proteins and Alzheimer's disease. J. Neurosci. Res., 2008, 86, (4), 744-754.
    • (2008) J. Neurosci. Res , vol.86 , Issue.4 , pp. 744-754
    • McLoughlin, D.M.1    Miller, C.C.2
  • 36
    • 70249123438 scopus 로고    scopus 로고
    • Ubiquitylation of Fe65 adaptor protein by neuronal precursor cell expressed developmentally down regulated 4-2 (Nedd4-2) via the WW domain interaction with Fe65
    • Lee, E. J.; Hyun, S.; Chun, J.; Shin, S. H.; Kang, S. S. Ubiquitylation of Fe65 adaptor protein by neuronal precursor cell expressed developmentally down regulated 4-2 (Nedd4-2) via the WW domain interaction with Fe65. Exp. Mol. Med., 2009, 41, (8), 555-568.
    • (2009) Exp. Mol. Med , vol.41 , Issue.8 , pp. 555-568
    • Lee, E.J.1    Hyun, S.2    Chun, J.3    Shin, S.H.4    Kang, S.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.