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Volumn 583, Issue 4, 2009, Pages 648-654

Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress

Author keywords

Calcium overload; Oxidative stress; Proteasomal degradation; Transglutaminase 2; Ubiquitination

Indexed keywords

CALCIMYCIN; CALCIUM; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2;

EID: 60049098220     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.01.032     Document Type: Article
Times cited : (22)

References (28)
  • 1
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., and Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4 (2003) 140-156
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 2
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: an enigmatic enzyme with diverse functions
    • Fesus L., and Piacentini M. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem. Sci. 27 (2002) 534-539
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 3
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus L., Thomazy V., and Falus A. Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett. 224 (1987) 104-108
    • (1987) FEBS Lett. , vol.224 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 4
    • 20444363472 scopus 로고    scopus 로고
    • Transglutaminase 2 in the balance of cell death and survival
    • Fesus L., and Szondy Z. Transglutaminase 2 in the balance of cell death and survival. FEBS Lett. 579 (2005) 3297-3302
    • (2005) FEBS Lett. , vol.579 , pp. 3297-3302
    • Fesus, L.1    Szondy, Z.2
  • 5
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi V., and Melino G. Gene disruption of tissue transglutaminase. Mol. Cell Biol. 21 (2001) 148-155
    • (2001) Mol. Cell Biol. , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 6
    • 33646858986 scopus 로고    scopus 로고
    • Implications of increased tissue transglutaminase (TG2) expression in drug-resistant breast cancer (MCF-7) cells
    • Herman J.F., Mangala L.S., and Mehta K. Implications of increased tissue transglutaminase (TG2) expression in drug-resistant breast cancer (MCF-7) cells. Oncogene 25 (2006) 3049-3058
    • (2006) Oncogene , vol.25 , pp. 3049-3058
    • Herman, J.F.1    Mangala, L.S.2    Mehta, K.3
  • 7
    • 0032929487 scopus 로고    scopus 로고
    • Reduction of transglutaminase 2 expression is associated with an induction of drug sensitivity in the PC-14 human lung cancer cell line
    • Han J.A., and Park S.C. Reduction of transglutaminase 2 expression is associated with an induction of drug sensitivity in the PC-14 human lung cancer cell line. J. Cancer Res. Clin. Oncol. 125 (1999) 89-95
    • (1999) J. Cancer Res. Clin. Oncol. , vol.125 , pp. 89-95
    • Han, J.A.1    Park, S.C.2
  • 8
    • 2442607838 scopus 로고    scopus 로고
    • Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis
    • Shin D.M., et al. Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis. J. Biol. Chem. 279 (2004) 15032-15039
    • (2004) J. Biol. Chem. , vol.279 , pp. 15032-15039
    • Shin, D.M.1
  • 9
    • 46749089164 scopus 로고    scopus 로고
    • TGFbeta mediates activation of transglutaminase 2 in response to oxidative stress that leads to protein aggregation
    • Shin D.M., et al. TGFbeta mediates activation of transglutaminase 2 in response to oxidative stress that leads to protein aggregation. Faseb J. 22 (2008) 2498-2507
    • (2008) Faseb J. , vol.22 , pp. 2498-2507
    • Shin, D.M.1
  • 10
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP
    • Lai T.S., Slaughter T.F., Peoples K.A., Hettasch J.M., and Greenberg C.S. Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP. J. Biol. Chem. 273 (1998) 1776-1781
    • (1998) J. Biol. Chem. , vol.273 , pp. 1776-1781
    • Lai, T.S.1    Slaughter, T.F.2    Peoples, K.A.3    Hettasch, J.M.4    Greenberg, C.S.5
  • 11
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu S., Cerione R.A., and Clardy J. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. USA 99 (2002) 2743-2747
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 12
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas D.M., Strop P., Brunger A.T., and Khosla C. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 5 (2007) e327
    • (2007) PLoS Biol. , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 13
    • 33744950386 scopus 로고    scopus 로고
    • Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity
    • Begg G.E., Holman S.R., Stokes P.H., Matthews J.M., Graham R.M., and Iismaa S.E. Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity. J. Biol. Chem. 281 (2006) 12603-12609
    • (2006) J. Biol. Chem. , vol.281 , pp. 12603-12609
    • Begg, G.E.1    Holman, S.R.2    Stokes, P.H.3    Matthews, J.M.4    Graham, R.M.5    Iismaa, S.E.6
  • 14
    • 0032708946 scopus 로고    scopus 로고
    • Tissue transglutaminase is a caspase substrate during apoptosis. Cleavage causes loss of transamidating function and is a biochemical marker of caspase 3 activation
    • Fabbi M., Marimpietri D., Martini S., Brancolini C., Amoresano A., Scaloni A., Bargellesi A., and Cosulich E. Tissue transglutaminase is a caspase substrate during apoptosis. Cleavage causes loss of transamidating function and is a biochemical marker of caspase 3 activation. Cell Death Differ. 6 (1999) 992-1001
    • (1999) Cell Death Differ. , vol.6 , pp. 992-1001
    • Fabbi, M.1    Marimpietri, D.2    Martini, S.3    Brancolini, C.4    Amoresano, A.5    Scaloni, A.6    Bargellesi, A.7    Cosulich, E.8
  • 15
    • 0141864664 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine
    • Jeon J.H., et al. Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine. Embo J. 22 (2003) 5273-5282
    • (2003) Embo J. , vol.22 , pp. 5273-5282
    • Jeon, J.H.1
  • 16
    • 34247608691 scopus 로고    scopus 로고
    • Calcium and reactive oxygen species increase in endothelial cells in response to releasers of endothelium-derived contracting factor
    • Tang E.H., Leung F.P., Huang Y., Feletou M., So K.F., Man R.Y., and Vanhoutte P.M. Calcium and reactive oxygen species increase in endothelial cells in response to releasers of endothelium-derived contracting factor. Br. J. Pharmacol. 151 (2007) 15-23
    • (2007) Br. J. Pharmacol. , vol.151 , pp. 15-23
    • Tang, E.H.1    Leung, F.P.2    Huang, Y.3    Feletou, M.4    So, K.F.5    Man, R.Y.6    Vanhoutte, P.M.7
  • 17
    • 0029017920 scopus 로고
    • Differential expression patterns of beta-actin mRNA in cells undergoing apoptosis
    • Naora H., and Naora H. Differential expression patterns of beta-actin mRNA in cells undergoing apoptosis. Biochem. Biophys. Res. Commun. 211 (1995) 491-496
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 491-496
    • Naora, H.1    Naora, H.2
  • 18
    • 9744235059 scopus 로고    scopus 로고
    • Fructose-1,6-diphosphate suppresses T-lymphocyte proliferation, promotes apoptosis and inhibits interleukins-1,6, beta-actin mRNAs, and transcription factors expression
    • Cohly H., Jenkins J., Skelton T., Meydrech E., and Markov A.K. Fructose-1,6-diphosphate suppresses T-lymphocyte proliferation, promotes apoptosis and inhibits interleukins-1,6, beta-actin mRNAs, and transcription factors expression. Immunol. Invest. 33 (2004) 407-421
    • (2004) Immunol. Invest. , vol.33 , pp. 407-421
    • Cohly, H.1    Jenkins, J.2    Skelton, T.3    Meydrech, E.4    Markov, A.K.5
  • 19
    • 0042886956 scopus 로고    scopus 로고
    • Reduction of thymosin beta4 and actin in HL60 cells during apoptosis is preceded by a decrease of their mRNAs
    • Muller C.S., Huff T., and Hannappel E. Reduction of thymosin beta4 and actin in HL60 cells during apoptosis is preceded by a decrease of their mRNAs. Mol. Cell Biochem. 250 (2003) 179-188
    • (2003) Mol. Cell Biochem. , vol.250 , pp. 179-188
    • Muller, C.S.1    Huff, T.2    Hannappel, E.3
  • 20
    • 0031866960 scopus 로고    scopus 로고
    • Tissue transglutaminase is an in situ substrate of calpain: regulation of activity
    • Zhang J., Guttmann R.P., and Johnson G.V. Tissue transglutaminase is an in situ substrate of calpain: regulation of activity. J. Neurochem. 71 (1998) 240-247
    • (1998) J. Neurochem. , vol.71 , pp. 240-247
    • Zhang, J.1    Guttmann, R.P.2    Johnson, G.V.3
  • 21
    • 0035823548 scopus 로고    scopus 로고
    • Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis
    • Antonyak M.A., Singh U.S., Lee D.A., Boehm J.E., Combs C., Zgola M.M., Page R.L., and Cerione R.A. Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis. J. Biol. Chem. 276 (2001) 33582-33587
    • (2001) J. Biol. Chem. , vol.276 , pp. 33582-33587
    • Antonyak, M.A.1    Singh, U.S.2    Lee, D.A.3    Boehm, J.E.4    Combs, C.5    Zgola, M.M.6    Page, R.L.7    Cerione, R.A.8
  • 22
    • 4744351463 scopus 로고    scopus 로고
    • Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells
    • Antonyak M.A., Miller A.M., Jansen J.M., Boehm J.E., Balkman C.E., Wakshlag J.J., Page R.L., and Cerione R.A. Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells. J. Biol. Chem. 279 (2004) 41461-41467
    • (2004) J. Biol. Chem. , vol.279 , pp. 41461-41467
    • Antonyak, M.A.1    Miller, A.M.2    Jansen, J.M.3    Boehm, J.E.4    Balkman, C.E.5    Wakshlag, J.J.6    Page, R.L.7    Cerione, R.A.8
  • 23
    • 0024471699 scopus 로고
    • Formation of N epsilon-(gamma-glutamyl)-lysine isodipeptide in Chinese-hamster ovary cells
    • Fesus L., and Tarcsa E. Formation of N epsilon-(gamma-glutamyl)-lysine isodipeptide in Chinese-hamster ovary cells. Biochem. J. 263 (1989) 843-848
    • (1989) Biochem. J. , vol.263 , pp. 843-848
    • Fesus, L.1    Tarcsa, E.2
  • 24
    • 34548764475 scopus 로고    scopus 로고
    • Tissue transglutaminase (TG2) facilitates phosphatidylserine exposure and calpain activity in calcium-induced death of erythrocytes
    • Sarang Z., et al. Tissue transglutaminase (TG2) facilitates phosphatidylserine exposure and calpain activity in calcium-induced death of erythrocytes. Cell Death Differ. 14 (2007) 1842-1844
    • (2007) Cell Death Differ. , vol.14 , pp. 1842-1844
    • Sarang, Z.1
  • 25
    • 29244447122 scopus 로고    scopus 로고
    • 2+ spiking to cell cycle progression
    • 2+ spiking to cell cycle progression. Reproduction 130 (2005) 813-823
    • (2005) Reproduction , vol.130 , pp. 813-823
    • Jones, K.T.1
  • 26
    • 1542571859 scopus 로고    scopus 로고
    • Calcium- and proteasome-dependent degradation of the JNK scaffold protein islet-brain 1
    • Allaman-Pillet N., et al. Calcium- and proteasome-dependent degradation of the JNK scaffold protein islet-brain 1. J. Biol. Chem. 278 (2003) 48720-48726
    • (2003) J. Biol. Chem. , vol.278 , pp. 48720-48726
    • Allaman-Pillet, N.1
  • 27
    • 27744480249 scopus 로고    scopus 로고
    • Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6
    • Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., and Chou M.M. Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6. J. Biol. Chem. 280 (2005) 35967-35973
    • (2005) J. Biol. Chem. , vol.280 , pp. 35967-35973
    • Shen, C.1    Ye, Y.2    Robertson, S.E.3    Lau, A.W.4    Mak, D.O.5    Chou, M.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.