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Volumn 421, Issue 4, 2012, Pages 773-779

Detection of Transglutaminase 2 conformational changes in living cell

Author keywords

Apoptosis; FRET; Transglutaminase 2

Indexed keywords

CALCIUM ION; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2;

EID: 84861225452     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.082     Document Type: Article
Times cited : (30)

References (29)
  • 1
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • Folk J.E. Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv. Enzymol. Relat. Areas. Mol. Biol. 1983, 54:1-56.
    • (1983) Adv. Enzymol. Relat. Areas. Mol. Biol. , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 2
    • 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., Clardy J. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. USA 2002, 99:2743-2747.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 3
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas D.M., Strop P., Brunger A.T., Khosla C. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 2007, 5:e327.
    • (2007) PLoS Biol. , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 4
    • 82755161784 scopus 로고    scopus 로고
    • 2+-dependent action of a multifunctional protein
    • 2+-dependent action of a multifunctional protein. FEBS J. 2011, 278:4717-4739.
    • (2011) FEBS J. , vol.278 , pp. 4717-4739
    • Kiraly, R.1    Demeny, M.2    Fesus, L.3
  • 5
    • 0028176166 scopus 로고
    • Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka H., Perez D.M., Baek K.J., et al. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 1994, 264:1593-1596.
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3
  • 6
    • 70350011814 scopus 로고    scopus 로고
    • The adenine nucleotide translocator 1 acts as a type 2 transglutaminase substrate: implications for mitochondrial-dependent apoptosis
    • Malorni W., Farrace M.G., Matarrese P., et al. The adenine nucleotide translocator 1 acts as a type 2 transglutaminase substrate: implications for mitochondrial-dependent apoptosis. Cell Death Differ. 2009, 16:1480-1492.
    • (2009) Cell Death Differ. , vol.16 , pp. 1480-1492
    • Malorni, W.1    Farrace, M.G.2    Matarrese, P.3
  • 7
    • 33646828721 scopus 로고    scopus 로고
    • Phosphorylation of histones by tissue transglutaminase
    • Mishra S., Saleh A., Espino P.S., et al. Phosphorylation of histones by tissue transglutaminase. J. Biol. Chem. 2006, 281:5532-5538.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5532-5538
    • Mishra, S.1    Saleh, A.2    Espino, P.S.3
  • 8
    • 77956916373 scopus 로고    scopus 로고
    • Transglutaminase 2: a multi-functional protein in multiple subcellular compartments
    • Park D., Choi S.S., Ha K.S. Transglutaminase 2: a multi-functional protein in multiple subcellular compartments. Amino Acids 2010, 39:619-631.
    • (2010) Amino Acids , vol.39 , pp. 619-631
    • Park, D.1    Choi, S.S.2    Ha, K.S.3
  • 9
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: nature's biological glues
    • Griffin M., Casadio R., Bergamini C.M. Transglutaminases: nature's biological glues. Biochem. J. 2002, 368:377-396.
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 11
    • 0031893826 scopus 로고    scopus 로고
    • Modulation of the in situ activity of tissue transglutaminase by calcium and GTP
    • Zhang J., Lesort M., Guttmann R.P., Johnson G.V.W. Modulation of the in situ activity of tissue transglutaminase by calcium and GTP. J. Biol. Chem. 1998, 273:2288-2295.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2288-2295
    • Zhang, J.1    Lesort, M.2    Guttmann, R.P.3    Johnson, G.V.W.4
  • 12
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort M., Attanavanich K., Zhang J., Johnson G.V.W. Distinct nuclear localization and activity of tissue transglutaminase. J. Biol. Chem. 1998, 273:11991-11994.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.W.4
  • 13
    • 21144444786 scopus 로고    scopus 로고
    • Transglutaminase activity is present in highly purified nonsynaptosomal mouse brain and liver mitochondria
    • Krasnikov B.F., Kim S., McConoughey S.J., et al. Transglutaminase activity is present in highly purified nonsynaptosomal mouse brain and liver mitochondria. Biochemistry 2005, 44:7830-7843.
    • (2005) Biochemistry , vol.44 , pp. 7830-7843
    • Krasnikov, B.F.1    Kim, S.2    McConoughey, S.J.3
  • 14
    • 67650538098 scopus 로고    scopus 로고
    • Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion
    • Antonyak M.A., Li B., Regan A.D., et al. Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion. J. Biol. Chem. 2009, 284:17914-17925.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17914-17925
    • Antonyak, M.A.1    Li, B.2    Regan, A.D.3
  • 15
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov S.S., Krylov D., Fleischman L.F., Belkin A.M. Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J. Cell. Biol. 2000, 148:825-838.
    • (2000) J. Cell. Biol. , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 16
    • 79955692581 scopus 로고    scopus 로고
    • Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes
    • Zemskov E.A., Mikhailenko I., Hsia R.-C., et al. Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes. PLoS ONE. 2011, 6:e19414.
    • (2011) PLoS ONE. , vol.6
    • Zemskov, E.A.1    Mikhailenko, I.2    Hsia, R.-C.3
  • 17
    • 35548939792 scopus 로고    scopus 로고
    • Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1
    • Zemskov E.A., Mikhailenko I., Strickland D.K., Belkin A.M. Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. J. Cell Sci. 2007, 120:3188-3199.
    • (2007) J. Cell Sci. , vol.120 , pp. 3188-3199
    • Zemskov, E.A.1    Mikhailenko, I.2    Strickland, D.K.3    Belkin, A.M.4
  • 18
    • 26844569694 scopus 로고    scopus 로고
    • PixFRET, an ImageJ plug-in for FRET calculation that can accommodate variations in spectral bleed-throughs
    • Feige J.N., Sage D., Wahli W., et al. PixFRET, an ImageJ plug-in for FRET calculation that can accommodate variations in spectral bleed-throughs. Microsc. Res. Tech. 2005, 68:51-58.
    • (2005) Microsc. Res. Tech. , vol.68 , pp. 51-58
    • Feige, J.N.1    Sage, D.2    Wahli, W.3
  • 19
    • 84860478831 scopus 로고    scopus 로고
    • Transglutaminase 2 is secreted from smooth muscle cells by transamidation-dependent microparticle formation
    • Van den Akker J., Van Weert A., Afink G., et al. Transglutaminase 2 is secreted from smooth muscle cells by transamidation-dependent microparticle formation. Amino Acids 2011, 42:961-973.
    • (2011) Amino Acids , vol.42 , pp. 961-973
    • Van den Akker, J.1    Van Weert, A.2    Afink, G.3
  • 20
    • 33751071631 scopus 로고    scopus 로고
    • Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2
    • Keresztessy Z., Csosz E., Harsfalvi J., et al. Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2. Protein Sci. 2006, 15:2466-2480.
    • (2006) Protein Sci. , vol.15 , pp. 2466-2480
    • Keresztessy, Z.1    Csosz, E.2    Harsfalvi, J.3
  • 21
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • Truong K., Ikura M. The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr. Opin. Struct. Biol. 2001, 11:573-578.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 22
    • 60049098220 scopus 로고    scopus 로고
    • Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress
    • Jeong E.M., Kim C.W., Cho S.Y., et al. Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress. FEBS Lett. 2009, 583:648-654.
    • (2009) FEBS Lett. , vol.583 , pp. 648-654
    • Jeong, E.M.1    Kim, C.W.2    Cho, S.Y.3
  • 23
    • 0026018479 scopus 로고
    • Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases
    • Gentile V., Saydak M., Chiocca E.A., et al. Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases. J. Biol. Chem. 1991, 266:478-483.
    • (1991) J. Biol. Chem. , vol.266 , pp. 478-483
    • Gentile, V.1    Saydak, M.2    Chiocca, E.A.3
  • 24
    • 14044258854 scopus 로고    scopus 로고
    • Lack of 'tissue' transglutaminase protein cross-linking leads to leakage of macromolecules from dying cells: relationship to development of autoimmunity in MRLIpr/Ipr mice
    • Piredda L., Amendola A., Colizzi V., et al. Lack of 'tissue' transglutaminase protein cross-linking leads to leakage of macromolecules from dying cells: relationship to development of autoimmunity in MRLIpr/Ipr mice. Cell Death Differ. 1997, 4:463-472.
    • (1997) Cell Death Differ. , vol.4 , pp. 463-472
    • Piredda, L.1    Amendola, A.2    Colizzi, V.3
  • 25
    • 0038641718 scopus 로고    scopus 로고
    • Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity
    • Nicholas B., Smethurst P., Verderio E., et al. Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity. Biochem. J. 2003, 371:413-422.
    • (2003) Biochem. J. , vol.371 , pp. 413-422
    • Nicholas, B.1    Smethurst, P.2    Verderio, E.3
  • 26
    • 19944428556 scopus 로고    scopus 로고
    • Tissue transglutaminase is a multifunctional BH3-only protein
    • Rodolfo C., Mormone E., Matarrese P., et al. Tissue transglutaminase is a multifunctional BH3-only protein. J. Biol. Chem. 2004, 279:54783-54792.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54783-54792
    • Rodolfo, C.1    Mormone, E.2    Matarrese, P.3
  • 27
    • 30644459554 scopus 로고    scopus 로고
    • Tissue transglutaminase serves as an inhibitor of apoptosis by cross-linking caspase 3 in thapsigargin-treated cells
    • Yamaguchi H., Wang H.G. Tissue transglutaminase serves as an inhibitor of apoptosis by cross-linking caspase 3 in thapsigargin-treated cells. Mol. Cell. Biol. 2006, 26:569-579.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 569-579
    • Yamaguchi, H.1    Wang, H.G.2
  • 28
    • 77954682668 scopus 로고    scopus 로고
    • Characterization of transglutaminase type II role in dendritic cell differentiation and function
    • Matic I., Sacchi A., Rinaldi A., et al. Characterization of transglutaminase type II role in dendritic cell differentiation and function. J. Leukoc. Biol. 2010, 88:181-188.
    • (2010) J. Leukoc. Biol. , vol.88 , pp. 181-188
    • Matic, I.1    Sacchi, A.2    Rinaldi, A.3
  • 29
    • 79251589371 scopus 로고    scopus 로고
    • Presence of tissue transglutaminase in granular endoplasmic reticulum is characteristic of melanized neurons in Parkinson's disease brain
    • Wilhelmus M.M., Verhaar R., Andringa G., et al. Presence of tissue transglutaminase in granular endoplasmic reticulum is characteristic of melanized neurons in Parkinson's disease brain. Brain. Pathol. 2011, 21:130-139.
    • (2011) Brain. Pathol. , vol.21 , pp. 130-139
    • Wilhelmus, M.M.1    Verhaar, R.2    Andringa, G.3


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