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Volumn 36, Issue 2, 2016, Pages

Development of a stable ERroGFP variant suitable for monitoring redox dynamics in the ER

Author keywords

Endoplasmic reticulum (ER) redox state; Glutathione; Protein quality control; Redox probe

Indexed keywords

GREEN FLUORESCENT PROTEIN; PROTEIN VARIANT; RECOMBINANT PROTEIN;

EID: 84964607483     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20160027     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • CrossRef PubMed
    • Ellgaard, L. and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191 CrossRef PubMed
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 2
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • PubMed
    • Hetz, C. (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89-102 PubMed
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 3
    • 84921901605 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in human pathology
    • CrossRef PubMed
    • Oakes, S.A. and Papa, F.R. (2015) The role of endoplasmic reticulum stress in human pathology. Annu. Rev. Pathol. 10, 173-194 CrossRef PubMed
    • (2015) Annu. Rev. Pathol. , vol.10 , pp. 173-194
    • Oakes, S.A.1    Papa, F.R.2
  • 4
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • CrossRef PubMed
    • Hwang, C., Sinskey, A.J. and Lodish, H.F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502 CrossRef PubMed
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 5
    • 84857530189 scopus 로고    scopus 로고
    • The protein disulfide isomerase family: Key players in health and disease
    • CrossRef PubMed
    • Benham, A.M. (2012) The protein disulfide isomerase family: key players in health and disease. Antioxid. Redox Signal. 16, 781-789 CrossRef PubMed
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 781-789
    • Benham, A.M.1
  • 6
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • CrossRef PubMed
    • Ushioda, R., Hoseki, J., Araki, K., Jansen, G., Thomas, D.Y. and Nagata, K. (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569-572 CrossRef PubMed
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 7
    • 79951491416 scopus 로고    scopus 로고
    • Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5
    • CrossRef PubMed
    • Hagiwara, M., Maegawa, K., Suzuki, M., Ushioda, R., Araki, K., Matsumoto, Y., Hoseki, J., Nagata, K. and Inaba, K. (2011) Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5. Mol. Cell 41, 432-444 CrossRef PubMed
    • (2011) Mol. Cell , vol.41 , pp. 432-444
    • Hagiwara, M.1    Maegawa, K.2    Suzuki, M.3    Ushioda, R.4    Araki, K.5    Matsumoto, Y.6    Hoseki, J.7    Nagata, K.8    Inaba, K.9
  • 8
    • 84885647401 scopus 로고    scopus 로고
    • Glycosylation-independent ERAD pathway serves as a backup system under ER stress
    • CrossRef PubMed
    • Ushioda, R., Hoseki, J. and Nagata, K. (2013) Glycosylation-independent ERAD pathway serves as a backup system under ER stress. Mol. Biol. Cell 24, 3155-3163 CrossRef PubMed
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3155-3163
    • Ushioda, R.1    Hoseki, J.2    Nagata, K.3
  • 9
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • CrossRef PubMed
    • Schafer, F.Q. and Buettner, G.R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30, 1191-1212 CrossRef PubMed
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 10
    • 79952808113 scopus 로고    scopus 로고
    • Glutathione-and non-glutathione-based oxidant control in the endoplasmic reticulum
    • CrossRef PubMed
    • Appenzeller-Herzog, C. (2011) Glutathione-and non-glutathione-based oxidant control in the endoplasmic reticulum. J. Cell Sci. 124, 847-855 CrossRef PubMed
    • (2011) J. Cell Sci. , vol.124 , pp. 847-855
    • Appenzeller-Herzog, C.1
  • 11
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • CrossRef PubMed
    • Cuozzo, J.W. and Kaiser, C.A. (1999) Competition between glutathione and protein thiols for disulphide-bond formation. Nat. Cell Biol. 1, 130-135 CrossRef PubMed
    • (1999) Nat. Cell Biol. , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 13
    • 11244319355 scopus 로고    scopus 로고
    • Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells
    • CrossRef PubMed
    • Jessop, C.E. and Bulleid, N.J. (2004) Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. J. Biol. Chem. 279, 55341-55347 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 55341-55347
    • Jessop, C.E.1    Bulleid, N.J.2
  • 14
    • 84905170031 scopus 로고    scopus 로고
    • Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants
    • CrossRef PubMed
    • Tsunoda, S., Avezov, E., Zyryanova, A., Konno, T., Mendes-Silva, L., Pinho Melo, E., Harding, H.P. and Ron, D. (2014) Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants. Elife 3, e03421 CrossRef PubMed
    • (2014) Elife , vol.3
    • Tsunoda, S.1    Avezov, E.2    Zyryanova, A.3    Konno, T.4    Mendes-Silva, L.5    Pinho Melo, E.6    Harding, H.P.7    Ron, D.8
  • 15
    • 39749200944 scopus 로고    scopus 로고
    • Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation
    • CrossRef PubMed
    • Dixon, B.M., Heath, S.H., Kim, R., Suh, J.H. and Hagen, T.M. (2008) Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation. Antioxid. Redox Signal. 10, 963-972 CrossRef PubMed
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 963-972
    • Dixon, B.M.1    Heath, S.H.2    Kim, R.3    Suh, J.H.4    Hagen, T.M.5
  • 16
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • CrossRef PubMed
    • Hanson, G.T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R.A., Tsien, R.Y. and Remington, S.J. (2004) Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J. Biol. Chem. 279, 13044-13053 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbee, D.3    Cannon, M.4    Capaldi, R.A.5    Tsien, R.Y.6    Remington, S.J.7
  • 17
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • CrossRef PubMed
    • Dooley, C.T., Dore, T.M., Hanson, G.T., Jackson, W.C., Remington, S.J. and Tsien, R.Y. (2004) Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J. Biol. Chem. 279, 22284-22293 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 22284-22293
    • Dooley, C.T.1    Dore, T.M.2    Hanson, G.T.3    Jackson, W.C.4    Remington, S.J.5    Tsien, R.Y.6
  • 18
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • CrossRef PubMed
    • Merksamer, P.I., Trusina, A. and Papa, F.R. (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135, 933-947 CrossRef PubMed
    • (2008) Cell , vol.135 , pp. 933-947
    • Merksamer, P.I.1    Trusina, A.2    Papa, F.R.3
  • 19
    • 49749114828 scopus 로고    scopus 로고
    • Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments
    • CrossRef
    • Lohman, J.R. and Remington, S.J. (2008) Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments. Biochemistry (Mosc) 47, 8678-8688 CrossRef
    • (2008) Biochemistry (Mosc) , vol.47 , pp. 8678-8688
    • Lohman, J.R.1    Remington, S.J.2
  • 22
    • 79960420766 scopus 로고    scopus 로고
    • Real-time monitoring of redox changes in the mammalian endoplasmic reticulum
    • CrossRef PubMed
    • van Lith, M., Tiwari, S., Pediani, J., Milligan, G. and Bulleid, N.J. (2011) Real-time monitoring of redox changes in the mammalian endoplasmic reticulum. J. Cell Sci. 124, 2349-2356 CrossRef PubMed
    • (2011) J. Cell Sci. , vol.124 , pp. 2349-2356
    • Van Lith, M.1    Tiwari, S.2    Pediani, J.3    Milligan, G.4    Bulleid, N.J.5
  • 23
    • 77950501289 scopus 로고    scopus 로고
    • Monitoring intracellular redox conditions in the endoplasmic reticulum of living yeasts
    • CrossRef PubMed
    • Delic, M., Mattanovich, D. and Gasser, B. (2010) Monitoring intracellular redox conditions in the endoplasmic reticulum of living yeasts. FEMS Microbiol. Lett. 306, 61-66 CrossRef PubMed
    • (2010) FEMS Microbiol. Lett. , vol.306 , pp. 61-66
    • Delic, M.1    Mattanovich, D.2    Gasser, B.3
  • 24
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • CrossRef PubMed
    • Pedelacq, J.D., Cabantous, S., Tran, T., Terwilliger, T.C. and Waldo, G.S. (2006) Engineering and characterization of a superfolder green fluorescent protein. Nat. Biotechnol. 24, 79-88 CrossRef PubMed
    • (2006) Nat. Biotechnol. , vol.24 , pp. 79-88
    • Pedelacq, J.D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 25
    • 1642413540 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+/Akita pancreatic beta cells
    • CrossRef PubMed
    • Nozaki, J., Kubota, H., Yoshida, H., Naitoh, M., Goji, J., Yoshinaga, T., Mori, K., Koizumi, A. and Nagata, K. (2004) The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+/Akita pancreatic beta cells. Genes Cells 9, 261-270 CrossRef PubMed
    • (2004) Genes Cells , vol.9 , pp. 261-270
    • Nozaki, J.1    Kubota, H.2    Yoshida, H.3    Naitoh, M.4    Goji, J.5    Yoshinaga, T.6    Mori, K.7    Koizumi, A.8    Nagata, K.9
  • 26
    • 28244481417 scopus 로고    scopus 로고
    • Proinsulin lacking the A7-B7 disulfide bond, Ins2Akita, tends to aggregate due to the exposed hydrophobic surface
    • CrossRef PubMed
    • Yoshinaga, T., Nakatome, K., Nozaki, J.I., Naitoh, M., Hoseki, J., Kubota, H., Nagata, K. and Koizumi, A. (2005) Proinsulin lacking the A7-B7 disulfide bond, Ins2Akita, tends to aggregate due to the exposed hydrophobic surface. Biol. Chem. 386, 1077-1085 CrossRef PubMed
    • (2005) Biol. Chem. , vol.386 , pp. 1077-1085
    • Yoshinaga, T.1    Nakatome, K.2    Nozaki, J.I.3    Naitoh, M.4    Hoseki, J.5    Kubota, H.6    Nagata, K.7    Koizumi, A.8
  • 27
    • 0032918044 scopus 로고    scopus 로고
    • A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse
    • CrossRef PubMed
    • Wang, J., Takeuchi, T., Tanaka, S., Kubo, S.K., Kayo, T., Lu, D., Takata, K., Koizumi, A. and Izumi, T. (1999) A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse. J. Clin. Invest. 103, 27-37 CrossRef PubMed
    • (1999) J. Clin. Invest. , vol.103 , pp. 27-37
    • Wang, J.1    Takeuchi, T.2    Tanaka, S.3    Kubo, S.K.4    Kayo, T.5    Lu, D.6    Takata, K.7    Koizumi, A.8    Izumi, T.9
  • 28
    • 31044452359 scopus 로고    scopus 로고
    • Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
    • CrossRef PubMed
    • Gross, E., Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C. and Fass, D. (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc. Natl. Acad. Sci. U.S.A. 103, 299-304 CrossRef PubMed
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 299-304
    • Gross, E.1    Sevier, C.S.2    Heldman, N.3    Vitu, E.4    Bentzur, M.5    Kaiser, C.A.6    Thorpe, C.7    Fass, D.8
  • 29
    • 58649096169 scopus 로고    scopus 로고
    • Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase
    • CrossRef PubMed
    • Wang, L., Li, S.J., Sidhu, A., Zhu, L., Liang, Y., Freedman, R.B. and Wang, C.C. (2009) Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase. J. Biol. Chem. 284, 199-206 CrossRef PubMed
    • (2009) J. Biol. Chem. , vol.284 , pp. 199-206
    • Wang, L.1    Li, S.J.2    Sidhu, A.3    Zhu, L.4    Liang, Y.5    Freedman, R.B.6    Wang, C.C.7
  • 31
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • CrossRef PubMed
    • Harding, H.P., Zhang, Y., Zeng, H., Novoa, I., Lu, P.D., Calfon, M., Sadri, N., Yun, C., Popko, B., Paules, R. et al. (2003) An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11, 619-633 CrossRef PubMed
    • (2003) Mol. Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5    Calfon, M.6    Sadri, N.7    Yun, C.8    Popko, B.9    Paules, R.10
  • 33
    • 84920441264 scopus 로고    scopus 로고
    • Altered intracellular calcium homeostasis and endoplasmic reticulum redox state in Saccharomyces cerevisiae cells lacking Grx6 glutaredoxin
    • CrossRef PubMed
    • Puigpinos, J., Casas, C. and Herrero, E. (2015) Altered intracellular calcium homeostasis and endoplasmic reticulum redox state in Saccharomyces cerevisiae cells lacking Grx6 glutaredoxin. Mol. Biol. Cell 26, 104-116 CrossRef PubMed
    • (2015) Mol. Biol. Cell , vol.26 , pp. 104-116
    • Puigpinos, J.1    Casas, C.2    Herrero, E.3
  • 34
    • 84899139079 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-activated transcription factor ATF6alpha requires the disulfide isomerase PDIA5 to modulate chemoresistance
    • CrossRef PubMed
    • Higa, A., Taouji, S., Lhomond, S., Jensen, D., Fernandez-Zapico, M.E., Simpson, J.C., Pasquet, J.M., Schekman, R. and Chevet, E. (2014) Endoplasmic reticulum stress-activated transcription factor ATF6alpha requires the disulfide isomerase PDIA5 to modulate chemoresistance. Mol. Cell. Biol. 34, 1839-1849 CrossRef PubMed
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 1839-1849
    • Higa, A.1    Taouji, S.2    Lhomond, S.3    Jensen, D.4    Fernandez-Zapico, M.E.5    Simpson, J.C.6    Pasquet, J.M.7    Schekman, R.8    Chevet, E.9
  • 35
    • 84894236302 scopus 로고    scopus 로고
    • Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling via disulfide-dependent association
    • CrossRef PubMed
    • Eletto, D., Dersh, D., Gidalevitz, T. and Argon, Y. (2014) Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling via disulfide-dependent association. Mol. Cell 53, 562-576 CrossRef PubMed
    • (2014) Mol. Cell , vol.53 , pp. 562-576
    • Eletto, D.1    Dersh, D.2    Gidalevitz, T.3    Argon, Y.4


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