메뉴 건너뛰기




Volumn 5, Issue 5, 2013, Pages 969-982

BiP negatively affects ricin transport

Author keywords

BiP; Endoplasmic reticulum; ER chaperones; Ricin; Toxicity; Toxin

Indexed keywords

GLUCOSE REGULATED PROTEIN 78; RICIN;

EID: 84878059355     PISSN: 20726651     EISSN: None     Source Type: Journal    
DOI: 10.3390/toxins5050969     Document Type: Article
Times cited : (8)

References (42)
  • 2
    • 0022536233 scopus 로고
    • Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas
    • Bole, D.G.; Hendershot, L.M.; Kearney, J.F. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J. Cell Biol. 1986, 102, 1558-1566
    • (1986) J. Cell Biol , vol.102 , pp. 1558-1566
    • Bole, D.G.1    Hendershot, L.M.2    Kearney, J.F.3
  • 3
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas, I.G.; Wabl, M. Immunoglobulin heavy chain binding protein. Nature 1983, 306, 387-389
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 4
    • 7444240833 scopus 로고    scopus 로고
    • The er function bip is a master regulator of er function
    • Hendershot, L.M. The er function bip is a master regulator of er function. Mount Sinai J. Med. N. Y. 2004, 71, 289-297
    • (2004) Mount Sinai J. Med. N. Y , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 5
    • 77953127589 scopus 로고    scopus 로고
    • Protein toxins from plants and bacteria: Probes for intracellular transport and tools in medicine
    • Sandvig, K.; Torgersen, M.L.; Engedal, N.; Skotland, T.; Iversen, T.G. Protein toxins from plants and bacteria: Probes for intracellular transport and tools in medicine. FEBS Lett. 2010, 584, 2626-2634
    • (2010) FEBS Lett , vol.584 , pp. 2626-2634
    • Sandvig, K.1    Torgersen, M.L.2    Engedal, N.3    Skotland, T.4    Iversen, T.G.5
  • 8
    • 84857880542 scopus 로고    scopus 로고
    • How ricin and shiga toxin reach the cytosol of target cells: Retrotranslocation from the endoplasmic reticulum
    • Spooner, R.A.; Lord, J.M. How ricin and shiga toxin reach the cytosol of target cells: Retrotranslocation from the endoplasmic reticulum. Curr. Top. Microbiol. Immunol. 2012, 357, 19-40
    • (2012) Curr. Top. Microbiol. Immunol , vol.357 , pp. 19-40
    • Spooner, R.A.1    Lord, J.M.2
  • 10
    • 77955106651 scopus 로고    scopus 로고
    • Folding-competent and folding-defective forms of ricin a chain have different fates after retrotranslocation from the endoplasmic reticulum
    • Li, S.; Spooner, R.A.; Allen, S.C.; Guise, C.P.; Ladds, G.; Schnoder, T.; Schmitt, M.J.; Lord, J.M.; Roberts, L.M. Folding-competent and folding-defective forms of ricin a chain have different fates after retrotranslocation from the endoplasmic reticulum. Mol. Biol. Cell 2010, 21, 2543-2554
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2543-2554
    • Li, S.1    Spooner, R.A.2    Allen, S.C.3    Guise, C.P.4    Ladds, G.5    Schnoder, T.6    Schmitt, M.J.7    Lord, J.M.8    Roberts, L.M.9
  • 11
    • 0033607688 scopus 로고    scopus 로고
    • Dependence of ricin toxicity on translocation of the toxin a-chain from the endoplasmic reticulum to the cytosol
    • Wesche, J.; Rapak, A.; Olsnes, S. Dependence of ricin toxicity on translocation of the toxin a-chain from the endoplasmic reticulum to the cytosol. J. Biol. Chem. 1999, 274, 34443-34449
    • (1999) J. Biol. Chem , vol.274 , pp. 34443-34449
    • Wesche, J.1    Rapak, A.2    Olsnes, S.3
  • 12
    • 33745395593 scopus 로고    scopus 로고
    • Edem is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol
    • Slominska-Wojewodzka, M.; Gregers, T.F.; Walchli, S.; Sandvig, K. Edem is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol. Mol. Biol. Cell 2006, 17, 1664-1675
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1664-1675
    • Slominska-Wojewodzka, M.1    Gregers, T.F.2    Walchli, S.3    Sandvig, K.4
  • 13
    • 79956042755 scopus 로고    scopus 로고
    • A single point mutation in ricin a-chain increases toxin degradation and inhibits edem1-dependent er retrotranslocation
    • Sokolowska, I.; Walchli, S.; Wegrzyn, G.; Sandvig, K.; Slominska-Wojewodzka, M. A single point mutation in ricin a-chain increases toxin degradation and inhibits edem1-dependent er retrotranslocation. Biochem. J. 2011, 436, 371-385
    • (2011) Biochem. J , vol.436 , pp. 371-385
    • Sokolowska, I.1    Walchli, S.2    Wegrzyn, G.3    Sandvig, K.4    Slominska-Wojewodzka, M.5
  • 14
    • 30344485142 scopus 로고    scopus 로고
    • Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: Co-opting basic mechanisms of endoplasmic reticulum-associated degradation
    • Lord, J.M.; Roberts, L.M.; Lencer, W.I. Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: Co-opting basic mechanisms of endoplasmic reticulum-associated degradation. Curr. Top. Microbiol. Immunol. 2005, 300, 149-168
    • (2005) Curr. Top. Microbiol. Immunol , vol.300 , pp. 149-168
    • Lord, J.M.1    Roberts, L.M.2    Lencer, W.I.3
  • 16
    • 80051469646 scopus 로고    scopus 로고
    • Genome-wide rnai screens identify genes required for ricin and pe intoxications
    • Moreau, D.; Kumar, P.; Wang, S.C.; Chaumet, A.; Chew, S.Y.; Chevalley, H.; Bard, F. Genome-wide rnai screens identify genes required for ricin and pe intoxications. Dev. Cell 2011, 21, 231-244
    • (2011) Dev. Cell , vol.21 , pp. 231-244
    • Moreau, D.1    Kumar, P.2    Wang, S.C.3    Chaumet, A.4    Chew, S.Y.5    Chevalley, H.6    Bard, F.7
  • 17
    • 32544457086 scopus 로고    scopus 로고
    • Shiga toxin b-subunit binds to the chaperone bip and the nucleolar protein b23
    • Falguieres, T.; Johannes, L. Shiga toxin b-subunit binds to the chaperone bip and the nucleolar protein b23. Biol. Cell Auspices Eur. Cell Biol. Organ. 2006, 98, 125-134
    • (2006) Biol. Cell Auspices Eur. Cell Biol. Organ , vol.98 , pp. 125-134
    • Falguieres, T.1    Johannes, L.2
  • 18
    • 16244400431 scopus 로고    scopus 로고
    • Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone hedj/erdj3
    • Yu, M.; Haslam, D.B. Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone hedj/erdj3. Infect. Immun. 2005, 73, 2524-2532
    • (2005) Infect. Immun , vol.73 , pp. 2524-2532
    • Yu, M.1    Haslam, D.B.2
  • 19
    • 0242626544 scopus 로고    scopus 로고
    • Bip-dependent export of cholera toxin from endoplasmic reticulum-derived microsomes
    • Winkeler, A.; Godderz, D.; Herzog, V.; Schmitz, A. Bip-dependent export of cholera toxin from endoplasmic reticulum-derived microsomes. FEBS Lett. 2003, 554, 439-442
    • (2003) FEBS Lett , vol.554 , pp. 439-442
    • Winkeler, A.1    Godderz, D.2    Herzog, V.3    Schmitz, A.4
  • 20
    • 0037191074 scopus 로고    scopus 로고
    • Unfolded cholera toxin is transferred to the er membrane and released from protein disulfide isomerase upon oxidation by ero1
    • Tsai, B.; Rapoport, T.A. Unfolded cholera toxin is transferred to the er membrane and released from protein disulfide isomerase upon oxidation by ero1. J. Cell Biol. 2002, 159, 207-216
    • (2002) J. Cell Biol , vol.159 , pp. 207-216
    • Tsai, B.1    Rapoport, T.A.2
  • 21
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B.; Rodighiero, C.; Lencer, W.I.; Rapoport, T.A. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 2001, 104, 937-948
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 22
    • 80051923636 scopus 로고    scopus 로고
    • Grp78(bip) facilitates the cytosolic delivery of anthrax lethal factor (lf) in vivo and functions as an unfoldase in vitro
    • Tamayo, A.G.; Slater, L.; Taylor-Parker, J.; Bharti, A.; Harrison, R.; Hung, D.T.; Murphy, J.R. Grp78(bip) facilitates the cytosolic delivery of anthrax lethal factor (lf) in vivo and functions as an unfoldase in vitro. Mol. Microbiol. 2011, 81, 1390-1401
    • (2011) Mol. Microbiol , vol.81 , pp. 1390-1401
    • Tamayo, A.G.1    Slater, L.2    Taylor-Parker, J.3    Bharti, A.4    Harrison, R.5    Hung, D.T.6    Murphy, J.R.7
  • 23
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of atf6 to bip in the endoplasmic reticulum stress response
    • Shen, J.; Snapp, E.L.; Lippincott-Schwartz, J.; Prywes, R. Stable binding of atf6 to bip in the endoplasmic reticulum stress response. Mol. Cell. Biol. 2005, 25, 921-932
    • (2005) Mol. Cell. Biol , vol.25 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 24
    • 0030929658 scopus 로고    scopus 로고
    • Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol
    • Rapak, A.; Falnes, P.O.; Olsnes, S. Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol. Proc. Natl. Acad. Sci. USA 1997, 94, 3783-3788
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3783-3788
    • Rapak, A.1    Falnes, P.O.2    Olsnes, S.3
  • 25
    • 0028853568 scopus 로고
    • In vitro dissociation of bip-peptide complexes requires a conformational change in bip after atp binding but does not require atp hydrolysis
    • Wei, J.; Gaut, J.R.; Hendershot, L.M. In vitro dissociation of bip-peptide complexes requires a conformational change in bip after atp binding but does not require atp hydrolysis. J. Biol. Chem. 1995, 270, 26677-26682
    • (1995) J. Biol. Chem , vol.270 , pp. 26677-26682
    • Wei, J.1    Gaut, J.R.2    Hendershot, L.M.3
  • 26
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of bip and er stress transducers in the unfolded-protein response
    • Bertolotti, A.; Zhang, Y.; Hendershot, L.M.; Harding, H.P.; Ron, D. Dynamic interaction of bip and er stress transducers in the unfolded-protein response. Nat. Cell Biol. 2000, 2, 326-332
    • (2000) Nat. Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 27
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of atf6 senses endoplasmic reticulum (er) stress and causes translocation of atf6 from the er to the golgi
    • Chen, X.; Shen, J.; Prywes, R. The luminal domain of atf6 senses endoplasmic reticulum (er) stress and causes translocation of atf6 from the er to the golgi. J. Biol. Chem. 2002, 277, 13045-13052
    • (2002) J. Biol. Chem , vol.277 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 28
    • 0036069980 scopus 로고    scopus 로고
    • Er stress regulation of atf6 localization by dissociation of bip/grp78 binding and unmasking of golgi localization signals
    • Shen, J.; Chen, X.; Hendershot, L.; Prywes, R. Er stress regulation of atf6 localization by dissociation of bip/grp78 binding and unmasking of golgi localization signals. Dev. Cell 2002, 3, 99-111
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 29
    • 20444406124 scopus 로고    scopus 로고
    • Compensatory regulation among er chaperones in c
    • Kapulkin, W.J.; Hiester, B.G.; Link, C.D. Compensatory regulation among er chaperones in c. Elegans. FEBS Lett. 2005, 579, 3063-3068
    • (2005) Elegans. FEBS Lett , vol.579 , pp. 3063-3068
    • Kapulkin, W.J.1    Hiester, B.G.2    Link, C.D.3
  • 30
    • 36049042707 scopus 로고    scopus 로고
    • Reduction of grp78 expression with sirna activates unfolded protein response leading to apoptosis in hela cells
    • Suzuki, T.; Lu, J.; Zahed, M.; Kita, K.; Suzuki, N. Reduction of grp78 expression with sirna activates unfolded protein response leading to apoptosis in hela cells. Arch. Biochem. Biophys. 2007, 468, 1-14
    • (2007) Arch. Biochem. Biophys , vol.468 , pp. 1-14
    • Suzuki, T.1    Lu, J.2    Zahed, M.3    Kita, K.4    Suzuki, N.5
  • 31
    • 15944408402 scopus 로고    scopus 로고
    • Er stress signaling by regulated proteolysis of atf6
    • Shen, J.; Prywes, R. Er stress signaling by regulated proteolysis of atf6. Methods 2005, 35, 382-389
    • (2005) Methods , vol.35 , pp. 382-389
    • Shen, J.1    Prywes, R.2
  • 32
  • 35
    • 33746370728 scopus 로고    scopus 로고
    • The role of bip in endoplasmic reticulum-associated degradation of major histocompatibility complex class i heavy chain induced by cytomegalovirus proteins
    • Hegde, N.R.; Chevalier, M.S.; Wisner, T.W.; Denton, M.C.; Shire, K.; Frappier, L.; Johnson, D.C. The role of bip in endoplasmic reticulum-associated degradation of major histocompatibility complex class i heavy chain induced by cytomegalovirus proteins. J. Biol. Chem. 2006, 281, 20910-20919
    • (2006) J. Biol. Chem , vol.281 , pp. 20910-20919
    • Hegde, N.R.1    Chevalier, M.S.2    Wisner, T.W.3    Denton, M.C.4    Shire, K.5    Frappier, L.6    Johnson, D.C.7
  • 36
    • 4444317796 scopus 로고    scopus 로고
    • Antitoxins: Novel strategies to target agents of bioterrorism
    • Rainey, G.J.; Young, J.A. Antitoxins: Novel strategies to target agents of bioterrorism. Nat. Rev. Microbiol. 2004, 2, 721-726
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 721-726
    • Rainey, G.J.1    Young, J.A.2
  • 37
    • 25144493280 scopus 로고    scopus 로고
    • Preclinical toxicity and efficacy testing of rivax, a recombinant protein vaccine against ricin
    • Smallshaw, J.E.; Richardson, J.A.; Pincus, S.; Schindler, J.; Vitetta, E.S. Preclinical toxicity and efficacy testing of rivax, a recombinant protein vaccine against ricin. Vaccine 2005, 23, 4775-4784
    • (2005) Vaccine , vol.23 , pp. 4775-4784
    • Smallshaw, J.E.1    Richardson, J.A.2    Pincus, S.3    Schindler, J.4    Vitetta, E.S.5
  • 38
    • 34748918488 scopus 로고    scopus 로고
    • Rivax, a recombinant ricin subunit vaccine, protects mice against ricin delivered by gavage or aerosol
    • Smallshaw, J.E.; Richardson, J.A.; Vitetta, E.S. Rivax, a recombinant ricin subunit vaccine, protects mice against ricin delivered by gavage or aerosol. Vaccine 2007, 25, 7459-7469
    • (2007) Vaccine , vol.25 , pp. 7459-7469
    • Smallshaw, J.E.1    Richardson, J.A.2    Vitetta, E.S.3
  • 39
    • 33748309412 scopus 로고    scopus 로고
    • Immunotoxins for targeted cancer therapy
    • Kreitman, R.J. Immunotoxins for targeted cancer therapy. AAPS J. 2006, 8, E532-E551
    • (2006) AAPS J , vol.8
    • Kreitman, R.J.1
  • 40
    • 0034282912 scopus 로고    scopus 로고
    • Activation of atf6 and an atf6 DNA binding site by the endoplasmic reticulum stress response
    • Wang, Y.; Shen, J.; Arenzana, N.; Tirasophon, W.; Kaufman, R.J.; Prywes, R. Activation of atf6 and an atf6 DNA binding site by the endoplasmic reticulum stress response. J. Biol. Chem. 2000, 275, 27013-27020
    • (2000) J. Biol. Chem , vol.275 , pp. 27013-27020
    • Wang, Y.1    Shen, J.2    Arenzana, N.3    Tirasophon, W.4    Kaufman, R.J.5    Prywes, R.6
  • 41
    • 12744273521 scopus 로고    scopus 로고
    • Golgi vesiculation induced by cholesterol occurs by a dynamin- and cpla2-dependent mechanism
    • Grimmer, S.; Ying, M.; Walchli, S.; van Deurs, B.; Sandvig, K. Golgi vesiculation induced by cholesterol occurs by a dynamin- and cpla2-dependent mechanism. Traffic 2005, 6, 144-156
    • (2005) Traffic , vol.6 , pp. 144-156
    • Grimmer, S.1    Ying, M.2    Walchli, S.3    van Deurs, B.4    Sandvig, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.