메뉴 건너뛰기




Volumn 1783, Issue 10, 2008, Pages 2001-2012

Cytosolic prion protein is the predominant anti-Bax prion protein form: Exclusion of transmembrane and secreted prion protein forms in the anti-Bax function

Author keywords

Apoptosis; Bax; Cytosolic prion protein; Neuroprotection; Prion; Secreted prion protein; Transmembrane prion protein

Indexed keywords

GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN; PRION PROTEIN; PROTEASOME; PROTEIN BAX;

EID: 50849114500     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.05.022     Document Type: Article
Times cited : (15)

References (67)
  • 2
    • 12844257374 scopus 로고    scopus 로고
    • Cellular prion protein neuroprotective function: implications in prion diseases
    • Roucou X., and LeBlanc A.C. Cellular prion protein neuroprotective function: implications in prion diseases. J. Mol. Med 83 (2005) 3-11
    • (2005) J. Mol. Med , vol.83 , pp. 3-11
    • Roucou, X.1    LeBlanc, A.C.2
  • 3
    • 34249936265 scopus 로고    scopus 로고
    • The cellular prion protein (PrP(C)): its physiological function and role in disease
    • Westergard L., Christensen H.M., and Harris D.A. The cellular prion protein (PrP(C)): its physiological function and role in disease. Biochim. Biophys. Acta 1772 (2007) 629-644
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 629-644
    • Westergard, L.1    Christensen, H.M.2    Harris, D.A.3
  • 4
    • 8644289373 scopus 로고    scopus 로고
    • Upregulation of cellular prion protein (PrPc) after focal cerebral ischemia and influence of lesion severity
    • Weise J., Crome O., Sandau R., Schulz-Schaeffer W., Bahr M., and Zerr I. Upregulation of cellular prion protein (PrPc) after focal cerebral ischemia and influence of lesion severity. Neurosci. Lett 372 (2004) 146-150
    • (2004) Neurosci. Lett , vol.372 , pp. 146-150
    • Weise, J.1    Crome, O.2    Sandau, R.3    Schulz-Schaeffer, W.4    Bahr, M.5    Zerr, I.6
  • 9
    • 34548331735 scopus 로고    scopus 로고
    • Enhanced susceptibility of Prnp-deficient mice to kainate-induced seizures, neuronal apoptosis, and death: role of AMPA/kainate receptors
    • Rangel A., Burgaya F., Gavin R., Soriano E., Aguzzi A., and Del Rio J.A. Enhanced susceptibility of Prnp-deficient mice to kainate-induced seizures, neuronal apoptosis, and death: role of AMPA/kainate receptors. J. Neurosci Res 85 (2007) 2741-2755
    • (2007) J. Neurosci Res , vol.85 , pp. 2741-2755
    • Rangel, A.1    Burgaya, F.2    Gavin, R.3    Soriano, E.4    Aguzzi, A.5    Del Rio, J.A.6
  • 11
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • Brown D.R., and Besinger A. Prion protein expression and superoxide dismutase activity. Biochem. J 334 Pt 2 (1998) 423-429
    • (1998) Biochem. J , vol.334 , Issue.PART 2 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 13
    • 36349016768 scopus 로고    scopus 로고
    • Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death
    • Meslin F., Hamai A., Gao P., Jalil A., Cahuzac N., Chouaib S., and Mehrpour M. Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death. Cancer Res 67 (2007) 10910-10919
    • (2007) Cancer Res , vol.67 , pp. 10910-10919
    • Meslin, F.1    Hamai, A.2    Gao, P.3    Jalil, A.4    Cahuzac, N.5    Chouaib, S.6    Mehrpour, M.7
  • 15
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against Bax-mediated apoptosis
    • Bounhar Y., Zhang Y., Goodyer C.G., and LeBlanc A. Prion protein protects human neurons against Bax-mediated apoptosis. J. Biol. Chem 276 (2001) 39145-39149
    • (2001) J. Biol. Chem , vol.276 , pp. 39145-39149
    • Bounhar, Y.1    Zhang, Y.2    Goodyer, C.G.3    LeBlanc, A.4
  • 16
    • 21744447704 scopus 로고    scopus 로고
    • Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells
    • Roucou X., Giannopoulos P.N., Zhang Y., Jodoin J., Goodyer C.G., and LeBlanc A. Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells. Cell Death Differ 12 (2005) 783-795
    • (2005) Cell Death Differ , vol.12 , pp. 783-795
    • Roucou, X.1    Giannopoulos, P.N.2    Zhang, Y.3    Jodoin, J.4    Goodyer, C.G.5    LeBlanc, A.6
  • 19
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber B., Lin J., and Andrews D.W. Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 12 (2007) 897-911
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 20
    • 33751271909 scopus 로고    scopus 로고
    • Prion protein prevents Bax-mediated cell death in the absence of other Bcl-2 family members in Saccharomyces cerevisiae
    • Bounhar Y., Mann K.K., Roucou X., and LeBlanc A.C. Prion protein prevents Bax-mediated cell death in the absence of other Bcl-2 family members in Saccharomyces cerevisiae. FEMS Yeast Res 6 (2006) 1204-1212
    • (2006) FEMS Yeast Res , vol.6 , pp. 1204-1212
    • Bounhar, Y.1    Mann, K.K.2    Roucou, X.3    LeBlanc, A.C.4
  • 23
  • 25
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia Y., Horonchik L., Tzaban S., Yanai A., and Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. Embo J 20 (2001) 5383-5391
    • (2001) Embo J , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 26
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma J., and Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. U. S. A 98 (2001) 14955-14960
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 27
    • 0142135128 scopus 로고    scopus 로고
    • Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons
    • Roucou X., Guo Q., Zhang Y., Goodyer C.G., and LeBlanc A.C. Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons. J. Biol. Chem 278 (2003) 40877-40881
    • (2003) J. Biol. Chem , vol.278 , pp. 40877-40881
    • Roucou, X.1    Guo, Q.2    Zhang, Y.3    Goodyer, C.G.4    LeBlanc, A.C.5
  • 28
    • 10644267669 scopus 로고    scopus 로고
    • Protection from cytosolic prion protein toxicity by modulation of protein translocation
    • Rane N.S., Yonkovich J.L., and Hegde R.S. Protection from cytosolic prion protein toxicity by modulation of protein translocation. Embo J 23 (2004) 4550-4559
    • (2004) Embo J , vol.23 , pp. 4550-4559
    • Rane, N.S.1    Yonkovich, J.L.2    Hegde, R.S.3
  • 29
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi B., Stewart R.S., Adles C., Stewart L.R., Quaglio E., Biasini E., Fioriti L., Chiesa R., and Harris D.A. Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J. Biol. Chem 278 (2003) 21732-21743
    • (2003) J. Biol. Chem , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3    Stewart, L.R.4    Quaglio, E.5    Biasini, E.6    Fioriti, L.7    Chiesa, R.8    Harris, D.A.9
  • 30
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J., Wollmann R., and Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298 (2002) 1781-1785
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 31
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • Ma J., and Lindquist S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298 (2002) 1785-1788
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 32
    • 34248351522 scopus 로고    scopus 로고
    • Defective retrotranslocation causes loss of anti-Bax function in human familial prion protein mutants
    • Jodoin J., Laroche-Pierre S., Goodyer C.G., and LeBlanc A.C. Defective retrotranslocation causes loss of anti-Bax function in human familial prion protein mutants. J. Neurosci 27 (2007) 5081-5091
    • (2007) J. Neurosci , vol.27 , pp. 5081-5091
    • Jodoin, J.1    Laroche-Pierre, S.2    Goodyer, C.G.3    LeBlanc, A.C.4
  • 34
    • 0025120245 scopus 로고
    • Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein
    • Yost C.S., Lopez C.D., Prusiner S.B., Myers R.M., and Lingappa V.R. Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein. Nature 343 (1990) 669-672
    • (1990) Nature , vol.343 , pp. 669-672
    • Yost, C.S.1    Lopez, C.D.2    Prusiner, S.B.3    Myers, R.M.4    Lingappa, V.R.5
  • 35
    • 0035854696 scopus 로고    scopus 로고
    • Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain
    • Kim S.J., Rahbar R., and Hegde R.S. Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain. J. Biol. Chem 276 (2001) 26132-26140
    • (2001) J. Biol. Chem , vol.276 , pp. 26132-26140
    • Kim, S.J.1    Rahbar, R.2    Hegde, R.S.3
  • 36
    • 4644357445 scopus 로고    scopus 로고
    • Signal sequences influence membrane integration of the prion protein
    • Ott C.M., and Lingappa V.R. Signal sequences influence membrane integration of the prion protein. Biochemistry 43 (2004) 11973-11982
    • (2004) Biochemistry , vol.43 , pp. 11973-11982
    • Ott, C.M.1    Lingappa, V.R.2
  • 38
    • 0032113448 scopus 로고    scopus 로고
    • Regulation of protein topology by trans-acting factors at the endoplasmic reticulum
    • Hegde R.S., Voigt S., and Lingappa V.R. Regulation of protein topology by trans-acting factors at the endoplasmic reticulum. Mol. Cell 2 (1998) 85-91
    • (1998) Mol. Cell , vol.2 , pp. 85-91
    • Hegde, R.S.1    Voigt, S.2    Lingappa, V.R.3
  • 39
    • 0032904215 scopus 로고    scopus 로고
    • Regulation of protein biogenesis at the endoplasmic reticulum membrane
    • Hegde R.S., and Lingappa V.R. Regulation of protein biogenesis at the endoplasmic reticulum membrane. Trends Cell Biol 9 (1999) 132-137
    • (1999) Trends Cell Biol , vol.9 , pp. 132-137
    • Hegde, R.S.1    Lingappa, V.R.2
  • 40
    • 33645239807 scopus 로고    scopus 로고
    • Cell-specific metabolism and pathogenesis of transmembrane prion protein
    • Gu Y., Luo X., Basu S., Fujioka H., and Singh N. Cell-specific metabolism and pathogenesis of transmembrane prion protein. Mol. Cell Biol 26 (2006) 2697-2715
    • (2006) Mol. Cell Biol , vol.26 , pp. 2697-2715
    • Gu, Y.1    Luo, X.2    Basu, S.3    Fujioka, H.4    Singh, N.5
  • 41
    • 41149144037 scopus 로고    scopus 로고
    • Pathogenic mutations in the glycosylphosphatidylinositol signal peptide of PrP modulate its topology in neuroblastoma cells
    • Gu Y., Singh A., Bose S., and Singh N. Pathogenic mutations in the glycosylphosphatidylinositol signal peptide of PrP modulate its topology in neuroblastoma cells. Mol. Cell Neurosci 37 (2008) 647-656
    • (2008) Mol. Cell Neurosci , vol.37 , pp. 647-656
    • Gu, Y.1    Singh, A.2    Bose, S.3    Singh, N.4
  • 43
    • 0025837194 scopus 로고
    • Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system
    • Rogers M., Serban D., Gyuris T., Scott M., Torchia T., and Prusiner S.B. Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system. J. Immunol 147 (1991) 3568-3574
    • (1991) J. Immunol , vol.147 , pp. 3568-3574
    • Rogers, M.1    Serban, D.2    Gyuris, T.3    Scott, M.4    Torchia, T.5    Prusiner, S.B.6
  • 44
    • 0022529448 scopus 로고
    • Monoclonal antibodies to the cellular and scrapie prion proteins
    • Barry R.A., and Prusiner S.B. Monoclonal antibodies to the cellular and scrapie prion proteins. J. Infect Dis 154 (1986) 518-521
    • (1986) J. Infect Dis , vol.154 , pp. 518-521
    • Barry, R.A.1    Prusiner, S.B.2
  • 45
    • 0024436502 scopus 로고
    • Directional antisense and sense cDNA cloning using Epstein-Barr virus episomal expression vectors
    • Groger R.K., Morrow D.M., and Tykocinski M.L. Directional antisense and sense cDNA cloning using Epstein-Barr virus episomal expression vectors. Gene 81 (1989) 285-294
    • (1989) Gene , vol.81 , pp. 285-294
    • Groger, R.K.1    Morrow, D.M.2    Tykocinski, M.L.3
  • 46
    • 0029609021 scopus 로고
    • Increased production of 4 kDa amyloid beta peptide in serum deprived human primary neuron cultures: possible involvement of apoptosis
    • LeBlanc A. Increased production of 4 kDa amyloid beta peptide in serum deprived human primary neuron cultures: possible involvement of apoptosis. J. Neurosci 15 (1995) 7837-7846
    • (1995) J. Neurosci , vol.15 , pp. 7837-7846
    • LeBlanc, A.1
  • 47
    • 0029860523 scopus 로고    scopus 로고
    • Amyloid ß peptide of Alzheimer's disease downregulates Bcl-2 and upregulates Bax expression in human neurons
    • Paradis E., Douillard H., Koutroumanis M., Goodyer C., and LeBlanc A. Amyloid ß peptide of Alzheimer's disease downregulates Bcl-2 and upregulates Bax expression in human neurons. J. Neurosci 16 (1996) 7533-7539
    • (1996) J. Neurosci , vol.16 , pp. 7533-7539
    • Paradis, E.1    Douillard, H.2    Koutroumanis, M.3    Goodyer, C.4    LeBlanc, A.5
  • 48
    • 0004167302 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Harlow E., and Lane D. Using Antibodies Vol. 1 (1999), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (1999) Using Antibodies , vol.1
    • Harlow, E.1    Lane, D.2
  • 50
    • 34249672143 scopus 로고    scopus 로고
    • Specific features of the prion protein transmembrane domain regulate nascent chain orientation
    • Ott C.M., Akhavan A., and Lingappa V.R. Specific features of the prion protein transmembrane domain regulate nascent chain orientation. J. Biol. Chem 282 (2007) 11163-11171
    • (2007) J. Biol. Chem , vol.282 , pp. 11163-11171
    • Ott, C.M.1    Akhavan, A.2    Lingappa, V.R.3
  • 51
    • 0035918202 scopus 로고    scopus 로고
    • Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus
    • Holscher C., Bach U.C., and Dobberstein B. Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus. J. Biol. Chem 276 (2001) 13388-13394
    • (2001) J. Biol. Chem , vol.276 , pp. 13388-13394
    • Holscher, C.1    Bach, U.C.2    Dobberstein, B.3
  • 55
    • 0033576323 scopus 로고    scopus 로고
    • Transmissible and genetic prion diseases share a common pathway of neurodegeneration
    • Hegde R.S., Tremblay P., Groth D., DeArmond S.J., Prusiner S.B., and Lingappa V.R. Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 402 (1999) 822-826
    • (1999) Nature , vol.402 , pp. 822-826
    • Hegde, R.S.1    Tremblay, P.2    Groth, D.3    DeArmond, S.J.4    Prusiner, S.B.5    Lingappa, V.R.6
  • 56
    • 0036854303 scopus 로고    scopus 로고
    • Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel
    • Kim S.J., and Hegde R.S. Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel. Mol. Biol. Cell 13 (2002) 3775-3786
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3775-3786
    • Kim, S.J.1    Hegde, R.S.2
  • 57
    • 0035158658 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic reticulum
    • Stewart R.S., Drisaldi B., and Harris D.A. A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic reticulum. Mol. Biol. Cell 12 (2001) 881-889
    • (2001) Mol. Biol. Cell , vol.12 , pp. 881-889
    • Stewart, R.S.1    Drisaldi, B.2    Harris, D.A.3
  • 58
    • 33846133296 scopus 로고    scopus 로고
    • The role of lipids in the biogenesis of integral membrane proteins
    • Schneiter R., and Toulmay A. The role of lipids in the biogenesis of integral membrane proteins. Appl Microbiol Biotechnol 73 (2007) 1224-1232
    • (2007) Appl Microbiol Biotechnol , vol.73 , pp. 1224-1232
    • Schneiter, R.1    Toulmay, A.2
  • 59
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • Fons R.D., Bogert B.A., and Hegde R.S. Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J. Cell Biol 160 (2003) 529-539
    • (2003) J. Cell Biol , vol.160 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 60
    • 0242424148 scopus 로고    scopus 로고
    • A complex of chaperones and disulfide isomerases occludes the cytosolic face of the translocation protein Sec61p and affects translocation of the prion protein
    • Stockton J.D., Merkert M.C., and Kellaris K.V. A complex of chaperones and disulfide isomerases occludes the cytosolic face of the translocation protein Sec61p and affects translocation of the prion protein. Biochemistry 42 (2003) 12821-12834
    • (2003) Biochemistry , vol.42 , pp. 12821-12834
    • Stockton, J.D.1    Merkert, M.C.2    Kellaris, K.V.3
  • 61
    • 0028911161 scopus 로고
    • The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system
    • Kurschner C., and Morgan J.I. The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system. Brain Res. Mol. Brain Res 30 (1995) 165-168
    • (1995) Brain Res. Mol. Brain Res , vol.30 , pp. 165-168
    • Kurschner, C.1    Morgan, J.I.2
  • 62
    • 0029932071 scopus 로고    scopus 로고
    • Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein.
    • Kurschner C., and Morgan J. Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein. Mol. Br. Res 37 (1996) 249-258
    • (1996) Mol. Br. Res , vol.37 , pp. 249-258
    • Kurschner, C.1    Morgan, J.2
  • 63
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai Z.N., Milliman C.L., and Korsmeyer S.J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74 (1993) 609-619
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 65
    • 33947118714 scopus 로고    scopus 로고
    • Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression
    • Liao H.J., and Carpenter G. Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression. Mol. Biol. Cell 18 (2007) 1064-1072
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1064-1072
    • Liao, H.J.1    Carpenter, G.2
  • 67
    • 18144422732 scopus 로고    scopus 로고
    • p97 Is in a complex with cholera toxin and influences the transport of cholera toxin and related toxins to the cytoplasm
    • Abujarour R.J., Dalal S., Hanson P.I., and Draper R.K. p97 Is in a complex with cholera toxin and influences the transport of cholera toxin and related toxins to the cytoplasm. J. Biol. Chem 280 (2005) 15865-15871
    • (2005) J. Biol. Chem , vol.280 , pp. 15865-15871
    • Abujarour, R.J.1    Dalal, S.2    Hanson, P.I.3    Draper, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.