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Volumn 1828, Issue 12, 2013, Pages 2801-2807

The site-2 protease

(1)  Rawson, Robert B a  

a NONE

Author keywords

ER stress; Regulated intramembrane proteolysis; Rip; S2P; Site 2 protease; SREBP

Indexed keywords

LIPID; MEMBRANE ENZYME; SITE 2 PROTEASE; STEROL REGULATORY ELEMENT BINDING PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84885183980     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.03.031     Document Type: Review
Times cited : (47)

References (67)
  • 1
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • M.S. Brown, J. Ye, R.B. Rawson, and J.L. Goldstein Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans Cell 100 4 2000 391 398
    • (2000) Cell , vol.100 , Issue.4 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 2
    • 0033621152 scopus 로고    scopus 로고
    • Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease
    • DOI 10.1021/bi991080q
    • M.S. Wolfe, J. De Los Angeles, D.D. Miller, W. Xia, and D.J. Selkoe Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease Biochemistry 38 35 1999 11223 11230 (Pubitemid 29420941)
    • (1999) Biochemistry , vol.38 , Issue.35 , pp. 11223-11230
    • Wolfe, M.S.1    De Los Angeles, J.2    Miller, D.D.3    Xia, W.4    Selkoe, D.J.5
  • 3
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • R.B. Rawson, N.G. Zelenski, D. Nijhawan, J. Ye, J. Sakai, M.T. Hasan, T.Y. Chang, M.S. Brown, and J.L. Goldstein Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs Mol. Cell 1 1 1997 47 57 (Pubitemid 127376392)
    • (1997) Molecular Cell , vol.1 , Issue.1 , pp. 47-57
    • Rawson, R.B.1    Zelenski, N.G.2    Nijhawan, D.3    Ye, J.4    Sakai, J.5    Hasan, M.T.6    Chang, T.Y.7    Brown, M.S.8    Goldstein, J.L.9
  • 4
    • 39849102805 scopus 로고    scopus 로고
    • Regulation of sterol synthesis in eukaryotes
    • P.J. Espenshade, and A.L. Hughes Regulation of sterol synthesis in eukaryotes Annu. Rev. Genet. 41 2007 401 427
    • (2007) Annu. Rev. Genet. , vol.41 , pp. 401-427
    • Espenshade, P.J.1    Hughes, A.L.2
  • 5
    • 70350411534 scopus 로고    scopus 로고
    • The site-2 protease at Ten
    • N.M. Hooper, U. Lendeckel, Springer Dordrecht
    • R.B. Rawson, and W.P. Li The site-2 protease at Ten N.M. Hooper, U. Lendeckel, Intramembrane-Cleaving Proteases (I-CLiPs) 2007 Springer Dordrecht 1 16
    • (2007) Intramembrane-Cleaving Proteases (I-CLiPs) , pp. 1-16
    • Rawson, R.B.1    Li, W.P.2
  • 6
    • 0028087833 scopus 로고
    • Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression
    • DOI 10.1007/BF02254759
    • M.T. Hasan, C.C. Chang, and T.Y. Chang Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression Somat. Cell Mol. Genet. 20 3 1994 183 194 (Pubitemid 24308069)
    • (1994) Somatic Cell and Molecular Genetics , vol.20 , Issue.3 , pp. 183-194
    • Hasan, M.T.1    Chang, C.C.Y.2    Chang, T.Y.3
  • 7
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • N.D. Rawlings, and A.J. Barrett Evolutionary families of metallopeptidases Methods Enzymol. 248 1995 183 228
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 8
    • 0033618342 scopus 로고    scopus 로고
    • Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins
    • N.G. Zelenski, R.B. Rawson, M.S. Brown, and J.L. Goldstein Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins J. Biol. Chem. 274 31 1999 21973 21980
    • (1999) J. Biol. Chem. , vol.274 , Issue.31 , pp. 21973-21980
    • Zelenski, N.G.1    Rawson, R.B.2    Brown, M.S.3    Goldstein, J.L.4
  • 9
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors
    • DOI 10.1073/pnas.96.26.14765
    • D.Z. Rudner, P. Fawcett, and R. Losick A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors Proc. Natl. Acad. Sci. U. S. A. 96 26 1999 14765 14770 (Pubitemid 30019714)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.26 , pp. 14765-14770
    • Rudner, D.Z.1    Fawcett, P.2    Losick, R.3
  • 10
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • DOI 10.1126/science.1150755
    • L. Feng, H. Yan, Z. Wu, N. Yan, Z. Wang, P.D. Jeffrey, and Y. Shi Structure of a site-2 protease family intramembrane metalloprotease Science 318 5856 2007 1608 1612 (Pubitemid 350233656)
    • (2007) Science , vol.318 , Issue.5856 , pp. 1608-1612
    • Feng, L.1    Yan, H.2    Wu, Z.3    Yan, N.4    Wang, Z.5    Jeffrey, P.D.6    Shi, Y.7
  • 11
    • 70349488828 scopus 로고    scopus 로고
    • Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP
    • R. Zhou, C. Cusumano, D. Sui, R.M. Garavito, and L. Kroos Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP Proc. Natl. Acad. Sci. U. S. A. 106 38 2009 16174 16179
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.38 , pp. 16174-16179
    • Zhou, R.1    Cusumano, C.2    Sui, D.3    Garavito, R.M.4    Kroos, L.5
  • 12
    • 29344444795 scopus 로고    scopus 로고
    • Site-2 protease regulated intramembrane proteolysis: Sequence homologs suggest an ancient signaling cascade
    • DOI 10.1110/ps.051766506
    • L.N. Kinch, K. Ginalski, and N.V. Grishin Site-2 protease regulated intramembrane proteolysis: sequence homologs suggest an ancient signaling cascade Protein Sci. 15 1 2006 84 93 (Pubitemid 43004236)
    • (2006) Protein Science , vol.15 , Issue.1 , pp. 84-93
    • Kinch, L.N.1    Ginalski, K.2    Grishin, N.V.3
  • 13
    • 0033529560 scopus 로고    scopus 로고
    • Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins
    • P.J. Espenshade, D. Cheng, J.L. Goldstein, and M.S. Brown Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins J. Biol. Chem. 274 32 1999 22795 22804
    • (1999) J. Biol. Chem. , vol.274 , Issue.32 , pp. 22795-22804
    • Espenshade, P.J.1    Cheng, D.2    Goldstein, J.L.3    Brown, M.S.4
  • 14
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of Site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • R.A. DeBose-Boyd, M.S. Brown, W.P. Li, A. Nohturfft, J.L. Goldstein, and P.J. Espenshade Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi Cell 99 7 1999 703 712 (Pubitemid 30017641)
    • (1999) Cell , vol.99 , Issue.7 , pp. 703-712
    • DeBose-Boyd, R.A.1    Brown, M.S.2    Li, W.-P.3    Nohturfft, A.4    Goldstein, J.L.5    Espenshade, P.J.6
  • 15
    • 5644244829 scopus 로고    scopus 로고
    • Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6
    • DOI 10.1074/jbc.M408466200
    • J. Shen, and R. Prywes Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6 J. Biol. Chem. 279 41 2004 43046 43051 (Pubitemid 39372199)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43046-43051
    • Shen, J.1    Prywes, R.2
  • 16
    • 0036480346 scopus 로고    scopus 로고
    • The SREBP pathway in Drosophila: Regulation by palmitate, not sterols
    • DOI 10.1016/S1534-5807(01)00119-8, PII S1534580701001198
    • A.C. Seegmiller, I. Dobrosotskaya, J.L. Goldstein, Y.K. Ho, M.S. Brown, and R.B. Rawson The SREBP pathway in Drosophila: regulation by palmitate, not sterols Dev. Cell 2 2 2002 229 238 (Pubitemid 38351587)
    • (2002) Developmental Cell , vol.2 , Issue.2 , pp. 229-238
    • Seegmiller, A.C.1    Dobrosotskaya, I.2    Goldstein, J.L.3    Ho, Y.K.4    Brown, M.S.5    Rawson, R.B.6
  • 17
    • 58049199407 scopus 로고    scopus 로고
    • A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli
    • K. Inaba, M. Suzuki, K. Maegawa, S. Akiyama, K. Ito, and Y. Akiyama A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli J. Biol. Chem. 283 50 2008 35042 35052
    • (2008) J. Biol. Chem. , vol.283 , Issue.50 , pp. 35042-35052
    • Inaba, K.1    Suzuki, M.2    Maegawa, K.3    Akiyama, S.4    Ito, K.5    Akiyama, Y.6
  • 19
    • 0036809216 scopus 로고    scopus 로고
    • Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis
    • DOI 10.1016/S1097-2765(02)00655-X
    • M.K. Lemberg, and B. Martoglio Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis Mol. Cell 10 4 2002 735 744 (Pubitemid 35335630)
    • (2002) Molecular Cell , vol.10 , Issue.4 , pp. 735-744
    • Lemberg, M.K.1    Martoglio, B.2
  • 20
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of Rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • DOI 10.1016/S1097-2765(03)00181-3
    • S. Urban, and M. Freeman Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain Mol. Cell 11 6 2003 1425 1434 (Pubitemid 36776530)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 21
    • 0032726294 scopus 로고    scopus 로고
    • Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism
    • M. Paetzel, and N.C. Strynadka Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism Protein Sci. 8 11 1999 2533 2536 (Pubitemid 29536424)
    • (1999) Protein Science , vol.8 , Issue.11 , pp. 2533-2536
    • Paetzel, M.1    Strynadka, N.C.J.2
  • 22
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Y. Wang, Y. Zhang, and Y. Ha Crystal structure of a rhomboid family intramembrane protease Nature 444 7116 2006 179 180
    • (2006) Nature , vol.444 , Issue.7116 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 24
    • 63649088506 scopus 로고    scopus 로고
    • Structure and mechanism of intramembrane protease
    • Y. Ha Structure and mechanism of intramembrane protease Semin. Cell Dev. Biol. 20 2 2009 240 250
    • (2009) Semin. Cell Dev. Biol. , vol.20 , Issue.2 , pp. 240-250
    • Ha, Y.1
  • 25
    • 31544450017 scopus 로고    scopus 로고
    • A chloroplastic inner envelope membrane protease is essential for plant development
    • DOI 10.1016/j.febslet.2005.12.098, PII S0014579306000123
    • B. Bolter, A. Nada, H. Fulgosi, and J. Soll A chloroplastic inner envelope membrane protease is essential for plant development FEBS Lett. 580 3 2006 789 794 (Pubitemid 43153786)
    • (2006) FEBS Letters , vol.580 , Issue.3 , pp. 789-794
    • Bolter, B.1    Nada, A.2    Fulgosi, H.3    Soll, J.4
  • 26
    • 53149117026 scopus 로고    scopus 로고
    • Membrane-bound transcription factors in plants
    • P.J. Seo, S.G. Kim, and C.M. Park Membrane-bound transcription factors in plants Trends Plant Sci. 13 10 2008 550 556
    • (2008) Trends Plant Sci. , vol.13 , Issue.10 , pp. 550-556
    • Seo, P.J.1    Kim, S.G.2    Park, C.M.3
  • 27
    • 70350397502 scopus 로고    scopus 로고
    • Cryptococcus neoformans Site-2 protease is required for virulence and survival in the presence of azole drugs
    • C.M. Bien, Y.C. Chang, W.D. Nes, K.J. Kwon-Chung, and P.J. Espenshade Cryptococcus neoformans Site-2 protease is required for virulence and survival in the presence of azole drugs Mol. Microbiol. 74 3 2009 672 690
    • (2009) Mol. Microbiol. , vol.74 , Issue.3 , pp. 672-690
    • Bien, C.M.1    Chang, Y.C.2    Nes, W.D.3    Kwon-Chung, K.J.4    Espenshade, P.J.5
  • 28
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • DOI 10.1016/S1097-2765(00)00133-7
    • J. Ye, R.B. Rawson, R. Komuro, X. Chen, U.P. Dave, R. Prywes, M.S. Brown, and J.L. Goldstein ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs Mol. Cell 6 6 2000 1355 1364 (Pubitemid 32045928)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6    Brown, M.S.7    Goldstein, J.L.8
  • 29
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • DOI 10.1016/j.cell.2005.11.040, PII S0092867406000043
    • K. Zhang, X. Shen, J. Wu, K. Sakaki, T. Saunders, D.T. Rutkowski, S.H. Back, and R.J. Kaufman Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response Cell 124 3 2006 587 599 (Pubitemid 43199443)
    • (2006) Cell , vol.124 , Issue.3 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5    Rutkowski, D.T.6    Back, S.H.7    Kaufman, R.J.8
  • 31
    • 56449110891 scopus 로고    scopus 로고
    • Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: A delicate balance
    • A. Radhakrishnan, J.L. Goldstein, J.G. McDonald, and M.S. Brown Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance Cell Metab. 8 6 2008 512 521
    • (2008) Cell Metab. , vol.8 , Issue.6 , pp. 512-521
    • Radhakrishnan, A.1    Goldstein, J.L.2    McDonald, J.G.3    Brown, M.S.4
  • 32
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • J. Sakai, R.B. Rawson, P.J. Espenshade, D. Cheng, A.C. Seegmiller, J.L. Goldstein, and M.S. Brown Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells Mol. Cell 2 4 1998 505 514 (Pubitemid 128381303)
    • (1998) Molecular Cell , vol.2 , Issue.4 , pp. 505-514
    • Sakai, J.1    Rawson, R.B.2    Espenshade, P.J.3    Cheng, D.4    Seegmiller, A.C.5    Goldstein, J.L.6    Brown, M.S.7
  • 34
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment
    • DOI 10.1016/S0092-8674(00)81304-5
    • J. Sakai, E.A. Duncan, R.B. Rawson, X. Hua, M.S. Brown, and J.L. Goldstein Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment Cell 85 7 1996 1037 1046 (Pubitemid 26231170)
    • (1996) Cell , vol.85 , Issue.7 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5    Goldstein, J.L.6
  • 35
    • 0030911517 scopus 로고    scopus 로고
    • Cleavage site for sterol-regulated protease localized to a Leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2
    • DOI 10.1074/jbc.272.19.12778
    • E.A. Duncan, M.S. Brown, J.L. Goldstein, and J. Sakai Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2 J. Biol. Chem. 272 19 1997 12778 12785 (Pubitemid 27203378)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.19 , pp. 12778-12785
    • Duncan, E.A.1    Brown, M.S.2    Goldstein, J.L.3    Sakai, J.4
  • 36
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • X. Wang, R. Sato, M.S. Brown, X. Hua, and J.L. Goldstein SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis Cell 77 1 1994 53 62
    • (1994) Cell , vol.77 , Issue.1 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 37
    • 0343890977 scopus 로고
    • Synthesis and destruction of cholesterol in the organism
    • R. Schoenheimer, and F. Breusch Synthesis and destruction of cholesterol in the organism J. Biol. Chem. 103 1933 439 448
    • (1933) J. Biol. Chem. , vol.103 , pp. 439-448
    • Schoenheimer, R.1    Breusch, F.2
  • 38
    • 0028657057 scopus 로고
    • Somatic cell genetic analysis of two classes of CHO cell mutants expressing opposite phenotypes in sterol-dependent regulation of cholesterol metabolism
    • M.T. Hasan, and T.Y. Chang Somatic cell genetic analysis of two classes of CHO cell mutants expressing opposite phenotypes in sterol-dependent regulation of cholesterol metabolism Somat. Cell Mol. Genet. 20 6 1994 481 491
    • (1994) Somat. Cell Mol. Genet. , vol.20 , Issue.6 , pp. 481-491
    • Hasan, M.T.1    Chang, T.Y.2
  • 40
    • 0027261368 scopus 로고
    • Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells
    • M.J. Evans, and J.E. Metherall Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells Mol. Cell. Biol. 13 9 1993 5175 5185 (Pubitemid 23260622)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.9 , pp. 5175-5185
    • Evans, M.J.1    Metherall, J.E.2
  • 41
    • 0017165502 scopus 로고
    • Isolation and characterization of an unsaturated fatty acid-requiring mutant of cultured mammalian cells
    • T.Y. Chang, and P.R. Vagelos Isolation and characterization of an unsaturated fatty acid-requiring mutant of cultured mammalian cells Proc. Natl. Acad. Sci. U. S. A. 73 1 1976 24 28
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , Issue.1 , pp. 24-28
    • Chang, T.Y.1    Vagelos, P.R.2
  • 42
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • K. Haze, H. Yoshida, H. Yanagi, T. Yura, and K. Mori Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress Mol. Biol. Cell 10 11 1999 3787 3799 (Pubitemid 29534025)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.11 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 43
    • 80054722420 scopus 로고    scopus 로고
    • The unfolded protein response: Integrating stress signals through the stress sensor IRE1α
    • C. Hetz, F. Martinon, D. Rodriguez, and L.H. Glimcher The unfolded protein response: integrating stress signals through the stress sensor IRE1α Physiol. Rev. 91 4 2011 1219 1243
    • (2011) Physiol. Rev. , vol.91 , Issue.4 , pp. 1219-1243
    • Hetz, C.1    Martinon, F.2    Rodriguez, D.3    Glimcher, L.H.4
  • 44
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response
    • DOI 10.1128/MCB.25.3.921-932.2005
    • J. Shen, E.L. Snapp, J. Lippincott-Schwartz, and R. Prywes Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response Mol. Cell. Biol. 25 3 2005 921 932 (Pubitemid 40165801)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.3 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 46
    • 79954490167 scopus 로고    scopus 로고
    • Physiological unfolded protein response regulated by OASIS family members, transmembrane bZIP transcription factors
    • S. Kondo, A. Saito, R. Asada, S. Kanemoto, and K. Imaizumi Physiological unfolded protein response regulated by OASIS family members, transmembrane bZIP transcription factors IUBMB Life 63 4 2011 233 239
    • (2011) IUBMB Life , vol.63 , Issue.4 , pp. 233-239
    • Kondo, S.1    Saito, A.2    Asada, R.3    Kanemoto, S.4    Imaizumi, K.5
  • 48
    • 35949003194 scopus 로고    scopus 로고
    • Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis
    • DOI 10.1111/j.1600-0854.2007.00654.x
    • D. Bailey, C. Barreca, and P. O'Hare Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis Traffic 8 12 2007 1796 1814 (Pubitemid 350066690)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1796-1814
    • Bailey, D.1    Barreca, C.2    O'Hare, P.3
  • 50
    • 33645107263 scopus 로고    scopus 로고
    • Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress
    • T. Murakami, S. Kondo, M. Ogata, S. Kanemoto, A. Saito, A. Wanaka, and K. Imaizumi Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress J. Neurochem. 96 4 2006 1090 1100
    • (2006) J. Neurochem. , vol.96 , Issue.4 , pp. 1090-1100
    • Murakami, T.1    Kondo, S.2    Ogata, M.3    Kanemoto, S.4    Saito, A.5    Wanaka, A.6    Imaizumi, K.7
  • 55
    • 33744544947 scopus 로고    scopus 로고
    • Fatty acid auxotrophy in Drosophila larvae lacking SREBP
    • DOI 10.1016/j.cmet.2006.04.011, PII S1550413106001306
    • A.S. Kunte, K.A. Matthews, and R.B. Rawson Fatty acid auxotrophy in Drosophila larvae lacking SREBP Cell Metab. 3 6 2006 439 448 (Pubitemid 43811777)
    • (2006) Cell Metabolism , vol.3 , Issue.6 , pp. 439-448
    • Kunte, A.S.1    Matthews, K.A.2    Rawson, R.B.3
  • 56
    • 61549138703 scopus 로고    scopus 로고
    • Alternative processing of sterol regulatory element binding protein during larval development in Drosophila melanogaster
    • K.A. Matthews, A.S. Kunte, E. Tambe-Ebot, and R.B. Rawson Alternative processing of sterol regulatory element binding protein during larval development in Drosophila melanogaster Genetics 181 1 2009 119 128
    • (2009) Genetics , vol.181 , Issue.1 , pp. 119-128
    • Matthews, K.A.1    Kunte, A.S.2    Tambe-Ebot, E.3    Rawson, R.B.4
  • 57
    • 65649133944 scopus 로고    scopus 로고
    • Activation of sterol regulatory element-binding protein by the caspase Drice in Drosophila larvae
    • B. Amarneh, K.A. Matthews, and R.B. Rawson Activation of sterol regulatory element-binding protein by the caspase Drice in Drosophila larvae J. Biol. Chem. 284 15 2009 9674 9682
    • (2009) J. Biol. Chem. , vol.284 , Issue.15 , pp. 9674-9682
    • Amarneh, B.1    Matthews, K.A.2    Rawson, R.B.3
  • 58
    • 0028978248 scopus 로고
    • Purification of an interleukin-1 beta converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains
    • X. Wang, J.T. Pai, E.A. Wiedenfeld, J.C. Medina, C.A. Slaughter, J.L. Goldstein, and M.S. Brown Purification of an interleukin-1 beta converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains J. Biol. Chem. 270 30 1995 18044 18050
    • (1995) J. Biol. Chem. , vol.270 , Issue.30 , pp. 18044-18050
    • Wang, X.1    Pai, J.T.2    Wiedenfeld, E.A.3    Medina, J.C.4    Slaughter, C.A.5    Goldstein, J.L.6    Brown, M.S.7
  • 59
    • 0029895343 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins
    • DOI 10.1073/pnas.93.11.5437
    • J.T. Pai, M.S. Brown, and J.L. Goldstein Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins Proc. Natl. Acad. Sci. U. S. A. 93 11 1996 5437 5442 (Pubitemid 26159468)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.11 , pp. 5437-5442
    • Pai, J.-T.1    Brown, M.S.2    Goldstein, J.L.3
  • 60
    • 0036315042 scopus 로고    scopus 로고
    • Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis
    • DOI 10.1128/MCB.22.16.5639-5649.2002
    • C. Raggo, N. Rapin, J. Stirling, P. Gobeil, E. Smith-Windsor, P. O'Hare, and V. Misra Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis Mol. Cell. Biol. 22 16 2002 5639 5649 (Pubitemid 34815814)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.16 , pp. 5639-5649
    • Raggo, C.1    Rapin, N.2    Stirling, J.3    Gobeil, P.4    Smith-Windsor, E.5    O'Hare, P.6    Misra, V.7
  • 62
    • 30044441047 scopus 로고    scopus 로고
    • CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P
    • DOI 10.1091/mbc.E05-06-0500
    • J. Stirling, and P. O'Hare CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P Mol. Biol. Cell 17 1 2006 413 426 (Pubitemid 43049493)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.1 , pp. 413-426
    • Stirling, J.1    O'Hare, P.2
  • 63
    • 35548990261 scopus 로고    scopus 로고
    • Transcriptional profiling of genes that are regulated by the endoplasmic reticulum-bound transcription factor AIbZIP/CREB3L4 in prostate cells
    • DOI 10.1152/physiolgenomics.00097.2007
    • S. Ben Aicha, J. Lessard, M. Pelletier, A. Fournier, E. Calvo, and C. Labrie Transcriptional profiling of genes that are regulated by the endoplasmic reticulum-bound transcription factor AIbZIP/CREB3L4 in prostate cells Physiol. Genomics 31 2 2007 295 305 (Pubitemid 350014407)
    • (2007) Physiological Genomics , vol.31 , Issue.2 , pp. 295-305
    • Aicha, S.B.1    Lessard, J.2    Pelletier, M.3    Fournier, A.4    Calvo, E.5    Labrie, C.6
  • 64
    • 63649142567 scopus 로고    scopus 로고
    • Rhomboids: 7 years of a new protease family
    • M. Freeman Rhomboids: 7 years of a new protease family Semin. Cell Dev. Biol. 20 2 2009 231 239
    • (2009) Semin. Cell Dev. Biol. , vol.20 , Issue.2 , pp. 231-239
    • Freeman, M.1
  • 65
    • 80054893675 scopus 로고    scopus 로고
    • The rhomboid protease family: A decade of progress on function and mechanism
    • S. Urban, and S.W. Dickey The rhomboid protease family: a decade of progress on function and mechanism Genome Biol. 12 10 2011 231 241
    • (2011) Genome Biol. , vol.12 , Issue.10 , pp. 231-241
    • Urban, S.1    Dickey, S.W.2
  • 66
    • 0035830840 scopus 로고    scopus 로고
    • Unsaturated fatty acids down-regulate srebp isoforms 1a and 1c by two mechanisms in HEK-293 cells
    • V.C. Hannah, J. Ou, A. Luong, J.L. Goldstein, and M.S. Brown Unsaturated fatty acids down-regulate srebp isoforms 1a and 1c by two mechanisms in HEK-293 cells J. Biol. Chem. 276 6 2001 4365 4372
    • (2001) J. Biol. Chem. , vol.276 , Issue.6 , pp. 4365-4372
    • Hannah, V.C.1    Ou, J.2    Luong, A.3    Goldstein, J.L.4    Brown, M.S.5
  • 67
    • 77956633770 scopus 로고    scopus 로고
    • Activation of sterol regulatory element binding proteins in the absence of Scap in Drosophila melanogaster
    • K.A. Matthews, C. Ozdemir, and R.B. Rawson Activation of sterol regulatory element binding proteins in the absence of Scap in Drosophila melanogaster Genetics 185 1 2010 189 198
    • (2010) Genetics , vol.185 , Issue.1 , pp. 189-198
    • Matthews, K.A.1    Ozdemir, C.2    Rawson, R.B.3


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