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Volumn 16, Issue 22, 1997, Pages 6636-6645

Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin

Author keywords

Calmodulin; Eukaryotic signal peptidase; HIV 1 gp160; Prolactin secretion; Signal sequence

Indexed keywords

CALMODULIN; ENVELOPE PROTEIN; GLYCOPROTEIN GP 160; PROLACTIN; SIGNAL PEPTIDASE; SIGNAL PEPTIDE;

EID: 0030732847     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.22.6636     Document Type: Article
Times cited : (125)

References (48)
  • 3
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes II. Reconstitution of functional rough microsomes from heterologous components
    • Blobel, G. and Dobberstein, B. (1975) Transfer of proteins across membranes II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol., 67, 852-862.
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 4
    • 0023894180 scopus 로고
    • SEC11 is required for signal peptide processing and yeast cell growth
    • Böhni, P.C., Deshaics, R.J. and Schekman, R. (1988) SEC11 is required for signal peptide processing and yeast cell growth. J. Cell Biol., 106, 1035-1042.
    • (1988) J. Cell Biol. , vol.106 , pp. 1035-1042
    • Böhni, P.C.1    Deshaics, R.J.2    Schekman, R.3
  • 5
    • 0024370455 scopus 로고
    • Photochemical labelling of apolar phase of membranes
    • Brunner, J. (1989) Photochemical labelling of apolar phase of membranes. Methods Enzymol., 172, 628-687.
    • (1989) Methods Enzymol. , vol.172 , pp. 628-687
    • Brunner, J.1
  • 7
    • 0029008813 scopus 로고
    • A role for calmodulin in organelle membrane tubulation
    • de Figueiredo, P. and Brown, W.J. (1995) A role for calmodulin in organelle membrane tubulation. Mol. Biol. Cell. 6, 871-887.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 871-887
    • De Figueiredo, P.1    Brown, W.J.2
  • 8
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson, A.H. and Blobel, G. (1983) Cell-free translation of messenger RNA in a wheat germ system. Methods Enymol., 96, 38-50.
    • (1983) Methods Enymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 9
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • Evans, E.A., Gilmore, R. and Blobel, G. (1986) Purification of microsomal signal peptidase as a complex. Proc. Natl Acad. Sci. USA. 83, 581-585.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 10
    • 0028278795 scopus 로고
    • Correlation between high level gp160 expression and reduced CD4 biosynthesis in clonal derivatives of human immunodeficiency virus type 1-infected U-937 cells
    • Geleziunas, R., Bour, S. and Wainberg, M.A. (1994) Correlation between high level gp160 expression and reduced CD4 biosynthesis in clonal derivatives of human immunodeficiency virus type 1-infected U-937 cells. J. Gen. Virol., 75, 837-865.
    • (1994) J. Gen. Virol. , vol.75 , pp. 837-865
    • Geleziunas, R.1    Bour, S.2    Wainberg, M.A.3
  • 11
    • 0021801342 scopus 로고
    • Genes-in-pieces revisited
    • Gilbert, W. (1985) Genes-in-pieces revisited. Science. 228, 823-824.
    • (1985) Science , vol.228 , pp. 823-824
    • Gilbert, W.1
  • 12
    • 0026038363 scopus 로고
    • Transcription of full-length and truncated mRNA transcripts to study protein translocation across the endoplasmic reticulum
    • Gilmore, R., Collins, P., Johnson, J., Kellaris, K. and Rapiejko, P. (1991) Transcription of full-length and truncated mRNA transcripts to study protein translocation across the endoplasmic reticulum. Methods Cell Biol., 34, 223-239.
    • (1991) Methods Cell Biol. , vol.34 , pp. 223-239
    • Gilmore, R.1    Collins, P.2    Johnson, J.3    Kellaris, K.4    Rapiejko, P.5
  • 14
    • 0024428204 scopus 로고
    • A subunit of mammalian signal peptidase is homologous to yeast SEC II protein
    • Greenburg, G., Shelness, G.S. and Blobel, G. (1989) A subunit of mammalian signal peptidase is homologous to yeast SEC II protein. J. Biol. Chem., 264, 15762-15765.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15762-15765
    • Greenburg, G.1    Shelness, G.S.2    Blobel, G.3
  • 15
    • 0029001515 scopus 로고
    • Generation, transtocation, and presentation of MHC class I-restricted peptides
    • Heemels, M.T. and Ploegh, H. (1995) Generation, transtocation, and presentation of MHC class I-restricted peptides. Annu. Rev. Biochem., 64, 463-491.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463-491
    • Heemels, M.T.1    Ploegh, H.2
  • 16
    • 0026521557 scopus 로고
    • HLA-A2.1-associated peptides from a mutant cell line: A second pathway of antigen presentation
    • Henderson, R.A., Michel, H., Sakaguchi, K., Shabanowitz, J., Appella, E., Hunt, D. and Engelhard, V.H. (1992) HLA-A2.1-associated peptides from a mutant cell line: a second pathway of antigen presentation. Science. 255, 1264-1266.
    • (1992) Science , vol.255 , pp. 1264-1266
    • Henderson, R.A.1    Michel, H.2    Sakaguchi, K.3    Shabanowitz, J.4    Appella, E.5    Hunt, D.6    Engelhard, V.H.7
  • 17
    • 0027229977 scopus 로고
    • Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion
    • High, S., Andersen, S.S.L., Görlich, D., Hartmann, F., Prehn, S., Rapoport, T.A. and Dobberstein, B. (1993a) Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. J. Cell Biol., 121, 743-750.
    • (1993) J. Cell Biol. , vol.121 , pp. 743-750
    • High, S.1    Andersen, S.S.L.2    Görlich, D.3    Hartmann, F.4    Prehn, S.5    Rapoport, T.A.6    Dobberstein, B.7
  • 18
    • 0027454264 scopus 로고
    • Site-specific photocross-linking reveals that Sec61 p and TRAM contact different regions of a membrane inserted signal sequence
    • High, S. et al. (1993b) Site-specific photocross-linking reveals that Sec61 p and TRAM contact different regions of a membrane inserted signal sequence. J. Biol. Chem., 268, 26745-26751.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26745-26751
    • High, S.1
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 20
    • 0028783818 scopus 로고
    • Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein
    • Hombach, J., Pircher, H., Tonegawa, S. and Zinkernagel, R.M. (1995) Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein. J. Exp. Med., 182, 1615-1619.
    • (1995) J. Exp. Med. , vol.182 , pp. 1615-1619
    • Hombach, J.1    Pircher, H.2    Tonegawa, S.3    Zinkernagel, R.M.4
  • 21
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two faced or multi-faceted?
    • James, P., Vorherr, T. and Carafoli, E. (1995) Calmodulin-binding domains: just two faced or multi-faceted? Trends Biochem. Sci., 20, 38-42.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 22
    • 0030057070 scopus 로고    scopus 로고
    • Cyclosporin A inhibits the degradation of signal sequences after processing of presecretory proteins by signal peptidase
    • Klappa, P., Dierks, T. and Zimmermann, R. (1996) Cyclosporin A inhibits the degradation of signal sequences after processing of presecretory proteins by signal peptidase. Eur. J. Biochem., 239, 509-518.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 509-518
    • Klappa, P.1    Dierks, T.2    Zimmermann, R.3
  • 24
    • 0025319664 scopus 로고
    • Regulation of prolactin secretion at the level of the lactotroph
    • Lamberts, S.W.J. and MacLeod, R.M. (1990) Regulation of prolactin secretion at the level of the lactotroph. Physiol. Rev., 70, 279-325.
    • (1990) Physiol. Rev. , vol.70 , pp. 279-325
    • Lamberts, S.W.J.1    MacLeod, R.M.2
  • 25
    • 0029792920 scopus 로고    scopus 로고
    • Effects of inefficient cleavage of the signal sequence of HIV-1 gp120 on its association with calnexin, folding and intracellular transport
    • Li, Y., Bergeron, J.J.M., Luo, L., Ou, W.J., Thomas, D.Y. and Kang, Y.(1996) Effects of inefficient cleavage of the signal sequence of HIV-1 gp120 on its association with calnexin, folding and intracellular transport. Proc. Natl Acad. Sci. USA. 93, 9606-9611.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9606-9611
    • Li, Y.1    Bergeron, J.J.M.2    Luo, L.3    Ou, W.J.4    Thomas, D.Y.5    Kang, Y.6
  • 27
    • 0029670548 scopus 로고    scopus 로고
    • Snapshots of membrane translocating proteins
    • Manoglio, B. and Dobberstein, B. (1996) Snapshots of membrane translocating proteins. Trends Cell Biol., 6, 142-147.
    • (1996) Trends Cell Biol. , vol.6 , pp. 142-147
    • Manoglio, B.1    Dobberstein, B.2
  • 28
    • 0029002962 scopus 로고
    • The protein conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M., Brunner, J. and Dobberstein, B. (1995) The protein conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell. 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.2    Brunner, J.3    Dobberstein, B.4
  • 29
    • 0027421380 scopus 로고
    • Identification uf a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein
    • Miller, M.A., Mietzner, T.A., Cloyd, M.W., Robey, G. and Montelaro, R.C. (1993) Identification uf a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein. AIDS Res. Hum. Retrovir., 9, 1057-1066.
    • (1993) AIDS Res. Hum. Retrovir. , vol.9 , pp. 1057-1066
    • Miller, M.A.1    Mietzner, T.A.2    Cloyd, M.W.3    Robey, G.4    Montelaro, R.C.5
  • 30
    • 0027417476 scopus 로고
    • Determination of the distance between oligossaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I. and von Heijne.G. (1993) Determination of the distance between oligossaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem., 268, 5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.1    Von Heijne, G.2
  • 31
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphipathic α-helices
    • O'Neil, K.T. and DeGrado, W.F. (1990) How calmodulin binds its targets: sequence independent recognition of amphipathic α-helices. Trends Biochem. Sci., 15, 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 34
    • 0029952518 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplsmic reticulum and bacterial inner membranes
    • Rapoport, T., Jungnickel, B. and Kutay, U. (1996) Protein translocation across the eukaryotic endoplsmic reticulum and bacterial inner membranes. Annu. Rev. Biochem., 65, 271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.1    Jungnickel, B.2    Kutay, U.3
  • 35
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow.G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 36
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S.L. and Crabtree, G.R. (1992) The mechanism of action of cyclosporin A and FK506. Immunol. Today. 13, 136-142.
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 37
    • 0025294104 scopus 로고
    • Two subunits of canine signal peptidase complex are homologous to yeast SEC11 protein
    • Shelness, G.S. and Blobel, G. (1990) Two subunits of canine signal peptidase complex are homologous to yeast SEC11 protein. J. Biol. Chem., 265, 9512-9519.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9512-9519
    • Shelness, G.S.1    Blobel, G.2
  • 38
    • 0027017177 scopus 로고
    • Receptor-mediated endocytosis in semiintact cells
    • Smythe, M., Redelmeier, T.E. and Schmid, S.L. (1992) Receptor-mediated endocytosis in semiintact cells. Methods Enzymol., 219, 223-234.
    • (1992) Methods Enzymol. , vol.219 , pp. 223-234
    • Smythe, M.1    Redelmeier, T.E.2    Schmid, S.L.3
  • 39
    • 0027971451 scopus 로고
    • Calmodulin antagonists inhibit human immunodeficiency virus-induced cell fusion but not virus replication
    • Srinivas, R.V., Bernstein, H., Oliver, C. and Compans, R.W. (1994) Calmodulin antagonists inhibit human immunodeficiency virus-induced cell fusion but not virus replication. AIDS Res. Hum. Retrovir., 10, 1489-1496.
    • (1994) AIDS Res. Hum. Retrovir. , vol.10 , pp. 1489-1496
    • Srinivas, R.V.1    Bernstein, H.2    Oliver, C.3    Compans, R.W.4
  • 40
    • 0027505042 scopus 로고
    • Cytosolic domain of the human immunodeficiency virus envelope glycoprotein binds to calmodulin and inhibits calmodulin regulated proteins
    • Srinivas, S.K., Srinivas, R.V. Anantharamaiah, G.M., Compans, R.W. and Segrest, J.P. (1993) Cytosolic domain of the human immunodeficiency virus envelope glycoprotein binds to calmodulin and inhibits calmodulin regulated proteins. J. Biol. Chem., 268, 22895-22899.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22895-22899
    • Srinivas, S.K.1    Srinivas, R.V.2    Anantharamaiah, G.M.3    Compans, R.W.4    Segrest, J.P.5
  • 42
    • 0026772152 scopus 로고
    • Signal peptidase I of Bacillus subtilis: Patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases
    • van Dijl, J.M., de Jong, A., Vehmaanperä, J., Venema, G. and Bron, S. (1992) Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. EMBO J., 11, 2819-2828.
    • (1992) EMBO J. , vol.11 , pp. 2819-2828
    • Van Dijl, J.M.1    De Jong, A.2    Vehmaanperä, J.3    Venema, G.4    Bron, S.5
  • 43
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • von Heijne, G. (1985) Signal sequences. The limits of variation. J. Mol. Biol., 184, 99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 46
    • 0017711756 scopus 로고
    • Modulator binding protein
    • Wung, J.H. and Desai, R. (1977) Modulator binding protein. J. Biol. Chem., 252, 4175-4184.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4175-4184
    • Wung, J.H.1    Desai, R.2
  • 47
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen processing mutant cell contain signal sequence-derived peptides
    • Wei, M.L. and Cresswell, P. (1992) HLA-A2 molecules in an antigen processing mutant cell contain signal sequence-derived peptides. Nature. 356, 443-446.
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 48
    • 0021995428 scopus 로고
    • Evidence for a role of calmodulin in the regulation of prolactin gene expression
    • White, B. (1985) Evidence for a role of calmodulin in the regulation of prolactin gene expression. J. Biol. Chem., 260, 1213-1217.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1213-1217
    • White, B.1


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