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Volumn 257, Issue 1, 1998, Pages 41-46

The propeptide of prohormone convertase PC2 acts as a transferable aggregation and membrane-association signal

Author keywords

Membrane association; Prohormone convertase 2; Protein targeting

Indexed keywords

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; ENZYME ACTIVITY; GENE DELETION; INTRACELLULAR TRANSPORT; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN TARGETING; SIGNAL TRANSDUCTION; XENOPUS;

EID: 0032189444     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570041.x     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly, R. B. (1985) Pathways of protein secretion in eukaryotes, Science 230, 25-32.
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 2
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban, P. A. & Irminger, J. (1994) Sorting and processing of secretory proteins, Biochem. J. 299, 1-18.
    • (1994) Biochem. J. , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.2
  • 3
    • 0030943904 scopus 로고    scopus 로고
    • Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells
    • Kuliawat, R., Klumperman, J., Ludwig, T. & Arvan, P. (1997) Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells, J. Cell. Biol. 137, 595-608.
    • (1997) J. Cell. Biol. , vol.137 , pp. 595-608
    • Kuliawat, R.1    Klumperman, J.2    Ludwig, T.3    Arvan, P.4
  • 4
    • 0027441696 scopus 로고
    • pH-dependent binding of chromogranin B and secretory vesicle matrix proteins to the vesicle membrane
    • Yoo, S. H. (1993) pH-dependent binding of chromogranin B and secretory vesicle matrix proteins to the vesicle membrane, Biochim. Biophys. Acta 1179, 239-246.
    • (1993) Biochim. Biophys. Acta , vol.1179 , pp. 239-246
    • Yoo, S.H.1
  • 5
    • 0025193033 scopus 로고
    • 2+-induced conformational change and aggregation of chromogranin A
    • 2+-induced conformational change and aggregation of chromogranin A, J. Biol. Chem. 265, 14414-14421.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14414-14421
    • Yoo, S.H.1    Albanesi, J.P.2
  • 6
    • 0027199503 scopus 로고
    • pH-dependent association of chromogranin A with secretory vesicle membrane and a putative membrane binding region of chromogranin A
    • Yoo, S. H. (1993) pH-dependent association of chromogranin A with secretory vesicle membrane and a putative membrane binding region of chromogranin A, Biochemistry 32, 8213-8219.
    • (1993) Biochemistry , vol.32 , pp. 8213-8219
    • Yoo, S.H.1
  • 7
    • 0024344257 scopus 로고
    • The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation
    • Geldes, H.-H., Rosa, P., Phillips, E., Baeuerle, P. A., Frank, R., Argos, P. & Huttner, W. B. (1989) The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation, J. Biol. Chem. 264, 12009-12015.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12009-12015
    • Geldes, H.-H.1    Rosa, P.2    Phillips, E.3    Baeuerle, P.A.4    Frank, R.5    Argos, P.6    Huttner, W.B.7
  • 8
    • 0028912393 scopus 로고
    • Calcium- and pH-dependent aggregation of carboxypeptidase E
    • Song, L. & Fricker, L. D. (1995) Calcium- and pH-dependent aggregation of carboxypeptidase E, J. Biol. Chem. 270, 7963-7967.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7963-7967
    • Song, L.1    Fricker, L.D.2
  • 9
    • 0028238359 scopus 로고
    • Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2
    • Shennan, K. I., Taylor, N. A. & Docherty, K. (1994) Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2, J. Biol. Chem. 269, 18646-18650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18646-18650
    • Shennan, K.I.1    Taylor, N.A.2    Docherty, K.3
  • 10
    • 0029995282 scopus 로고    scopus 로고
    • The C-terminal region of carboxypeptidase E involved in membrane hinding is distinct from the region involved with intracellular routing
    • Varlamov, O. & Fricker, L. D. (1996) The C-terminal region of carboxypeptidase E involved in membrane hinding is distinct from the region involved with intracellular routing, J. Biol. Chem. 271, 6077-6083.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6077-6083
    • Varlamov, O.1    Fricker, L.D.2
  • 12
    • 0030974124 scopus 로고    scopus 로고
    • Lit mice associated with a carboxypeptidase K mutation
    • Lit mice associated with a carboxypeptidase K mutation, Proc. Natl Acad. Sci. USA 94, 5314-5319.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5314-5319
    • Shen, F.S.1    Loh, Y.P.2
  • 15
    • 0027322942 scopus 로고
    • Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways
    • Chanat, E., Weiss, U., Huttner, W. B. & Tooze, S. A. (1993) Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways, EMBO J. 12, 2159-2168.
    • (1993) EMBO J. , vol.12 , pp. 2159-2168
    • Chanat, E.1    Weiss, U.2    Huttner, W.B.3    Tooze, S.A.4
  • 16
    • 0028958751 scopus 로고
    • Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway
    • Cool, D. R., Fenger, M. Snell, C. R. & Loh, Y. P. (1995) Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway, J. Biol. Chem. 270, 8723-8729.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8723-8729
    • Cool, D.R.1    Fenger, M.2    Snell, C.R.3    Loh, Y.P.4
  • 17
    • 0028940393 scopus 로고
    • An N-terminal hydrophobic peak is the sorting signal of regulated secretory proteins
    • Gorr, S. U. & Darling, D. S. (1995) An N-terminal hydrophobic peak is the sorting signal of regulated secretory proteins, FEBS Lett. 361, 8-12.
    • (1995) FEBS Lett. , vol.361 , pp. 8-12
    • Gorr, S.U.1    Darling, D.S.2
  • 18
    • 0343307146 scopus 로고    scopus 로고
    • Eukaryotic protein processing: Endoproteolysis of precursor proteins
    • Seidah, N. G. & Chrétien, M. (1997) Eukaryotic protein processing: endoproteolysis of precursor proteins, Curr. Opin. Biotechnol 8, 602-607.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 602-607
    • Seidah, N.G.1    Chrétien, M.2
  • 19
  • 20
    • 0021770917 scopus 로고
    • Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
    • Kreig, P. A. & Melton, D. A. (1984) Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter, Nucleic Acids Res. 12, 7057-7070.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7057-7070
    • Kreig, P.A.1    Melton, D.A.2
  • 21
    • 0031032892 scopus 로고    scopus 로고
    • Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfeeted COS-7 cells
    • Taylor, N. A., Shennan, K. I., Cutler, D. F. & Docherty, K. (1997) Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfeeted COS-7 cells, Biochem. J. 321, 367-373.
    • (1997) Biochem. J. , vol.321 , pp. 367-373
    • Taylor, N.A.1    Shennan, K.I.2    Cutler, D.F.3    Docherty, K.4
  • 22
    • 0028881510 scopus 로고
    • Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events
    • Shennan, K. I., Taylor, N. A., Jermany, J. L., Matthews, G. & Docherty, K. (1995) Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events, J. Biol. Chem. 270, 1402-1407.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1402-1407
    • Shennan, K.I.1    Taylor, N.A.2    Jermany, J.L.3    Matthews, G.4    Docherty, K.5
  • 23
    • 0026410596 scopus 로고
    • A highly efficient, cell-free translation/translocation system prepared from Xenopus eggs
    • Matthews, O. & Colman, A. (1991) A highly efficient, cell-free translation/translocation system prepared from Xenopus eggs, Nucleic Acids Res. 19, 6405-6412.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6405-6412
    • Matthews, O.1    Colman, A.2
  • 24
    • 0026329399 scopus 로고
    • Site-directed mutagenesis and expression of PC2 in microinjected Xenophus oocytes
    • Shennan, K. I. J., Seal, A. J., Smeekens, S. P., Steiner, D. F. & Docherty, K. (1991) Site-directed mutagenesis and expression of PC2 in microinjected Xenophus oocytes, J. Biol. Chem. 266, 24011-24017.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24011-24017
    • Shennan, K.I.J.1    Seal, A.J.2    Smeekens, S.P.3    Steiner, D.F.4    Docherty, K.5
  • 25
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat, E. & Huttner, W. B. (1991) Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network, J. Cell Biol. 115, 1505.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505
    • Chanat, E.1    Huttner, W.B.2
  • 26
    • 0019978195 scopus 로고
    • The internal pH and membrane potential of the insulin-secretory granule
    • Hutton, J. C. (1982) The internal pH and membrane potential of the insulin-secretory granule, Biochem. J. 204, 171-178.
    • (1982) Biochem. J. , vol.204 , pp. 171-178
    • Hutton, J.C.1
  • 27
    • 0031033158 scopus 로고    scopus 로고
    • H-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules
    • Urbé, S., Dittié, A. S. & Tooze, S. A. (1997) pH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules, Biochem. J. 321, 65-74.
    • (1997) Biochem. J. , vol.321 , pp. 65-74
    • Urbé, S.1    Dittié, A.S.2    Tooze, S.A.3
  • 28
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta-cells
    • Kuliawat, R. & Arvan, P. (1994) Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta-cells., J. Cell Biol. 126, 77-86.
    • (1994) J. Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 29
    • 0029973842 scopus 로고    scopus 로고
    • Expression of tyrosine-sulfated secretory proteins in Xenophus laevis oocytes. Differential export of constitutive and regulated proteins
    • Vannier, C. & Huttner, W. B. (1996) Expression of tyrosine-sulfated secretory proteins in Xenophus laevis oocytes. Differential export of constitutive and regulated proteins, Eur. J. Biochem. 239, 111-116.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 111-116
    • Vannier, C.1    Huttner, W.B.2
  • 30
    • 0027933035 scopus 로고
    • The disulphide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network
    • Chanat, E., Weiß, U. & Huttner, W. B. (1994) The disulphide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network, FEBS Lett. 351, 225-230.
    • (1994) FEBS Lett. , vol.351 , pp. 225-230
    • Chanat, E.1    Weiß, U.2    Huttner, W.B.3
  • 31
    • 0027929948 scopus 로고
    • The C-terminal region of carboxypeptidase E is involved in membrane binding and intracellular routing in AtT-20 cells
    • Mitra, A., Song, L. & Fricker, L. D. (1994) The C-terminal region of carboxypeptidase E is involved in membrane binding and intracellular routing in AtT-20 cells, J. Biol. Chem. 269, 19876-19881.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19876-19881
    • Mitra, A.1    Song, L.2    Fricker, L.D.3


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