메뉴 건너뛰기




Volumn 141, Issue 7, 1998, Pages 1515-1527

The mammalian calcium-binding protein, nucleobindin (CALNUC), is a Golgi resident protein

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; NUCLEOBINDIN; UNCLASSIFIED DRUG;

EID: 0032577972     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.7.1515     Document Type: Article
Times cited : (143)

References (59)
  • 1
    • 0002141007 scopus 로고    scopus 로고
    • Basic characteristics and ion binding to calreticulin
    • M. Michalak, editor. R.G. Landes Company, Georgetown
    • Baksh, S., and M. Michalak. 1996. Basic characteristics and ion binding to calreticulin. In Calreticulin. M. Michalak, editor. R.G. Landes Company, Georgetown. 11-26.
    • (1996) Calreticulin , pp. 11-26
    • Baksh, S.1    Michalak, M.2
  • 3
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth, C., and G.L.E. Koch. 1989. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell. 59:729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 4
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1991. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1991) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 6
    • 9544255798 scopus 로고    scopus 로고
    • Secretory granule targeting of atrial nalriuretic peptide correlates with its calcium-mediated aggregation
    • Canaff, L., and V. Brechler. 1996. Secretory granule targeting of atrial nalriuretic peptide correlates with its calcium-mediated aggregation. Proc. Natl. Acad. Sci. USA. 93:9483-9487.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9483-9487
    • Canaff, L.1    Brechler, V.2
  • 7
    • 0028131971 scopus 로고
    • Transport via the regulated secretory pathway in semi-intact PC12 cells: Role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II
    • Carnell, L., and H.P. Moore. 1994. Transport via the regulated secretory pathway in semi-intact PC12 cells: role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II. J. Cell Biol. 127:693-705.
    • (1994) J. Cell Biol. , vol.127 , pp. 693-705
    • Carnell, L.1    Moore, H.P.2
  • 8
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat, E., and W.B. Huttner. 1991. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 115:1505-1519.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 9
    • 0026335806 scopus 로고
    • Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy
    • Chandra, S., E.P.W. Kable, G.H. Morrison, and W.W. Webb. 1991. Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy. J. Cell Sci. 100:747-752.
    • (1991) J. Cell Sci. , vol.100 , pp. 747-752
    • Chandra, S.1    Kable, E.P.W.2    Morrison, G.H.3    Webb, W.W.4
  • 10
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien, C.T., P.L. Bartel, R. Sternglanz, and S. Fields. 1991. The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl. Acad. Sci. USA. 88:9578-9582.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 14
    • 0026034357 scopus 로고
    • β-COP, a 110 kd protein associated with non-clathrin-couted vesicles and the Golgi complex, shows homology to β-adaptin
    • Duden, R., G. Griffiths, R. Frank, P. Argos, and T.E. Kreis. 1991. β-COP, a 110 kd protein associated with non-clathrin-couted vesicles and the Golgi complex, shows homology to β-adaptin. Cell. 64:649-665.
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 15
    • 0002335822 scopus 로고    scopus 로고
    • Protein sorting and vesicular traffic in the Golgi apparatus
    • E.G. Berger and J. Roth, editors. Birkhauser, Basel
    • Farquhar, M.G., and H.-P. Hauri. 1997. Protein sorting and vesicular traffic in the Golgi apparatus. In The Golgi Apparatus. E.G. Berger and J. Roth, editors. Birkhauser, Basel. 63-129.
    • (1997) The Golgi Apparatus , pp. 63-129
    • Farquhar, M.G.1    Hauri, H.-P.2
  • 16
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A.L. Hubbard, S. Flower, and P.B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Flower, S.3    Lazarow, P.B.4
  • 17
    • 0029943272 scopus 로고    scopus 로고
    • High resolution ultrastructural mapping of total calcium: Electron spectroscopic imaging/electron energy loss spectroscopy analysis of a physically/chemically processed nerve-muscle preparation
    • Grohovaz, F., M. Bossi, R. Pezzati, J. Meldolesi, and F.T. Tarelli. 1996. High resolution ultrastructural mapping of total calcium: electron spectroscopic imaging/electron energy loss spectroscopy analysis of a physically/chemically processed nerve-muscle preparation. Proc. Natl. Acad. Sci. USA. 93:4799-4803.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4799-4803
    • Grohovaz, F.1    Bossi, M.2    Pezzati, R.3    Meldolesi, J.4    Tarelli, F.T.5
  • 18
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarente, L. 1983. Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol. 101:181-183.
    • (1983) Methods Enzymol. , vol.101 , pp. 181-183
    • Guarente, L.1
  • 20
    • 0027467164 scopus 로고
    • Disruption of endoplasmic reticulum to Golgi transport leads to the accumulation of large aggregates containing β-COP in pancreatic acinar cells
    • Hendricks, L.C., M. McCaffery, G.E. Palade, and M.G. Farquhar. 1993. Disruption of endoplasmic reticulum to Golgi transport leads to the accumulation of large aggregates containing β-COP in pancreatic acinar cells. Mol. Biol. Cell. 4:413-124.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 413-1124
    • Hendricks, L.C.1    McCaffery, M.2    Palade, G.E.3    Farquhar, M.G.4
  • 21
    • 0029910707 scopus 로고    scopus 로고
    • Rab1a and multiple other Rab proteins are associated with the transcytotic pathway in rat liver
    • Jin, M., L. Saucan, M.G. Farquhar, and G.E. Palade. 1996. Rab1a and multiple other Rab proteins are associated with the transcytotic pathway in rat liver. J. Biol. Chem. 271:30105-30113.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30105-30113
    • Jin, M.1    Saucan, L.2    Farquhar, M.G.3    Palade, G.E.4
  • 22
    • 0027240379 scopus 로고
    • A cystolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • Jones, S.M., J.R. Croshy, J. Salamero, and K.E. Howell. 1993. A cystolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J. Cell Biol. 122:775-788.
    • (1993) J. Cell Biol. , vol.122 , pp. 775-788
    • Jones, S.M.1    Croshy, J.R.2    Salamero, J.3    Howell, K.E.4
  • 23
    • 0022541887 scopus 로고
    • An established MRL/Mp-lpr/lpr cell line with null cell properties produces a B cell differentiation factor(s) that promotes anti-single-stranded DNA antibody production in MRL spleen cell culture
    • Kanai, Y., T. Katagiri, S. Mori, and T. Kubota. 1986. An established MRL/Mp-lpr/lpr cell line with null cell properties produces a B cell differentiation factor(s) that promotes anti-single-stranded DNA antibody production in MRL spleen cell culture. Int. Arch. Allergy Appl. Immunol. 81:92-94.
    • (1986) Int. Arch. Allergy Appl. Immunol. , vol.81 , pp. 92-94
    • Kanai, Y.1    Katagiri, T.2    Mori, S.3    Kubota, T.4
  • 25
    • 0028040761 scopus 로고
    • Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells
    • Kaufman, R.J., M. Swaroop, and P. Murtha-Riel. 1994. Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells. Biochemistry. 33:9813-9819.
    • (1994) Biochemistry , vol.33 , pp. 9813-9819
    • Kaufman, R.J.1    Swaroop, M.2    Murtha-Riel, P.3
  • 26
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K.-H., and M. Michalak. 1997. Calreticulin. Cell. 88:439-143.
    • (1997) Cell , vol.88 , pp. 439-1143
    • Krause, K.-H.1    Michalak, M.2
  • 27
    • 0027401769 scopus 로고
    • A class of membrane proteins with a C-terminal anchor
    • Kulay, U., E. Hartmann, and T.A. Rapoport. 1993. A class of membrane proteins with a C-terminal anchor. Trends Cell Biol. 3:72-75.
    • (1993) Trends Cell Biol. , vol.3 , pp. 72-75
    • Kulay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 29
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory protein from the rough endoplasmic reticulum
    • Lodish, H.F., and N. Kong. 1990. Perturbation of cellular calcium blocks exit of secretory protein from the rough endoplasmic reticulum. J. Biol. Chem. 265: 10893-10899.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 30
    • 0026654505 scopus 로고
    • Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum
    • Lodish, U.F., N. Kong, and L. Wikstrom. 1992. Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J. Biol. Chem. 267:12753-12760.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12753-12760
    • Lodish, U.F.1    Kong, N.2    Wikstrom, L.3
  • 31
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J. Biochem. 95:511-519.
    • (1984) J. Biochem. , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 32
    • 0029088005 scopus 로고
    • Localization of GTPases (GTP-binding proteins) by indirect immunofluorescence and immunoelectron microscopy
    • McCaffery, M., and M.G. Farquhar. 1995. Localization of GTPases (GTP-binding proteins) by indirect immunofluorescence and immunoelectron microscopy. Methods Enzymol. 257:259-279.
    • (1995) Methods Enzymol. , vol.257 , pp. 259-279
    • McCaffery, M.1    Farquhar, M.G.2
  • 33
    • 0016335085 scopus 로고
    • A new fixative for immunoelectron microscopy
    • McLean, W., and P.F. Nakane. 1973. A new fixative for immunoelectron microscopy. J Histochem. Cytochem. 22:1077-1083.
    • (1973) J Histochem. Cytochem. , vol.22 , pp. 1077-1083
    • McLean, W.1    Nakane, P.F.2
  • 36
    • 0028357838 scopus 로고
    • Calcium-binding activity of nucleobindin mediated by an EF hand moiety
    • Miura, K., Y. Kurosawa, and Y. Kanai. 1994. Calcium-binding activity of nucleobindin mediated by an EF hand moiety. Biochem. Biophys. Res. Commun. 199:1388-1393.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1388-1393
    • Miura, K.1    Kurosawa, Y.2    Kanai, Y.3
  • 37
    • 0026657729 scopus 로고
    • Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure
    • Miura, K., K. Titani, Y. Kurosawa, and Y. Kanai. 1992. Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure. Biochem. Biophys. Res. Commun. 187:375-380.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 375-380
    • Miura, K.1    Titani, K.2    Kurosawa, Y.3    Kanai, Y.4
  • 38
    • 0029130768 scopus 로고
    • Interaction of the protein nucleobindin with Gαi2. as revealed by the yeast two-hybrid system
    • Mochizuki, N., M. Hibi, Y. Kanai, and P.A. Insel. 1995. Interaction of the protein nucleobindin with Gαi2. as revealed by the yeast two-hybrid system. FEBS Lett. 373:155-158.
    • (1995) FEBS Lett. , vol.373 , pp. 155-158
    • Mochizuki, N.1    Hibi, M.2    Kanai, Y.3    Insel, P.A.4
  • 39
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby, S.M. 1997. Reversible palmitoylation of signaling proteins. Curr. Opin. Cell Biol. 9:148-154.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 41
    • 0027982729 scopus 로고
    • Calreticulin: Not just another calcium-binding protein
    • Nash, P.D., M. Opas, and M. Michalak. 1994. Calreticulin: Not just another calcium-binding protein. Mol. Cell. Biochem. 135:71-78.
    • (1994) Mol. Cell. Biochem. , vol.135 , pp. 71-78
    • Nash, P.D.1    Opas, M.2    Michalak, M.3
  • 42
    • 0342732290 scopus 로고    scopus 로고
    • The intracellular distribution and expression of calreticulin
    • M. Michalak, editor. R.G. Landes Company. Georgetown
    • Opas, M. 1996. The intracellular distribution and expression of calreticulin. In Calreticulin. M. Michalak, editor. R.G. Landes Company. Georgetown. 31-36.
    • (1996) Calreticulin , pp. 31-36
    • Opas, M.1
  • 43
    • 0039238718 scopus 로고    scopus 로고
    • The roles of calnexin and calreticulin as the endoplasmic reticulum molecular chaperones
    • M. Michalak, editor. R.G. Landes Company, Georgetown
    • Parlati, F., R. Hemming, W.-J. Ou, J.J.M. Bergeron, and D.Y. Thomas. 1996. The roles of calnexin and calreticulin as the endoplasmic reticulum molecular chaperones. In Calreticulin. M. Michalak, editor. R.G. Landes Company, Georgetown. 43-53.
    • (1996) Calreticulin , pp. 43-53
    • Parlati, F.1    Hemming, R.2    Ou, W.-J.3    Bergeron, J.J.M.4    Thomas, D.Y.5
  • 44
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • Pezzati, R., M. Bossi, P. Podini, J. Meldolesi, and F. Grohovaz. 1997. High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells. Mol. Biol. Cell. 8:1501-1512.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 45
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan, T., R. Rizzuto, P. Volpe, and J. Meldolesi. 1994. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74:595-636.
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 46
    • 0031106614 scopus 로고    scopus 로고
    • Coats and vesicle budding
    • Robinson, M.S. 1997. Coats and vesicle budding. Trends Cell Biol. 7:99-102.
    • (1997) Trends Cell Biol. , vol.7 , pp. 99-102
    • Robinson, M.S.1
  • 47
    • 0025361036 scopus 로고
    • The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum
    • Sambrook, J.F. 1990. The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum. Cell. 61:197-199.
    • (1990) Cell , vol.61 , pp. 197-199
    • Sambrook, J.F.1
  • 48
    • 0028270799 scopus 로고
    • Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers
    • Saucan, L., and G.E. Palade. 1994. Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers. J. Cell Biol. 125:733-741.
    • (1994) J. Cell Biol. , vol.125 , pp. 733-741
    • Saucan, L.1    Palade, G.E.2
  • 50
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R.H., and R.D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16:339-346.
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 51
    • 0343617118 scopus 로고    scopus 로고
    • Calreticulin and autoimmunity
    • M. Michalak, editor. R.G. Landes Company, Georgetown
    • Southeimer, R.D., T.Q. Nguyen, S.-T. Cheng, T.-S. Lieu, and J.D. Capra. 1996. Calreticulin and autoimmunity. In Calreticulin. M. Michalak, editor. R.G. Landes Company, Georgetown. 117-134.
    • (1996) Calreticulin , pp. 117-134
    • Southeimer, R.D.1    Nguyen, T.Q.2    Cheng, S.-T.3    Lieu, T.-S.4    Capra, J.D.5
  • 52
    • 0020405935 scopus 로고
    • Purification and characterization of UDP-GalNAc:Polypeptide N-acelylgalactosamine transferase from an ascites hepatoma, AH 66
    • Sugiura, M., T. Kawasaki, and I. Yamashina. 1982. Purification and characterization of UDP-GalNAc:polypeptide N-acelylgalactosamine transferase from an ascites hepatoma, AH 66. J. Biol. Chem. 257:9501-9507.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9501-9507
    • Sugiura, M.1    Kawasaki, T.2    Yamashina, I.3
  • 53
    • 0030822623 scopus 로고    scopus 로고
    • Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities
    • Taylor, R.S., S.M. Jones, R.H. Dahl, M.H. Nordeen, and K.E. Howell. 1997. Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities. Mol. Biol. Cell. 8:1911-1931.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1911-1931
    • Taylor, R.S.1    Jones, S.M.2    Dahl, R.H.3    Nordeen, M.H.4    Howell, K.E.5
  • 57
    • 0028965878 scopus 로고
    • Isolation, characterization, and primary structure of a calcium-binding 63-kD bone protein
    • Wendel, M., Y. Sommarin, T. Bergman, and D. Heinegard. 1995. Isolation, characterization, and primary structure of a calcium-binding 63-kD bone protein. J. Biol. Chem. 270:6125-6133.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6125-6133
    • Wendel, M.1    Sommarin, Y.2    Bergman, T.3    Heinegard, D.4
  • 58
    • 0029921620 scopus 로고    scopus 로고
    • A 12-residue-long polyleucine tail is sufficient to anchor synaptobrevin to the endoplasmic reticulum membrane
    • Whitley, P., E. Grahn, U. Kutay, T.A. Rapoport, and G. von Heijne. 1996. A 12-residue-long polyleucine tail is sufficient to anchor synaptobrevin to the endoplasmic reticulum membrane. J. Biol Chem. 271:7583-7586.
    • (1996) J. Biol Chem. , vol.271 , pp. 7583-7586
    • Whitley, P.1    Grahn, E.2    Kutay, U.3    Rapoport, T.A.4    Von Heijne, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.