메뉴 건너뛰기




Volumn 18, Issue 3, 2007, Pages 839-849

Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; COAT PROTEIN COMPLEX II; FUNGAL PROTEIN; MEMBRANE PROTEIN; PROTEIN SEC16; PROTEIN SEC16L; PROTEIN SEC16S; PROTEIN SEC23; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 33947104123     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-08-0707     Document Type: Article
Times cited : (124)

References (45)
  • 1
    • 0030742746 scopus 로고    scopus 로고
    • Membrane dynamics at the endoplasmic reticulum-Golgi interface
    • Bannykh, S. I., and Balch, W. E. (1997). Membrane dynamics at the endoplasmic reticulum-Golgi interface. J. Cell Biol. 138, 1-4.
    • (1997) J. Cell Biol , vol.138 , pp. 1-4
    • Bannykh, S.I.1    Balch, W.E.2
  • 2
    • 0036799651 scopus 로고    scopus 로고
    • De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
    • Bevis, B. J., Hammond, A. T., Reinke, C. A., and Glick, B. S. (2002). De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat. Cell Biol. 4, 750-756.
    • (2002) Nat. Cell Biol , vol.4 , pp. 750-756
    • Bevis, B.J.1    Hammond, A.T.2    Reinke, C.A.3    Glick, B.S.4
  • 3
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sari NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • Bielli, A., Haney, C. J., Gabreski, G., Watkins, S. C., Bannykh, S. I., and Aridor, M. (2005). Regulation of Sari NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J. Cell Biol. 171, 919-924.
    • (2005) J. Cell Biol , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 5
    • 0004630953 scopus 로고    scopus 로고
    • Insights into Golgi function through mutants in yeast and animal cells
    • ed. E. G. Berger and J. Roth, Basel, Switzerland: Birkhäuser Verlag
    • Duden, R., and Schekman, R. (1997). Insights into Golgi function through mutants in yeast and animal cells. In: The Golgi Apparatus, ed. E. G. Berger and J. Roth, Basel, Switzerland: Birkhäuser Verlag, 219-246.
    • (1997) The Golgi Apparatus , pp. 219-246
    • Duden, R.1    Schekman, R.2
  • 6
    • 0028803617 scopus 로고
    • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p
    • Espenshade, P., Gimeno, R. E., Holzmacher, E., Teung, P., and Kaiser, C. A. (1995). Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J. Cell Biol. 131, 311-324.
    • (1995) J. Cell Biol , vol.131 , pp. 311-324
    • Espenshade, P.1    Gimeno, R.E.2    Holzmacher, E.3    Teung, P.4    Kaiser, C.A.5
  • 7
    • 0028885714 scopus 로고
    • SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation
    • Gimeno, R. E., Espenshade, P., and Kaiser, C. A. (1995). SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation. J. Cell Biol. 131, 325-338.
    • (1995) J. Cell Biol , vol.131 , pp. 325-338
    • Gimeno, R.E.1    Espenshade, P.2    Kaiser, C.A.3
  • 8
    • 0029905137 scopus 로고    scopus 로고
    • COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p
    • Gimeno, R. E., Espenshade, P., and Kaiser, C. A. (1996). COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Mol. Biol. Cell 7, 1815-1823.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1815-1823
    • Gimeno, R.E.1    Espenshade, P.2    Kaiser, C.A.3
  • 9
    • 0026706469 scopus 로고
    • Development of the yeast Pichia pastoris as a model organism for a genetic and molecular analysis of peroxisome assembly
    • Gould, S. J., McCollum, D., Spong, A. P., Heyman, J. A., and Subramani, S. (1992). Development of the yeast Pichia pastoris as a model organism for a genetic and molecular analysis of peroxisome assembly. Yeast 8, 613-628.
    • (1992) Yeast , vol.8 , pp. 613-628
    • Gould, S.J.1    McCollum, D.2    Spong, A.P.3    Heyman, J.A.4    Subramani, S.5
  • 10
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond, A. T., and Glick, B. S. (2000). Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell 11, 3013-3030.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 12
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., Halladay, J., and Craig, E. A. (1996). Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 13
    • 12844249950 scopus 로고    scopus 로고
    • Nm23H2 facilitates coat protein complex II assembly and endoplasmic reticulum export in mammalian cells
    • Kapetanovich, L., Baughman, C., and Lee, T. H. (2005). Nm23H2 facilitates coat protein complex II assembly and endoplasmic reticulum export in mammalian cells. Mol. Biol. Cell 16, 835-848.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 835-848
    • Kapetanovich, L.1    Baughman, C.2    Lee, T.H.3
  • 15
    • 0032517780 scopus 로고    scopus 로고
    • Role of Xklp3, a subunit of the Xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus
    • Le Bot, N., Antony, C., White, J., Karsenti, E., and Vernos, I. (1998). Role of Xklp3, a subunit of the Xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus. J. Cell Biol. 143, 1559-1573.
    • (1998) J. Cell Biol , vol.143 , pp. 1559-1573
    • Le Bot, N.1    Antony, C.2    White, J.3    Karsenti, E.4    Vernos, I.5
  • 16
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • Lee, M. C., Orci, L., Hamamoto, S., Futai, E., Ravazzola, M., and Schekman, R. (2005). Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122, 605-617.
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 17
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt, A. D., and Hauri, H.-P. (1993). Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol. Biol. Cell 4, 679-693.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.-P.2
  • 18
    • 0842344613 scopus 로고    scopus 로고
    • Recent advances in the (molecular) phylogeny of vertebrates
    • Meyer, A., and Zardoya, R. (2003). Recent advances in the (molecular) phylogeny of vertebrates. Annu. Rev. Ecol. Evol. Syst. 34, 311-338.
    • (2003) Annu. Rev. Ecol. Evol. Syst , vol.34 , pp. 311-338
    • Meyer, A.1    Zardoya, R.2
  • 19
    • 0035513546 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of the cDNA coding for a novel regucalcin gene promoter region-related protein in rat, mouse and human liver
    • Misawa, H., and Yamaguchi, M. (2001). Molecular cloning and sequencing of the cDNA coding for a novel regucalcin gene promoter region-related protein in rat, mouse and human liver. Int. J. Mol. Med. 8, 513-520.
    • (2001) Int. J. Mol. Med , vol.8 , pp. 513-520
    • Misawa, H.1    Yamaguchi, M.2
  • 20
  • 21
    • 0031589004 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Nagase, T., Ishikawa, K., Nakajima, D., Ohira, M., Seki, N., Miyajima, N., Tanaka, A., Kotani, H., Nomura, N., and Ohara, O. (1997). Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 4, 141-150.
    • (1997) DNA Res , vol.4 , pp. 141-150
    • Nagase, T.1    Ishikawa, K.2    Nakajima, D.3    Ohira, M.4    Seki, N.5    Miyajima, N.6    Tanaka, A.7    Kotani, H.8    Nomura, N.9    Ohara, O.10
  • 22
    • 0036932506 scopus 로고    scopus 로고
    • Construction of expression-ready cDNA clones for KIAA genes: Manual curation of 330 KIAA cDNA clones
    • Nakajima, D., Okazaki, N., Yamakura, H., Kikuno, R., Ohara, O., and Nagase, T. (2002). Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 9, 99-106.
    • (2002) DNA Res , vol.9 , pp. 99-106
    • Nakajima, D.1    Okazaki, N.2    Yamakura, H.3    Kikuno, R.4    Ohara, O.5    Nagase, T.6
  • 24
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G. (1975). Intracellular aspects of the process of protein synthesis. Science 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 25
    • 0002471181 scopus 로고    scopus 로고
    • Three-dimensional structure of the Golgi apparatus in mammalian cells
    • ed. E. G. Berger and J. Roth, Basel, Switzerland: Birkhäuser Verlag
    • Rambourg, A., and Clermont, Y. (1997). Three-dimensional structure of the Golgi apparatus in mammalian cells. In: The Golgi Apparatus, ed. E. G. Berger and J. Roth, Basel, Switzerland: Birkhäuser Verlag, 37-61.
    • (1997) The Golgi Apparatus , pp. 37-61
    • Rambourg, A.1    Clermont, Y.2
  • 26
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese, O. W., Soderholm, J., Bevis, B. J., Sears, I. B., O'Connor, J., Williamson, E. K., and Glick, B. S. (1999). Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 145, 69-81.
    • (1999) J. Cell Biol , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 27
    • 33644614728 scopus 로고    scopus 로고
    • Nuclear localization of a novel protein, RGPR-p117, in cloned normal rat kidney proximal tubular epithelial cells
    • Sawada, N., Nakagawa, T., Murata, T., and Yamaguchi, M. (2005). Nuclear localization of a novel protein, RGPR-p117, in cloned normal rat kidney proximal tubular epithelial cells. Int. J. Mol. Med. 16, 809-814.
    • (2005) Int. J. Mol. Med , vol.16 , pp. 809-814
    • Sawada, N.1    Nakagawa, T.2    Murata, T.3    Yamaguchi, M.4
  • 28
    • 21644480608 scopus 로고    scopus 로고
    • A novel regucalcin gene promoter region-related protein: Comparison of nucleotide and amino acid sequences in vertebrate species
    • Sawada, N., and Yamaguchi, M. (2005a). A novel regucalcin gene promoter region-related protein: comparison of nucleotide and amino acid sequences in vertebrate species. Int. J. Mol. Med. 15, 97-104.
    • (2005) Int. J. Mol. Med , vol.15 , pp. 97-104
    • Sawada, N.1    Yamaguchi, M.2
  • 29
    • 33644878289 scopus 로고    scopus 로고
    • Overexpression of RGPR-p117 enhances regucalcin gene expression in cloned normal rat kidney proximal tubular epithelial cells
    • Sawada, N., and Yamaguchi, M. (2005b). Overexpression of RGPR-p117 enhances regucalcin gene expression in cloned normal rat kidney proximal tubular epithelial cells. Int. J. Mol. Med. 16, 1049-1055.
    • (2005) Int. J. Mol. Med , vol.16 , pp. 1049-1055
    • Sawada, N.1    Yamaguchi, M.2
  • 30
    • 0030771853 scopus 로고    scopus 로고
    • COPII subunit interactions in the assembly of the vesicle coat
    • Shaywitz, D. A., Espenshade, P. J., Gimeno, R. E., and Kaiser, C. A. (1997). COPII subunit interactions in the assembly of the vesicle coat. J. Biol. Chem. 272, 25413-25416.
    • (1997) J. Biol. Chem , vol.272 , pp. 25413-25416
    • Shaywitz, D.A.1    Espenshade, P.J.2    Gimeno, R.E.3    Kaiser, C.A.4
  • 33
    • 33645211019 scopus 로고    scopus 로고
    • Human Sec31B: A family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat
    • Stankewich, M. C., Stabach, P. R., and Morrow, J. S. (2006). Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat. J. Cell Sci. 119, 958-969.
    • (2006) J. Cell Sci , vol.119 , pp. 958-969
    • Stankewich, M.C.1    Stabach, P.R.2    Morrow, J.S.3
  • 34
    • 0037296519 scopus 로고    scopus 로고
    • De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites
    • Stephens, D. J. (2003). De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites. EMBO Rep. 4, 210-217.
    • (2003) EMBO Rep , vol.4 , pp. 210-217
    • Stephens, D.J.1
  • 35
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie, B., White, J., Röttger, S., Stelzer, E.H.K., Suganuma, T., and Nilsson, T. (1998). Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143, 1505-1521.
    • (1998) J. Cell Biol , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Röttger, S.3    Stelzer, E.H.K.4    Suganuma, T.5    Nilsson, T.6
  • 36
    • 0037119988 scopus 로고    scopus 로고
    • Sec16p potentiates the action of COPII proteins to bud transport vesicles
    • Supek, F., Madden, D. T., Hamamoto, S., Orci, L., and Schekman, R. (2002). Sec16p potentiates the action of COPII proteins to bud transport vesicles. J. Cell Biol. 158, 1029-1038.
    • (2002) J. Cell Biol , vol.158 , pp. 1029-1038
    • Supek, F.1    Madden, D.T.2    Hamamoto, S.3    Orci, L.4    Schekman, R.5
  • 38
    • 0000505092 scopus 로고    scopus 로고
    • The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Tang, B. L., Peter, F., Krijnse-Locker, J., Low, S., Griffiths, G., and Hong, W. (1997). The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol. Cell Biol. 17, 256-266.
    • (1997) Mol. Cell Biol , vol.17 , pp. 256-266
    • Tang, B.L.1    Peter, F.2    Krijnse-Locker, J.3    Low, S.4    Griffiths, G.5    Hong, W.6
  • 39
    • 20544451051 scopus 로고    scopus 로고
    • COPII and exit from the endoplasmic reticulum
    • Tang, B. L., Wang, Y., Ong, Y. S., and Hong, W. (2005). COPII and exit from the endoplasmic reticulum. Biochim. Biophys. Acta 1744, 293-303.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 293-303
    • Tang, B.L.1    Wang, Y.2    Ong, Y.S.3    Hong, W.4
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 20544471158 scopus 로고    scopus 로고
    • ER-to-Golgi transport: Form and formation of vesicular and tubular carriers
    • Watson, P., and Stephens, D. J. (2005). ER-to-Golgi transport: form and formation of vesicular and tubular carriers. Biochim. Biophys. Acta 1744, 304-315.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 304-315
    • Watson, P.1    Stephens, D.J.2
  • 42
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • Watson, P., Townley, A. K., Koka, P., Palmer, K. J., and Stephens, D. J. (2006). Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7, 1678-1687.
    • (2006) Traffic , vol.7 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 43
    • 0034946168 scopus 로고    scopus 로고
    • The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export
    • Weissman, J. T., Plumer, H., and Balch, W. E. (2001). The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export. Traffic 2, 465-475.
    • (2001) Traffic , vol.2 , pp. 465-475
    • Weissman, J.T.1    Plumer, H.2    Balch, W.E.3
  • 44
    • 0037446096 scopus 로고    scopus 로고
    • Novel protein RGPR-p 117, the gene expression in physiologic state and the binding activity to regucalcin gene promoter region in rat liver
    • Yamaguchi, M., Misawa, H., and Ma, Z. J. (2003). Novel protein RGPR-p 117, the gene expression in physiologic state and the binding activity to regucalcin gene promoter region in rat liver. J. Cell. Biochem. 88, 1092-1100.
    • (2003) J. Cell. Biochem , vol.88 , pp. 1092-1100
    • Yamaguchi, M.1    Misawa, H.2    Ma, Z.J.3
  • 45
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D. A., Violin, J. D., Newton, A. C., and Tsien, R. Y. (2002). Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.