메뉴 건너뛰기




Volumn 58, Issue 6, 2017, Pages 1103-1117

A non-classical member of the protein disulfide isomerase family, pdi7 of arabidopsis thaliana, localizes to the cis-golgi and endoplasmic reticulum membranes

Author keywords

cargo receptor; cis Golgi; endoplasmic reticulum; membrane protein traffic; protein disulfide isomerase; Secretory pathway

Indexed keywords

ARABIDOPSIS PROTEIN; GREEN FLUORESCENT PROTEIN; PROTEIN DISULFIDE ISOMERASE;

EID: 85021170976     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pcx057     Document Type: Article
Times cited : (10)

References (79)
  • 1
    • 77952852840 scopus 로고    scopus 로고
    • Maximum yields of microsomal-Type membranes from small amounts of plant material without requiring ultracentrifugation
    • Abas, L., and Luschnig, C. (2010) Maximum yields of microsomal-Type membranes from small amounts of plant material without requiring ultracentrifugation. Anal. Biochem. 401: 217-227.
    • (2010) Anal. Biochem. , vol.401 , pp. 217-227
    • Abas, L.1    Luschnig, C.2
  • 2
    • 0028267092 scopus 로고
    • Gp74, a membrane glycoprotein of the cis-Golgi network that cycles through the endoplasmic reticulum and intermediate compartment
    • Alcalde, J., Egea, G., and Sandoval, I.V. (1994) gp74, a membrane glycoprotein of the cis-Golgi network that cycles through the endoplasmic reticulum and intermediate compartment. J. Cell Biol. 124: 649-665.
    • (1994) J. Cell Biol. , vol.124 , pp. 649-665
    • Alcalde, J.1    Egea, G.2    Sandoval, I.V.3
  • 3
    • 51349130209 scopus 로고    scopus 로고
    • Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds
    • Andéme Ondzighi C., Christopher, D.A., Cho, E.J., Chang, S.C., and Staehelin, L.A. (2008) Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds. Plant Cell 20: 2205-2220.
    • (2008) Plant Cell , vol.20 , pp. 2205-2220
    • Andéme Ondzighi, C.1    Christopher, D.A.2    Cho, E.J.3    Chang, S.C.4    Staehelin, L.A.5
  • 4
    • 0141753993 scopus 로고    scopus 로고
    • Thiol-mediated protein retention in the endoplasmic reticulum: The role of ERp44
    • Anelli, T., Alessio, M., Bachi, A., Bergamelli, L., Bertoli, G., Camerini, S., et al. (2003) Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J. 22: 5015-5022
    • (2003) EMBO J. , vol.22 , pp. 5015-5022
    • Anelli, T.1    Alessio, M.2    Bachi, A.3    Bergamelli, L.4    Bertoli, G.5    Camerini, S.6
  • 5
    • 34948899397 scopus 로고    scopus 로고
    • Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis
    • Anelli, T., Ceppi, S., Bergamelli, L., Cortini, M., Masciarelli, S., Valetti, C., et al. (2007) Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis. EMBO J. 26: 4177-4188.
    • (2007) EMBO J. , vol.26 , pp. 4177-4188
    • Anelli, T.1    Ceppi, S.2    Bergamelli, L.3    Cortini, M.4    Masciarelli, S.5    Valetti, C.6
  • 6
    • 0033202958 scopus 로고    scopus 로고
    • The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
    • Appenzeller, C., Andersson, H., Kappeler, F., and Hauri, H.P. (1999) The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat. Cell Biol. 1: 330-334.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 330-334
    • Appenzeller, C.1    Andersson, H.2    Kappeler, F.3    Hauri, H.P.4
  • 7
    • 33845917867 scopus 로고    scopus 로고
    • Isolation and proteomic analysis of rice Golgi membranes: Cis-Golgi membranes labeled with GFP-SYP31
    • Asakura, T., Hirose, S., Katamine, H., Kitajima, A., Hori, H., Sato, M.H., et al. (2006) Isolation and proteomic analysis of rice Golgi membranes: cis-Golgi membranes labeled with GFP-SYP31. Plant Biotechnol. 23: 475-485.
    • (2006) Plant Biotechnol. , vol.23 , pp. 475-485
    • Asakura, T.1    Hirose, S.2    Katamine, H.3    Kitajima, A.4    Hori, H.5    Sato, M.H.6
  • 8
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh, S.I., Rowe, T., and Balch, W.E. (1996) The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135: 19-35
    • (1996) J. Cell Biol. , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 9
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • Barlowe, C., Orci, L., Yeung, T., Hosobuchi, M., Hamamoto, S., Salama, N., et al. (1994) COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77: 895-907.
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1    Orci, L.2    Yeung, T.3    Hosobuchi, M.4    Hamamoto, S.5    Salama, N.6
  • 10
    • 0029910214 scopus 로고    scopus 로고
    • Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport
    • Belden, W.J., and Barlowe, C. (1996) Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. J. Biol. Chem. 271: 26939-26946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26939-26946
    • Belden, W.J.1    Barlowe, C.2
  • 11
    • 0035900480 scopus 로고    scopus 로고
    • Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles
    • Belden, W.J., and Barlowe, C. (2001) Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles. Science 294: 1528-1531.
    • (2001) Science , vol.294 , pp. 1528-1531
    • Belden, W.J.1    Barlowe, C.2
  • 12
    • 84878257598 scopus 로고    scopus 로고
    • The crystal structure of the lumenal domain of Erv41p, a protein involved in transport between the endoplasmic reticulum and Golgi apparatus
    • Biterova, E.I., Svärd, M., Possner, D.D., and Guy, J.E. (2013) The crystal structure of the lumenal domain of Erv41p, a protein involved in transport between the endoplasmic reticulum and Golgi apparatus. J. Mol. Biol. 425: 2208-2218.
    • (2013) J. Mol. Biol. , vol.425 , pp. 2208-2218
    • Biterova, E.I.1    Svärd, M.2    Possner, D.D.3    Guy, J.E.4
  • 13
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network
    • Boevink, P., Oparka, K., Santa Cruz, S., Martin, B., Betteridge, A., and Hawes, C. (1998) Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15: 441-447.
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1    Oparka, K.2    Santa Cruz, S.3    Martin, B.4    Betteridge, A.5    Hawes, C.6
  • 14
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • Brandizzi, F., and Barlowe, C. (2013) Organization of the ER-Golgi interface for membrane traffic control. Nat. Rev. Mol. Cell Biol. 14: 382-392
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 15
    • 8744259809 scopus 로고    scopus 로고
    • Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-Treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46
    • Breuza, L., Halbeisen, R., Jenö, P., Otte, S., Barlowe, C., Hong, W., et al. (2004) Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-Treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279: 47242-47253.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47242-47253
    • Breuza, L.1    Halbeisen, R.2    Jenö, P.3    Otte, S.4    Barlowe, C.5    Hong, W.6
  • 16
    • 51849151243 scopus 로고    scopus 로고
    • The syntaxins SYP31 and SYP81 control ER-Golgi trafficking in the plant secretory pathway
    • Bubeck, J., Scheuring, D., Hummel, E., Langhans, M., Viotti, C., Foresti, O., et al. (2008) The syntaxins SYP31 and SYP81 control ER-Golgi trafficking in the plant secretory pathway. Traffic 9: 1629-1652.
    • (2008) Traffic , vol.9 , pp. 1629-1652
    • Bubeck, J.1    Scheuring, D.2    Hummel, E.3    Langhans, M.4    Viotti, C.5    Foresti, O.6
  • 17
    • 33750499937 scopus 로고    scopus 로고
    • Erv26p directs proalkaline phosphatase into endoplasmic reticulum-derived coat protein complex II transport vesicles
    • Bue, C.A., Bentivoglio, C.M., and Barlowe, C. (2006) Erv26p directs proalkaline phosphatase into endoplasmic reticulum-derived coat protein complex II transport vesicles. Mol. Biol. Cell 17: 4780-4789.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4780-4789
    • Bue, C.A.1    Bentivoglio, C.M.2    Barlowe, C.3
  • 19
    • 84855691883 scopus 로고    scopus 로고
    • Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor
    • Cho, E.J., Yuen, C.Y., Kang, B.H., Ondzighi, C.A., Staehelin, L.A., and Christopher, D.A. (2011) Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor. Mol. Cells 32: 459-475
    • (2011) Mol. Cells , vol.32 , pp. 459-475
    • Cho, E.J.1    Yuen, C.Y.2    Kang, B.H.3    Ondzighi, C.A.4    Staehelin, L.A.5    Christopher, D.A.6
  • 20
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16: 735-743.
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 21
    • 77953148190 scopus 로고    scopus 로고
    • ERp44 and ERGIC-53 synergize in coupling efficiency and fidelity of IgM polymerization and secretion
    • Cortini, M., and Sitia, R. (2010) ERp44 and ERGIC-53 synergize in coupling efficiency and fidelity of IgM polymerization and secretion. Traffic 11: 651-659
    • (2010) Traffic , vol.11 , pp. 651-659
    • Cortini, M.1    Sitia, R.2
  • 22
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • daSilva, L.L., Snapp, E.L., Denecke, J., Lippincott-Schwartz, J., Hawes, C., and Brandizzi, F. (2004) Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 16: 1753-1771.
    • (2004) Plant Cell , vol.16 , pp. 1753-1771
    • DaSilva, L.L.1    Snapp, E.L.2    Denecke, J.3    Lippincott-Schwartz, J.4    Hawes, C.5    Brandizzi, F.6
  • 23
    • 77953642000 scopus 로고    scopus 로고
    • Protein sorting receptors in the early secretory pathway
    • Dancourt, J., and Barlowe, C. (2010) Protein sorting receptors in the early secretory pathway. Annu. Rev. Biochem. 79: 777-802.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 777-802
    • Dancourt, J.1    Barlowe, C.2
  • 24
    • 0026623115 scopus 로고
    • ADPribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes
    • Donaldson, J.G., Cassel, D., Kahn, R.A., and Klausner, R.D. (1992) ADPribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89: 6408-6412.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 25
    • 84876106182 scopus 로고    scopus 로고
    • Cis-Golgi cisternal assembly and biosynthetic activation occur sequentially in plants and algae
    • Donohoe, B.S., Kang, B.H., Gerl, M.J., Gergely, Z.R., McMichael, C.M., Bednarek, S.Y., et al. (2013) Cis-Golgi cisternal assembly and biosynthetic activation occur sequentially in plants and algae. Traffic 14: 551-567
    • (2013) Traffic , vol.14 , pp. 551-567
    • Donohoe, B.S.1    Kang, B.H.2    Gerl, M.J.3    Gergely, Z.R.4    McMichael, C.M.5    Bednarek, S.Y.6
  • 26
    • 33846041607 scopus 로고    scopus 로고
    • Identification and characterization of COPIa-And COPIb-Type vesicle classes associated with plant and algal Golgi
    • Donohoe, B.S., Kang, B.H., and Staehelin, L.A. (2007) Identification and characterization of COPIa-And COPIb-Type vesicle classes associated with plant and algal Golgi. Proc. Natl. Acad. Sci. USA 104: 163-168.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 163-168
    • Donohoe, B.S.1    Kang, B.H.2    Staehelin, L.A.3
  • 27
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman, J.C., Ellis, L., Blacher, R.W., Roth, R.A., and Rutter, W.J. (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317: 267-270.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 28
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand, A.R., Cuozzo, J.W., and Kaiser, C.A. (2000) Pathways for protein disulphide bond formation. Trends Cell Biol. 10: 203-210.
    • (2000) Trends Cell Biol. , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 29
    • 79953287551 scopus 로고    scopus 로고
    • Endoglycosidase and glycoamidase release of N-linked glycans
    • Freeze, H.H., and Kranz, C. (2010) Endoglycosidase and glycoamidase release of N-linked glycans. Curr. Protoc. Protein Sci. 62: 12.4.1-12.4.25
    • (2010) Curr. Protoc. Protein Sci. , vol.62 , pp. 1241-12425
    • Freeze, H.H.1    Kranz, C.2
  • 30
    • 0343487717 scopus 로고    scopus 로고
    • Characterization of brefeldin A induced vesicular structures containing cycling proteins of the intermediate compartment/ cis-Golgi network
    • Füllekrug, J., Sönnichsen, B., Schäfer, U., Nguyen Van, P., Söling, H.D., and Mieskes, G. (1997) Characterization of brefeldin A induced vesicular structures containing cycling proteins of the intermediate compartment/ cis-Golgi network. FEBS Lett. 404: 75-81.
    • (1997) FEBS Lett. , vol.404 , pp. 75-81
    • Füllekrug, J.1    Sönnichsen, B.2    Schäfer, U.3    Van, N.P.4    Söling, H.D.5    Mieskes, G.6
  • 31
    • 84937468247 scopus 로고    scopus 로고
    • Regulation and quality control of adiponectin assembly by endoplasmic reticulum chaperone ERp44
    • Hampe, L., Radjainia, M., Xu C., Harris, P.W., Bashiri, G., Goldstone, D.C., et al. (2015) Regulation and quality control of adiponectin assembly by endoplasmic reticulum chaperone ERp44. J. Biol. Chem. 290: 18111-18123.
    • (2015) J. Biol. Chem. , vol.290 , pp. 18111-18123
    • Hampe, L.1    Radjainia, M.2    Xu, C.3    Harris, P.W.4    Bashiri, G.5    Goldstone, D.C.6
  • 32
    • 23844459888 scopus 로고    scopus 로고
    • Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments
    • Inadome, H., Noda, Y., Adachi, H., and Yoda, K. (2005) Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments. Mol. Cell. Biol. 25: 7696-7710.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7696-7710
    • Inadome, H.1    Noda, Y.2    Adachi, H.3    Yoda, K.4
  • 33
    • 84871897748 scopus 로고    scopus 로고
    • Cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells
    • Ito, Y., Uemura, T., Shoda, K., Fujimoto, M., Ueda, T., and Nakano, A. (2012) cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells. Mol. Biol. Cell 23: 3203-3214.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3203-3214
    • Ito, Y.1    Uemura, T.2    Shoda, K.3    Fujimoto, M.4    Ueda, T.5    Nakano, A.6
  • 34
    • 84870826366 scopus 로고    scopus 로고
    • Molecular basis for recognition of dilysine trafficking motifs by COPI
    • Jackson, L.P., Lewis, M., Kent, H.M., Edeling, M.A., Evans, P.R., Duden, R., et al. (2012) Molecular basis for recognition of dilysine trafficking motifs by COPI. Dev. Cell 23: 1255-1262.
    • (2012) Dev. Cell , vol.23 , pp. 1255-1262
    • Jackson, L.P.1    Lewis, M.2    Kent, H.M.3    Edeling, M.A.4    Evans, P.R.5    Duden, R.6
  • 35
    • 79751495582 scopus 로고    scopus 로고
    • Electron tomography of RabA4b-And PI-4Kb1-labeled trans Golgi network compartments in Arabidopsis
    • Kang, B.H., Nielsen, E., Preuss, M.L., Mastronarde, D., and Staehelin, L.A. (2011) Electron tomography of RabA4b-And PI-4Kb1-labeled trans Golgi network compartments in Arabidopsis. Traffic 12: 313-329
    • (2011) Traffic , vol.12 , pp. 313-329
    • Kang, B.H.1    Nielsen, E.2    Preuss, M.L.3    Mastronarde, D.4    Staehelin, L.A.5
  • 36
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., and Creighton, T.E. (1997) The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr. Bio.l 7: 239-245.
    • (1997) Curr. Bio.l , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 39
    • 0028643562 scopus 로고
    • Coatomer is essential for retrieval of dilysine-Tagged proteins to the endoplasmic reticulum
    • Letourneur, F., Gaynor, E.C., Hennecke, S., Demolliére, C., Duden, R., Emr, S.D., et al. (1994) Coatomer is essential for retrieval of dilysine-Tagged proteins to the endoplasmic reticulum. Cell 79: 1199-1207.
    • (1994) Cell , vol.79 , pp. 1199-1207
    • Letourneur, F.1    Gaynor, E.C.2    Hennecke, S.3    Demolliére, C.4    Duden, R.5    Emr, S.D.6
  • 40
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and Pelham, H.R. (1992) Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 68: 353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.2
  • 41
    • 49749118645 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZIP60 modulates the response in Arabidopsis thaliana
    • Lu, D.P., and Christopher D.A. (2008) Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZIP60 modulates the response in Arabidopsis thaliana. Mol. Genet. Genomics 280: 199-210.
    • (2008) Mol. Genet. Genomics , vol.280 , pp. 199-210
    • Lu, D.P.1    Christopher, D.A.2
  • 42
    • 0040958829 scopus 로고    scopus 로고
    • A simple, rapid and quantitative method for preparing Arabidopsis protein extracts for immunoblot analysis
    • Martínez-García, J.F., Monte, E., and Quail, P.H. (1999) A simple, rapid and quantitative method for preparing Arabidopsis protein extracts for immunoblot analysis. Plant J. 20: 251-257
    • (1999) Plant J. , vol.20 , pp. 251-257
    • Martínez-García, J.F.1    Monte, E.2    Quail, P.H.3
  • 44
    • 70450224864 scopus 로고    scopus 로고
    • Evolution and diversity of the Golgi body
    • Mowbrey, K., and Dacks, J.B. (2009) Evolution and diversity of the Golgi body. FEBS Lett. 583: 3738-3745.
    • (2009) FEBS Lett. , vol.583 , pp. 3738-3745
    • Mowbrey, K.1    Dacks, J.B.2
  • 45
    • 34848907786 scopus 로고    scopus 로고
    • Protein lipidation
    • Nadolski, M.J., and Linder, M.E. (2007) Protein lipidation. FEBS J. 274: 5202-5210.
    • (2007) FEBS J. , vol.274 , pp. 5202-5210
    • Nadolski, M.J.1    Linder, M.E.2
  • 47
    • 34548487513 scopus 로고    scopus 로고
    • A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants
    • Nelson, B.K., Cai, X., and Nebenführ, A. (2007) A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J. 51: 1126-1136.
    • (2007) Plant J. , vol.51 , pp. 1126-1136
    • Nelson, B.K.1    Cai, X.2    Nebenführ, A.3
  • 48
    • 77952061161 scopus 로고    scopus 로고
    • Svp26 facilitates endoplasmic reticulum to golgi transport of a set of mannosyltransferases in Saccharomyces cerevisiae
    • Noda, Y., and Yoda, K. (2010) Svp26 facilitates endoplasmic reticulum to golgi transport of a set of mannosyltransferases in Saccharomyces cerevisiae. J. Biol. Chem. 285: 15420-15429.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15420-15429
    • Noda, Y.1    Yoda, K.2
  • 49
    • 0037446895 scopus 로고    scopus 로고
    • Mammalian Erv46 localizes to the endoplasmic reticulum-Golgi intermediate compartment and to cis-Golgi cisternae
    • Orci, L., Ravazzola, M., Mack, G.J., Barlowe, C., and Otte, S. (2003) Mammalian Erv46 localizes to the endoplasmic reticulum-Golgi intermediate compartment and to cis-Golgi cisternae. Proc. Natl. Acad. Sci. USA 100: 4586-4591
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4586-4591
    • Orci, L.1    Ravazzola, M.2    Mack, G.J.3    Barlowe, C.4    Otte, S.5
  • 50
    • 0026046098 scopus 로고
    • Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm
    • Orci, L., Ravazzola, M., Meda, P., Holcomb, C., Moore, H.P., Hicke, L., et al. (1991) Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm. Proc. Natl. Acad. Sci. USA 88: 8611-8615.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8611-8615
    • Orci, L.1    Ravazzola, M.2    Meda, P.3    Holcomb, C.4    Moore, H.P.5    Hicke, L.6
  • 51
    • 0034641703 scopus 로고    scopus 로고
    • Anterograde flow of cargo across the golgi stack potentially mediated via bidirectional 'percolating' COPI vesicles
    • Orci, L., Ravazzola, M., Volchuk, A., Engel, T., Gmachl, M., Amherdt, M., et al. (2000) Anterograde flow of cargo across the golgi stack potentially mediated via bidirectional 'percolating' COPI vesicles. Proc. Natl. Acad. Sci. USA 97: 10400-10405.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10400-10405
    • Orci, L.1    Ravazzola, M.2    Volchuk, A.3    Engel, T.4    Gmachl, M.5    Amherdt, M.6
  • 52
    • 0034802410 scopus 로고    scopus 로고
    • Three-dimensional analysis of syncytial-Type cell plates during endosperm cellularization visualized by high resolution electron tomography
    • Otegui, M.S., Mastronarde, D.N., Kang, B.H., Bednarek, S.Y., and Staehelin, L.A. (2001) Three-dimensional analysis of syncytial-Type cell plates during endosperm cellularization visualized by high resolution electron tomography. Plant Cell 13: 2033-2051.
    • (2001) Plant Cell , vol.13 , pp. 2033-2051
    • Otegui, M.S.1    Mastronarde, D.N.2    Kang, B.H.3    Bednarek, S.Y.4    Staehelin, L.A.5
  • 53
    • 0037112783 scopus 로고    scopus 로고
    • The Erv41p-Erv46p complex: Multiple export signals are required in trans for COPII-dependent transport from the ER
    • Otte, S., and Barlowe, C. (2002) The Erv41p-Erv46p complex: multiple export signals are required in trans for COPII-dependent transport from the ER. EMBO J. 21: 6095-6104
    • (2002) EMBO J. , vol.21 , pp. 6095-6104
    • Otte, S.1    Barlowe, C.2
  • 54
    • 0035809210 scopus 로고    scopus 로고
    • Erv41p and Erv46p: New components of COPII vesicles involved in transport between the ER and Golgi complex
    • Otte, S., Belden, W.J., Heidtman, M., Liu, J., Jensen, O.N., and Barlowe, C. (2001) Erv41p and Erv46p: new components of COPII vesicles involved in transport between the ER and Golgi complex. J. Cell Biol. 152: 503-518.
    • (2001) J. Cell Biol. , vol.152 , pp. 503-518
    • Otte, S.1    Belden, W.J.2    Heidtman, M.3    Liu, J.4    Jensen, O.N.5    Barlowe, C.6
  • 55
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer, D.J., Helms, J.B., Beckers, C.J., Orci, L., and Rothman, J.E. (1993) Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J. Biol. Chem. 268: 12083-12089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.3    Orci, L.4    Rothman, J.E.5
  • 56
    • 70450224859 scopus 로고    scopus 로고
    • The yeast Golgi apparatus: Insights and mysteries
    • Papanikou, E., and Glick, B.S. (2009) The yeast Golgi apparatus: insights and mysteries. FEBS Lett. 583: 3746-3751
    • (2009) FEBS Lett. , vol.583 , pp. 3746-3751
    • Papanikou, E.1    Glick, B.S.2
  • 57
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: Involvement of specific residues of the Sec7 domain
    • Peyroche, A., Antonny, B., Robineau, S., Acker, J., Cherfils, J., and Jackson, C.L. (1999) Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol. Cell 3: 275-285.
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 59
    • 84924331272 scopus 로고    scopus 로고
    • Dual protein trafficking to secretory and non-secretory cell compartments: Clear or double vision?
    • Porter, B.W., Yuen, C.Y., and Christopher, D.A. (2015) Dual protein trafficking to secretory and non-secretory cell compartments: clear or double vision? Plant Sci. 234: 174-179.
    • (2015) Plant Sci. , vol.234 , pp. 174-179
    • Porter, B.W.1    Yuen, C.Y.2    Christopher, D.A.3
  • 60
    • 0036196829 scopus 로고    scopus 로고
    • Erv14p directs a transmembrane secretory protein into COPII-coated transport vesicles
    • Powers, J., and Barlowe, C. (2002) Erv14p directs a transmembrane secretory protein into COPII-coated transport vesicles. Mol. Biol. Cell 13: 880-891
    • (2002) Mol. Biol. Cell , vol.13 , pp. 880-891
    • Powers, J.1    Barlowe, C.2
  • 61
    • 0036007958 scopus 로고    scopus 로고
    • Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-Targeted green fluorescent protein and COPI antisera
    • Ritzenthaler, C., Nebenführ, A., Movafeghi, A., Stussi-Garaud, C., Behnia, L., Pimpl, P., et al. (2002) Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-Targeted green fluorescent protein and COPI antisera. Plant Cell 14: 237-261.
    • (2002) Plant Cell , vol.14 , pp. 237-261
    • Ritzenthaler, C.1    Nebenführ, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5    Pimpl, P.6
  • 62
    • 33845762779 scopus 로고    scopus 로고
    • Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
    • Saint-Jore-Dupas, C., Nebenführ, A., Boulaflous, A., Follet-Gueye, M.L., Plasson, C., Hawes, C., et al. (2006) Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway. Plant Cell 18: 3182-200.
    • (2006) Plant Cell , vol.18 , pp. 3182-3200
    • Saint-Jore-Dupas, C.1    Nebenführ, A.2    Boulaflous, A.3    Follet-Gueye, M.L.4    Plasson, C.5    Hawes, C.6
  • 63
    • 0030932017 scopus 로고    scopus 로고
    • Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins
    • Sato, K., Sato, M., and Nakano, A. (1997) Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins. Proc. Natl. Acad. Sci. USA 94: 9693-9698
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9693-9698
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 64
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmöller, F., Singer-Krüger, B., Schröder, S., Krüger, U., Barlowe, C., and Riezman, H. (1995) The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14: 1329-1339.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmöller, F.1    Singer-Krüger, B.2    Schröder, S.3    Krüger, U.4    Barlowe, C.5    Riezman, H.6
  • 65
    • 0030782188 scopus 로고    scopus 로고
    • Golgi tubule traffic and the effects of brefeldin A visualized in living cells
    • Sciaky, N., Presley, J., Smith, C., Zaal, K.J.M., Cole, N., Moreira, J.E., et al. (1997) Golgi tubule traffic and the effects of brefeldin A visualized in living cells. J. Cell Biol. 139: 1137-1155.
    • (1997) J. Cell Biol. , vol.139 , pp. 1137-1155
    • Sciaky, N.1    Presley, J.2    Smith, C.3    Zaal, K.J.M.4    Cole, N.5    Moreira, J.E.6
  • 66
    • 78650781753 scopus 로고    scopus 로고
    • Comparative genomic study of protein disulfide isomerases from photosynthetic organisms
    • Selles, B., Jacquot, J.P., and Rouhier N. (2011) Comparative genomic study of protein disulfide isomerases from photosynthetic organisms. Genomics 97: 37-50.
    • (2011) Genomics , vol.97 , pp. 37-50
    • Selles, B.1    Jacquot, J.P.2    Rouhier, N.3
  • 67
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J.C., Hardwick, K.G., Dean, N., and Pelham, H.R. (1990) ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61: 1349-1357
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 68
    • 84921730514 scopus 로고    scopus 로고
    • The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins
    • Shibuya, A., Margulis, N., Christiano, R., Walther, T.C., and Barlowe, C. (2015) The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins. J. Cell Biol. 208: 197-209.
    • (2015) J. Cell Biol. , vol.208 , pp. 197-209
    • Shibuya, A.1    Margulis, N.2    Christiano, R.3    Walther, T.C.4    Barlowe, C.5
  • 69
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E.L., Eddy, S.R., and Durbin, R. (1997) Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins 28: 405-420.
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 70
    • 0032476574 scopus 로고    scopus 로고
    • Reconstitution of retrograde transport from the Golgi to the ER in vitro
    • Spang, A., and Schekman, R. (1998) Reconstitution of retrograde transport from the Golgi to the ER in vitro. J. Cell Biol. 143: 589-599
    • (1998) J. Cell Biol. , vol.143 , pp. 589-599
    • Spang, A.1    Schekman, R.2
  • 71
    • 64849095076 scopus 로고    scopus 로고
    • Grab a Golgi: Laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum
    • Sparkes, I.A., Ketelaar, T., de Ruijter, N.C., and Hawes, C. (2009) Grab a Golgi: laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum. Traffic 10: 567-571.
    • (2009) Traffic , vol.10 , pp. 567-571
    • Sparkes, I.A.1    Ketelaar, T.2    De Ruijter, N.C.3    Hawes, C.4
  • 72
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R.G. (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12: 43R-56R.
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 73
    • 53749093685 scopus 로고    scopus 로고
    • Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography
    • Staehelin, L.A., and Kang B.H. (2008) Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography. Plant Physiol. 147: 1454-1468.
    • (2008) Plant Physiol. , vol.147 , pp. 1454-1468
    • Staehelin, L.A.1    Kang, B.H.2
  • 74
    • 33646832927 scopus 로고    scopus 로고
    • In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery
    • Stefano, G., Renna, L., Chatre, L., Hanton, S.L., Moreau, P., Hawes, C., et al. (2006) In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery. Plant J. 46: 95-110.
    • (2006) Plant J. , vol.46 , pp. 95-110
    • Stefano, G.1    Renna, L.2    Chatre, L.3    Hanton, S.L.4    Moreau, P.5    Hawes, C.6
  • 75
    • 0027136018 scopus 로고
    • Protein disulfide isomerase is both an enzyme and a chaperone
    • Wang, C.C., and Tsou, C.L. (1993) Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J. 7: 1515-1517
    • (1993) FASEB J. , vol.7 , pp. 1515-1517
    • Wang, C.C.1    Tsou, C.L.2
  • 76
    • 62549099551 scopus 로고    scopus 로고
    • Truncation of a protein disulfide isomerase, PDIL2-1, delays embryo sac maturation and disrupts pollen tube guidance in Arabidopsis thaliana
    • Wang, H., Boavida, L.C., Ron, M., and McCormick, S. (2008) Truncation of a protein disulfide isomerase, PDIL2-1, delays embryo sac maturation and disrupts pollen tube guidance in Arabidopsis thaliana. Plant Cell 20: 3300-3311.
    • (2008) Plant Cell , vol.20 , pp. 3300-3311
    • Wang, H.1    Boavida, L.C.2    Ron, M.3    McCormick, S.4
  • 77
    • 84902368384 scopus 로고    scopus 로고
    • Knockdown of the Arabidopsis thaliana chloroplast protein disulfide isomerase 6 results in reduced levels of photoinhibition and increased D1 synthesis in high light
    • Wittenberg, G., Levitan, A., Klein, T., Dangoor, I., Keren, N., and Danon, A. (2014) Knockdown of the Arabidopsis thaliana chloroplast protein disulfide isomerase 6 results in reduced levels of photoinhibition and increased D1 synthesis in high light. Plant J. 78: 1003-1013.
    • (2014) Plant J. , vol.78 , pp. 1003-1013
    • Wittenberg, G.1    Levitan, A.2    Klein, T.3    Dangoor, I.4    Keren, N.5    Danon, A.6
  • 78
    • 85017188767 scopus 로고    scopus 로고
    • Variation in the subcellular localization and protein folding activity among Arabidopsis thaliana homologs of protein disulfide isomerase
    • Yuen, C.Y., Matsumoto, K.O., and Christopher, D.A. (2013) Variation in the subcellular localization and protein folding activity among Arabidopsis thaliana homologs of protein disulfide isomerase. Biomolecules 3: 848-869.
    • (2013) Biomolecules , vol.3 , pp. 848-869
    • Yuen, C.Y.1    Matsumoto, K.O.2    Christopher, D.A.3
  • 79
    • 84955756336 scopus 로고    scopus 로고
    • Phylogenetic characterization and promoter expression analysis of a novel hybrid protein disulfide isomerase/cargo receptor subfamily unique to plants and chromalveolates
    • Yuen, C.Y., Wong, K., and Christopher, D.A. (2016) Phylogenetic characterization and promoter expression analysis of a novel hybrid protein disulfide isomerase/cargo receptor subfamily unique to plants and chromalveolates. Mol. Genet. Genomics 291: 455-469
    • (2016) Mol. Genet. Genomics , vol.291 , pp. 455-469
    • Yuen, C.Y.1    Wong, K.2    Christopher, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.