메뉴 건너뛰기




Volumn 20, Issue 9, 2008, Pages 2529-2540

NAI2 is an endoplasmic reticulum body component that enables ER body formation in Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; BRASSICACEAE; BRASSICALES;

EID: 57749091765     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.108.059345     Document Type: Article
Times cited : (57)

References (42)
  • 1
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J.M., et al. (2003). Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science 301: 653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1
  • 2
    • 0029105386 scopus 로고
    • Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco
    • Bagga, S., Adams, H., Kemp, J.D., and Sengupta-Gopalan, C. (1995). Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco. Plant Physiol. 107: 13-23.
    • (1995) Plant Physiol , vol.107 , pp. 13-23
    • Bagga, S.1    Adams, H.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 3
    • 33750063596 scopus 로고
    • Dilated cisternae in Capparales: An attempt towards the characterization of a specific endoplasmic reticulum
    • Behnke, H.-D., and Eschlbeck, G. (1978). Dilated cisternae in Capparales: An attempt towards the characterization of a specific endoplasmic reticulum. Protoplasma 97: 351-363.
    • (1978) Protoplasma , vol.97 , pp. 351-363
    • Behnke, H.-D.1    Eschlbeck, G.2
  • 4
    • 0033840913 scopus 로고    scopus 로고
    • Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles
    • Chrispeels, M.J., and Herman, E.M. (2000). Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles. Plant Physiol. 123: 1227-1233.
    • (2000) Plant Physiol , vol.123 , pp. 1227-1233
    • Chrispeels, M.J.1    Herman, E.M.2
  • 5
    • 0035807828 scopus 로고    scopus 로고
    • Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells
    • Di Cola, A., Frigerio, L., Lord, J.M., Ceriotti, A., and Roberts, L.M. (2001). Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells. Proc. Natl. Acad. Sci. USA 98: 14726-14731.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14726-14731
    • Di Cola, A.1    Frigerio, L.2    Lord, J.M.3    Ceriotti, A.4    Roberts, L.M.5
  • 6
    • 33646236590 scopus 로고    scopus 로고
    • Mapping the Arabidopsis organelle proteome
    • Dunkley, T.P., et al. (2006). Mapping the Arabidopsis organelle proteome. Proc. Natl. Acad. Sci. USA 103: 6518-6523.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6518-6523
    • Dunkley, T.P.1
  • 7
    • 16544368038 scopus 로고    scopus 로고
    • ER-derived compartments are formed by highly regulated processes and have special functions in plants
    • Galili, G. (2004). ER-derived compartments are formed by highly regulated processes and have special functions in plants. Plant Physiol. 136: 3411-3413.
    • (2004) Plant Physiol , vol.136 , pp. 3411-3413
    • Galili, G.1
  • 8
    • 0344100119 scopus 로고    scopus 로고
    • A wound-inducible organelle derived from endoplasmic reticulum: A plant strategy against environmental stress?
    • Hara-Nishimura, I., and Matsushima, R. (2003). A wound-inducible organelle derived from endoplasmic reticulum: A plant strategy against environmental stress? Curr. Opin. Plant Biol. 6: 583-588.
    • (2003) Curr. Opin. Plant Biol , vol.6 , pp. 583-588
    • Hara-Nishimura, I.1    Matsushima, R.2
  • 9
    • 16544378458 scopus 로고    scopus 로고
    • Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells?
    • Hara-Nishimura, I., Matsushima, R., Shimada, T., and Nishimura, M. (2004). Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells? Plant Physiol. 136: 3435-3439.
    • (2004) Plant Physiol , vol.136 , pp. 3435-3439
    • Hara-Nishimura, I.1    Matsushima, R.2    Shimada, T.3    Nishimura, M.4
  • 10
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein-storage vacuoles is mediated by large precursor-accumulating vesicles
    • Hara-Nishimura, I., Shimada, T., Hatano, K., Takeuchi, Y., and Nishimura, M. (1998). Transport of storage proteins to protein-storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 10: 825-836.
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchi, Y.4    Nishimura, M.5
  • 11
    • 0033103645 scopus 로고    scopus 로고
    • Accumulation of a fusion protein containing 2S albumin induces novel vesicles in vegetative cells of Arabidopsis
    • Hayashi, M., Toriyama, K., Kondo, M., Hara-Nishimura, I., and Nishimura, M. (1999). Accumulation of a fusion protein containing 2S albumin induces novel vesicles in vegetative cells of Arabidopsis. Plant Cell Physiol. 40: 263-272.
    • (1999) Plant Cell Physiol , vol.40 , pp. 263-272
    • Hayashi, M.1    Toriyama, K.2    Kondo, M.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 13
    • 0032718660 scopus 로고    scopus 로고
    • Protein storage bodies and vacuoles
    • Herman, E.M., and Larkins, B.A. (1999). Protein storage bodies and vacuoles. Plant Cell 11: 601-613.
    • (1999) Plant Cell , vol.11 , pp. 601-613
    • Herman, E.M.1    Larkins, B.A.2
  • 14
    • 16544372267 scopus 로고    scopus 로고
    • Endoplasmic reticulum to vacuole trafficking of endoplasmic reticulum bodies an alternate pathway for protein transfer to the vacuole
    • Herman, E.M., and Schmid, M. (2004). Endoplasmic reticulum to vacuole trafficking of endoplasmic reticulum bodies an alternate pathway for protein transfer to the vacuole. Plant Physiol. 136: 3440-3446.
    • (2004) Plant Physiol , vol.136 , pp. 3440-3446
    • Herman, E.M.1    Schmid, M.2
  • 15
    • 4043153341 scopus 로고    scopus 로고
    • Versatile gene-specific sequence tags for Arabidopsis functional genomics: Transcript profiling and reverse genetics applications
    • Hilson, P., et al. (2004). Versatile gene-specific sequence tags for Arabidopsis functional genomics: Transcript profiling and reverse genetics applications. Genome Res. 14: 2176-2189.
    • (2004) Genome Res , vol.14 , pp. 2176-2189
    • Hilson, P.1
  • 16
    • 35348866853 scopus 로고    scopus 로고
    • The maize Floury1 gene encodes a novel endoplasmic reticulum protein involved in zein protein body formation
    • Holding, D.R., Otegui, M.S., Li, B., Meeley, R.B., Dam, T., Hunter, B. G., Jung, R., and Larkins, B.A. (2007). The maize Floury1 gene encodes a novel endoplasmic reticulum protein involved in zein protein body formation. Plant Cell 19: 2569-2582.
    • (2007) Plant Cell , vol.19 , pp. 2569-2582
    • Holding, D.R.1    Otegui, M.S.2    Li, B.3    Meeley, R.B.4    Dam, T.5    Hunter, B.G.6    Jung, R.7    Larkins, B.A.8
  • 17
    • 0000106608 scopus 로고
    • Cytochemical localization of myrosinase (β-thioglucosidase) in root tips of Sinapis alba
    • Iversen, T.-H. (1970a). Cytochemical localization of myrosinase (β-thioglucosidase) in root tips of Sinapis alba. Protoplasma 71: 451-466.
    • (1970) Protoplasma , vol.71 , pp. 451-466
    • Iversen, T.-H.1
  • 18
    • 0000838661 scopus 로고
    • The morphology, occurrence, and distribution of dilated cisternae of the endoplasmic reticulum in tissues of plants of the Cruciferae
    • Iversen, T.-H. (1970b). The morphology, occurrence, and distribution of dilated cisternae of the endoplasmic reticulum in tissues of plants of the Cruciferae. Protoplasma 71: 467-477.
    • (1970) Protoplasma , vol.71 , pp. 467-477
    • Iversen, T.-H.1
  • 19
    • 0030575903 scopus 로고    scopus 로고
    • CKI1, a histidine kinase homolog implicated in cytokinin signal transduction
    • Kakimoto, T. (1996). CKI1, a histidine kinase homolog implicated in cytokinin signal transduction. Science 274: 982-985.
    • (1996) Science , vol.274 , pp. 982-985
    • Kakimoto, T.1
  • 21
    • 2942677348 scopus 로고    scopus 로고
    • NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body
    • Matsushima, R., Fukao, Y., Nishimura, M., and Hara-Nishimura, I. (2004). NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body. Plant Cell 16: 1536-1549.
    • (2004) Plant Cell , vol.16 , pp. 1536-1549
    • Matsushima, R.1    Fukao, Y.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 22
    • 0346037065 scopus 로고    scopus 로고
    • An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis
    • Matsushima, R., Hayashi, Y., Shimada, T., Nishimura, M., and Hara-Nishimura, I. (2002). An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis. Plant Physiol. 130: 1807-1814.
    • (2002) Plant Physiol , vol.130 , pp. 1807-1814
    • Matsushima, R.1    Hayashi, Y.2    Shimada, T.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 24
    • 0242515793 scopus 로고    scopus 로고
    • A novel ER-derived compartment, the ER body, selectively accumulates β-glucosidase with an ER-retention signal in Arabidopsis
    • Matsushima, R., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (2003b). A novel ER-derived compartment, the ER body, selectively accumulates β-glucosidase with an ER-retention signal in Arabidopsis. Plant J. 33: 493-502.
    • (2003) Plant J , vol.33 , pp. 493-502
    • Matsushima, R.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 25
    • 0033780821 scopus 로고    scopus 로고
    • Characterization of organelles in the vacuolar-sorting pathway by visualization with GFP in tobacco BY-2 cells
    • Mitsuhashi, N., Shimada, T., Mano, S., Nishimura, M., and Hara-Nishimura, I. (2000). Characterization of organelles in the vacuolar-sorting pathway by visualization with GFP in tobacco BY-2 cells. Plant Cell Physiol. 41: 993-1001.
    • (2000) Plant Cell Physiol , vol.41 , pp. 993-1001
    • Mitsuhashi, N.1    Shimada, T.2    Mano, S.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 26
    • 48849112921 scopus 로고    scopus 로고
    • Antagonistic jacalin-related lectins regulate the size of ER body-type β-glucosidase complexes in Arabidopsis thaliana
    • Nagano, A.J., Fukao, Y., Fujiwara, M., Nishimura, M., and Hara-Nishimura, I. (2008). Antagonistic jacalin-related lectins regulate the size of ER body-type β-glucosidase complexes in Arabidopsis thaliana. Plant Cell Physiol. 49: 969-980.
    • (2008) Plant Cell Physiol , vol.49 , pp. 969-980
    • Nagano, A.J.1    Fukao, Y.2    Fujiwara, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 27
    • 25444452649 scopus 로고    scopus 로고
    • Activation of an ER-body-localized β-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana
    • Nagano, A.J., Matsushima, R., and Hara-Nishimura, I. (2005). Activation of an ER-body-localized β-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana. Plant Cell Physiol. 46: 1140-1148.
    • (2005) Plant Cell Physiol , vol.46 , pp. 1140-1148
    • Nagano, A.J.1    Matsushima, R.2    Hara-Nishimura, I.3
  • 28
    • 34547677722 scopus 로고    scopus 로고
    • Development of series of Gateway binary vectors, pGWBs for realizing efficient construction of fusion genes for plant transformation
    • Nakagawa, T., Kurose, T., Hino, T., Tanaka, K., Kawamukai, M., Niwa, Y., Toyooka, K., Matsuoka, K., Jinbo, T., and Kimura, T. (2007). Development of series of Gateway binary vectors, pGWBs for realizing efficient construction of fusion genes for plant transformation. J. Biosci. Bioeng. 2007: 34-41.
    • (2007) J. Biosci. Bioeng , vol.2007 , pp. 34-41
    • Nakagawa, T.1    Kurose, T.2    Hino, T.3    Tanaka, K.4    Kawamukai, M.5    Niwa, Y.6    Toyooka, K.7    Matsuoka, K.8    Jinbo, T.9    Kimura, T.10
  • 30
    • 0041464460 scopus 로고    scopus 로고
    • C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydrylendopeptidase
    • Okamoto, T., Shimada, T., Hara-Nishimura, I., Nishimura, M., and Minamikawa, T. (2003). C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydrylendopeptidase. Plant Physiol. 132: 1892-1900.
    • (2003) Plant Physiol , vol.132 , pp. 1892-1900
    • Okamoto, T.1    Shimada, T.2    Hara-Nishimura, I.3    Nishimura, M.4    Minamikawa, T.5
  • 31
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway
    • Pimpl, P., Taylor, J.P., Snowden, C., Hillmer, S., Robinson, D.G., and Denecke, J. (2006). Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway. Plant Cell 18: 198-211.
    • (2006) Plant Cell , vol.18 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 32
    • 0033598774 scopus 로고    scopus 로고
    • Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes
    • Schmid, M., Simpson, D., and Gietl, C. (1999). Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes. Proc. Natl. Acad. Sci. USA 96: 14159-14164.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14159-14164
    • Schmid, M.1    Simpson, D.2    Gietl, C.3
  • 34
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N.C., Campbell, R.E., Steinbach, P.A., Giepmans, B.N., Palmer, A.E., and Tsien, R.Y. (2004). Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22: 1567-1572.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 35
    • 42549165922 scopus 로고    scopus 로고
    • PYK10, a b-glucosidase located in the endoplasmic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and endophytic fungus Piriformospora indica
    • Sherameti, I., Venus, Y., Drzewiecki, C., Tripathi, S., Dan, V.M., Nitz, I., Varma, A., Grundler, F.M., and Oelmüller, R. (2008). PYK10, a b-glucosidase located in the endoplasmic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and endophytic fungus Piriformospora indica. Plant J. 54: 428-439.
    • (2008) Plant J , vol.54 , pp. 428-439
    • Sherameti, I.1    Venus, Y.2    Drzewiecki, C.3    Tripathi, S.4    Dan, V.M.5    Nitz, I.6    Varma, A.7    Grundler, F.M.8    Oelmüller, R.9
  • 36
    • 26444461164 scopus 로고    scopus 로고
    • An Arabidopsis protein with a novel calcium-binding repeat sequence interacts with TONSOKU/MGOUN3/BRUSHY1 involved in meristem maintenance
    • Suzuki, T., Nakajima, S., Morikami, A., and Nakamura, K. (2005). An Arabidopsis protein with a novel calcium-binding repeat sequence interacts with TONSOKU/MGOUN3/BRUSHY1 involved in meristem maintenance. Plant Cell Physiol. 46: 1452-1461.
    • (2005) Plant Cell Physiol , vol.46 , pp. 1452-1461
    • Suzuki, T.1    Nakajima, S.2    Morikami, A.3    Nakamura, K.4
  • 37
    • 3843103539 scopus 로고    scopus 로고
    • Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation
    • Tamura, K., Yamada, K., Shimada, T., and Hara-Nishimura, I. (2004). Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation. Plant J. 39: 393-402.
    • (2004) Plant J , vol.39 , pp. 393-402
    • Tamura, K.1    Yamada, K.2    Shimada, T.3    Hara-Nishimura, I.4
  • 38
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds
    • Toyooka, K., Okamoto, T., and Minamikawa, T. (2000). Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds. J. Cell Biol. 148: 453-463.
    • (2000) J. Cell Biol , vol.148 , pp. 453-463
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 39
    • 16544394131 scopus 로고    scopus 로고
    • Protein quality control mechanisms and protein storage in the endoplasmic reticulum. A conflict of interests?
    • Vitale, A., and Ceriotti, A. (2004). Protein quality control mechanisms and protein storage in the endoplasmic reticulum. A conflict of interests? Plant Physiol. 136: 3420-3426.
    • (2004) Plant Physiol , vol.136 , pp. 3420-3426
    • Vitale, A.1    Ceriotti, A.2
  • 40
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986). A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14: 4683-4690.
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • von Heijne, G.1
  • 41
    • 33846455426 scopus 로고    scopus 로고
    • Protein disulfide isomerase family proteins involved in soybean protein biogenesis
    • Wadahama, H., Kamauchi, S., Ishimoto, M., Kawada, T., and Urade, R. (2007). Protein disulfide isomerase family proteins involved in soybean protein biogenesis. FEBS J. 274: 687-703.
    • (2007) FEBS J , vol.274 , pp. 687-703
    • Wadahama, H.1    Kamauchi, S.2    Ishimoto, M.3    Kawada, T.4    Urade, R.5
  • 42
    • 38049153332 scopus 로고    scopus 로고
    • Cytosolic HSP90 regulates the heat shock response that is responsible for heat acclimation in Arabidopsis thaliana
    • Yamada, K., Fukao, Y., Hayashi, M., Fukazawa, M., Suzuki, I., and Nishimura, M. (2007). Cytosolic HSP90 regulates the heat shock response that is responsible for heat acclimation in Arabidopsis thaliana. J. Biol. Chem. 282: 37794-37804.
    • (2007) J. Biol. Chem , vol.282 , pp. 37794-37804
    • Yamada, K.1    Fukao, Y.2    Hayashi, M.3    Fukazawa, M.4    Suzuki, I.5    Nishimura, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.