메뉴 건너뛰기




Volumn 41, Issue 1, 2005, Pages 81-94

Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum

Author keywords

Export signal; Membrane protein; Prolyl hydroxylase; Secretory pathway; Tobacco BY 2 cells

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CLONING; CYTOLOGY; DNA; IMMUNOLOGY; PLANTS (BOTANY); POLYPEPTIDES; TOBACCO;

EID: 12744261335     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2004.02279.x     Document Type: Article
Times cited : (118)

References (45)
  • 1
    • 0030807022 scopus 로고    scopus 로고
    • Cloning of the human prolyl 4-hydroxylase α subunit isoform α (II) and characterization of the type II enzyme tetramer
    • Annunen, P., Helaakoski, T., Myllyharju, J., Veijola, J., Pihlajaniemi, T. and Kivirikko, K.I. (1997) Cloning of the human prolyl 4-hydroxylase α subunit isoform α (II) and characterization of the type II enzyme tetramer. J. Biol. Cbem. 272, 17342-17348.
    • (1997) J. Biol. Cbem. , vol.272 , pp. 17342-17348
    • Annunen, P.1    Helaakoski, T.2    Myllyharju, J.3    Veijola, J.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 2
    • 0032513230 scopus 로고    scopus 로고
    • The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells
    • Annunen, P., Autio-Harmainen, H. and Kivirikko, K.I. (1998) The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells. J. Biol. Chem. 273, 5989-5992.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5989-5992
    • Annunen, P.1    Autio-Harmainen, H.2    Kivirikko, K.I.3
  • 3
    • 0035423555 scopus 로고    scopus 로고
    • ER export: Public transportation by the COPII coach
    • Antonnv, B. and Schekman, R. (2001) ER export: public transportation by the COPII coach. Curr. Opin. Cell Biol. 13, 438-443.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 438-443
    • Antonnv, B.1    Schekman, R.2
  • 4
    • 0029278821 scopus 로고
    • Development and application of an in vivo plant peroxisome import system
    • Banjoko, A. and Trelease, R.N. (1995) Development and application of an in vivo plant peroxisome import system. Plant Physiol. 107, 1201-1208.
    • (1995) Plant Physiol. , vol.107 , pp. 1201-1208
    • Banjoko, A.1    Trelease, R.N.2
  • 5
    • 0027437951 scopus 로고
    • Dynamic aspects of the plant extracellular matrix
    • Bolwell, G.P. (1993) Dynamic aspects of the plant extracellular matrix. Int. Rev. Cytol. 146, 261-324.
    • (1993) Int. Rev. Cytol. , vol.146 , pp. 261-324
    • Bolwell, G.P.1
  • 6
    • 0022102924 scopus 로고
    • Elicitor-induced prolyl hydroxylase from French bean (Phaseolus vulgaris)
    • Bolwell, G.P., Robbins, M.P. and Dixon, R.A. (1985) Elicitor-induced prolyl hydroxylase from French bean (Phaseolus vulgaris). Biochem. J. 229, 693-699.
    • (1985) Biochem. J. , vol.229 , pp. 693-699
    • Bolwell, G.P.1    Robbins, M.P.2    Dixon, R.A.3
  • 8
    • 0036957144 scopus 로고    scopus 로고
    • Molecular properties of a matrix attachment region-binding protein located in the nucleoli of tobacco cells
    • Fujiwara, S., Matsuda, N., Sato, T., Sonobe, S. and Maeshima, M. (2002) Molecular properties of a matrix attachment region-binding protein located in the nucleoli of tobacco cells. Plant Cell Physiol. 43, 1558-1567.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1558-1567
    • Fujiwara, S.1    Matsuda, N.2    Sato, T.3    Sonobe, S.4    Maeshima, M.5
  • 9
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1
    • Giraudo, C.G. and Maccioni, H.J. (2003) Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol. Biol. Cell. 14, 3753-3766.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3753-3766
    • Giraudo, C.G.1    Maccioni, H.J.2
  • 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
  • 13
    • 0037189554 scopus 로고    scopus 로고
    • Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana
    • Hieta, R. and Myllyharju, J. (2002) Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. J. Biol. Chem. 277, 23965-23971.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23965-23971
    • Hieta, R.1    Myllyharju, J.2
  • 14
    • 0031308635 scopus 로고    scopus 로고
    • Retention of glycosyltransferases in the Golgi apparatus
    • Jaskiewicz, E. (1997) Retention of glycosyltransferases in the Golgi apparatus. Acta Biochim. Pol. 44, 173-179.
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 173-179
    • Jaskiewicz, E.1
  • 15
    • 0023653673 scopus 로고
    • Characterization of a low-relative-molecular-mass prolyl 4-hydroxylase from the green alga Chlamydomonas reinhardii
    • Kaska, D.D., Gunzler, V., Kivirikko, K.I. and Myllyla, R. (1987) Characterization of a low-relative-molecular-mass prolyl 4-hydroxylase from the green alga Chlamydomonas reinhardii. Biochem. J. 241, 483-490.
    • (1987) Biochem. J. , vol.241 , pp. 483-490
    • Kaska, D.D.1    Gunzler, V.2    Kivirikko, K.I.3    Myllyla, R.4
  • 16
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes
    • Kivirikko, K.I. and Myllyla, R. (1982) Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 82, 245-304.
    • (1982) Methods Enzymol. , vol.82 , pp. 245-304
    • Kivirikko, K.I.1    Myllyla, R.2
  • 17
    • 0031893340 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
    • Kivirikko, K.I. and Myllyla, R. (1998) Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 16, 357-368.
    • (1998) Matrix Biol. , vol.16 , pp. 357-368
    • Kivirikko, K.I.1    Myllyla, R.2
  • 18
    • 7944227960 scopus 로고    scopus 로고
    • Dynamic behavior of microtubules and vacuoles at M/G1 interface observed in living tobacco BY-2 cells
    • (Nagata, T., Hasezawa, S. and Inze, D., eds). Heidelberg: Springer
    • Kumagai, F., Yoneda, A., Kutsuna, N. and Hasezawa, S. (2004) Dynamic behavior of microtubules and vacuoles at M/G1 interface observed in living tobacco BY-2 cells. In Tobacco BY-2 cells (Nagata, T., Hasezawa, S. and Inze, D., eds). Heidelberg: Springer, pp. 81-97.
    • (2004) Tobacco BY-2 Cells , pp. 81-97
    • Kumagai, F.1    Yoneda, A.2    Kutsuna, N.3    Hasezawa, S.4
  • 19
    • 0036343016 scopus 로고    scopus 로고
    • BP-80 and homologues are concentrated on post-Golgi, probable lytic prevacuolar compartments
    • Li, Y.B., Rogers, S.W., Tse, Y.C., Lo, S.W., Sun, S.S., Jauh, G.Y. and Jiang, L. (2002) BP-80 and homologues are concentrated on post-Golgi, probable lytic prevacuolar compartments. Plant Cell Physiol. 43, 726-742.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 726-742
    • Li, Y.B.1    Rogers, S.W.2    Tse, Y.C.3    Lo, S.W.4    Sun, S.S.5    Jauh, G.Y.6    Jiang, L.7
  • 20
    • 0024306480 scopus 로고
    • Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean
    • Maeshima, M. and Yoshida, S. (1989) Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean. J. Biol. Chem. 264, 20068-20073.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20068-20073
    • Maeshima, M.1    Yoshida, S.2
  • 22
    • 7944237619 scopus 로고    scopus 로고
    • A comprehensive gene expression analysis toward the understanding of growth and differentiation of tobacco BY-2 cells
    • Matsuoka, K., Demura, T., Galis, I., Horiguchi, T., Sasaki, M., Tashiro, G. and Fukuda, H. (2004) A comprehensive gene expression analysis toward the understanding of growth and differentiation of tobacco BY-2 cells. Plant Cell Physiol. 45, 1280-1289.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1280-1289
    • Matsuoka, K.1    Demura, T.2    Galis, I.3    Horiguchi, T.4    Sasaki, M.5    Tashiro, G.6    Fukuda, H.7
  • 23
    • 0026023554 scopus 로고
    • Properties of a precursor to a plant vacuolar protein required for vacuolar targeting
    • Matsuoka, K. and Nakamura, K. (1991) Properties of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc. Natl Acad. Sci. USA, 88, 834-838.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 834-838
    • Matsuoka, K.1    Nakamura, K.2
  • 24
    • 0033379217 scopus 로고    scopus 로고
    • Large alkyl side-chains of isoleucine and leucine in the NPIRL region constitute the core of the vacuolar sorting determinant of sporamin precursor
    • Matsuoka, K. and Nakamura, K. (1999) Large alkyl side-chains of isoleucine and leucine in the NPIRL region constitute the core of the vacuolar sorting determinant of sporamin precursor. Plant Mol. Biol. 41, 825-835.
    • (1999) Plant Mol. Biol. , vol.41 , pp. 825-835
    • Matsuoka, K.1    Nakamura, K.2
  • 25
    • 0029611736 scopus 로고
    • O-glycosylation of a precursor to a sweet potato vacuolar protein, sporamin, expressed in tobacco cells
    • Matsuoka, K., Watanabe, N. and Nakamura, K. (1995) O-glycosylation of a precursor to a sweet potato vacuolar protein, sporamin, expressed in tobacco cells. Plant J. 8, 877-889.
    • (1995) Plant J. , vol.8 , pp. 877-889
    • Matsuoka, K.1    Watanabe, N.2    Nakamura, K.3
  • 26
    • 0031021175 scopus 로고    scopus 로고
    • +-ATPase in a nonvacuolar organelle is required for the sorting of soluble vacuolar protein precursors in tobacco cells
    • +-ATPase in a nonvacuolar organelle is required for the sorting of soluble vacuolar protein precursors in tobacco cells. Plant Cell, 9, 533-546.
    • (1997) Plant Cell , vol.9 , pp. 533-546
    • Matsuoka, K.1    Higuchi, T.2    Maeshima, M.3    Nakamura, K.4
  • 27
    • 0037358282 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
    • Myllyharju, J. (2003) Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis. Matrix Biol. 22, 15-24.
    • (2003) Matrix Biol. , vol.22 , pp. 15-24
    • Myllyharju, J.1
  • 28
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron-and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase
    • Myllyharju, J. and Kivirikko, K.I. (1997) Characterization of the iron-and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase. EMBO J. 16, 1173-1180.
    • (1997) EMBO J. , vol.16 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 29
    • 0034754544 scopus 로고    scopus 로고
    • Low aquaporin content and low osmotic water permeability of the plasma and vacuolar membranes of a CAM plant Graptopetalum paraguayens: Comparison with radish
    • Ohshima, Y., Iwasaki, I., Suga, S., Murakami, M., Inoue, K. and Maeshima, M. (2001) Low aquaporin content and low osmotic water permeability of the plasma and vacuolar membranes of a CAM plant Graptopetalum paraguayens: Comparison with radish. Plant Cell Physiol. 42, 1119-1129.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1119-1129
    • Ohshima, Y.1    Iwasaki, I.2    Suga, S.3    Murakami, M.4    Inoue, K.5    Maeshima, M.6
  • 30
    • 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., Nebenfuhr, A., Movafeghi, A., Stussi-Garaud, C., Behnia, L., Pimpl, P., Staehelin, L.A. and Robinson, D.G. (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    Nebenfuhr, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5    Pimpl, P.6    Staehelin, L.A.7    Robinson, D.G.8
  • 32
    • 12744281440 scopus 로고    scopus 로고
    • A pumpkin 72 kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor
    • Shimada, T., Kuroyanagi, M., Nishimura, M. and Hara-Nishimura, I. (1997) A pumpkin 72 kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor. Plant Cell Physiol. 43, 726-742.
    • (1997) Plant Cell Physiol. , vol.43 , pp. 726-742
    • Shimada, T.1    Kuroyanagi, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 33
    • 0026688273 scopus 로고
    • Vacuolar chitinases of tobacco: A new class of hydroxyproline-containing proteins
    • Sticher, L., Hofsteenge, J., Milani, A., Neuhaus, J.M. and Meins, F., Jr (1992) Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins. Science, 257, 655-657.
    • (1992) Science , vol.257 , pp. 655-657
    • Sticher, L.1    Hofsteenge, J.2    Milani, A.3    Neuhaus, J.M.4    Meins Jr., F.5
  • 34
    • 0033838323 scopus 로고    scopus 로고
    • A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells
    • Takeuchi, M., Ueda, T., Sato, K., Abe, H., Nagata, T. and Nakano, A. (2000) A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J. 23, 517-525.
    • (2000) Plant J. , vol.23 , pp. 517-525
    • Takeuchi, M.1    Ueda, T.2    Sato, K.3    Abe, H.4    Nagata, T.5    Nakano, A.6
  • 35
    • 0019316690 scopus 로고
    • A new prolyl hydroxylase acting on poly-L-proline, from suspension cultured cells of Vinca rosea
    • Tanaka, M., Shibata, H. and Uchida, T. (1980) A new prolyl hydroxylase acting on poly-L-proline, from suspension cultured cells of Vinca rosea. Biochim. Biophys. Acta, 616, 188-198.
    • (1980) Biochim. Biophys. Acta , vol.616 , pp. 188-198
    • Tanaka, M.1    Shibata, H.2    Uchida, T.3
  • 36
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus
    • Teasdale, R.D. and Jackson, M.R. (1996) Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus. Annu. Rev. Cell Dev. Biol. 12, 27-54.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 37
    • 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, 453-464.
    • (2000) J. Cell Biol. , vol.148 , pp. 453-464
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 38
    • 1542370795 scopus 로고    scopus 로고
    • Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells
    • Tse, Y.C., Mo, B., Hillmer, S., Zhao, M., Lo, S.W., Robinson, D.G. and Jiang, L. (2004) Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells. Plant Cell, 16, 672-693.
    • (2004) Plant Cell , vol.16 , pp. 672-693
    • Tse, Y.C.1    Mo, B.2    Hillmer, S.3    Zhao, M.4    Lo, S.W.5    Robinson, D.G.6    Jiang, L.7
  • 39
    • 0028027778 scopus 로고
    • Cloning, baculovirus expression, and characterization of the α subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans
    • Veijola, J., Koivunen, P., Annunen, P., Pihlajaniemi, T. and Kivirikko, K.I. (1994) Cloning, baculovirus expression, and characterization of the α subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. J. Biol. Chem. 269, 26746-26753.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26746-26753
    • Veijola, J.1    Koivunen, P.2    Annunen, P.3    Pihlajaniemi, T.4    Kivirikko, K.I.5
  • 40
    • 0030005258 scopus 로고    scopus 로고
    • Co-expression of the α subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes
    • Veijola, J., Pihlajaniemi, T. and Kivirikko, K.I. (1996) Co-expression of the α subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Biochem. J. 315, 613-618.
    • (1996) Biochem. J. , vol.315 , pp. 613-618
    • Veijola, J.1    Pihlajaniemi, T.2    Kivirikko, K.I.3
  • 41
    • 0031906797 scopus 로고    scopus 로고
    • Cloning and expression of two genes encoding auxin-binding proteins from tobacco
    • Watanabe, S. and Shimomura, S. (1998) Cloning and expression of two genes encoding auxin-binding proteins from tobacco. Plant Mol. Biol. 36, 63-74.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 63-74
    • Watanabe, S.1    Shimomura, S.2
  • 42
    • 0026052386 scopus 로고
    • Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein
    • Wetterau, J.R., Combs, K.A., McLean, L.R., Spinner, S.N. and Aggerbeck, L.P. (1991) Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein. Biochemistry, 30, 9728-9735.
    • (1991) Biochemistry , vol.30 , pp. 9728-9735
    • Wetterau, J.R.1    Combs, K.A.2    McLean, L.R.3    Spinner, S.N.4    Aggerbeck, L.P.5
  • 43
    • 0037462716 scopus 로고    scopus 로고
    • A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase
    • Winter, A.D., Myllyharju, J. and Page, A.P. (2003) A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase. J. Biol. Chem., 278, 2554-2562.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2554-2562
    • Winter, A.D.1    Myllyharju, J.2    Page, A.P.3
  • 44
    • 0032990359 scopus 로고    scopus 로고
    • Ultrastructural localisation and further biochemical characterisation of prolyl 4-hydroxylase from Phaseolus vulgaris: Comparative analysis
    • Wojtaszek, P., Smith, C.G. and Bolwell, G.P. (1999) Ultrastructural localisation and further biochemical characterisation of prolyl 4-hydroxylase from Phaseolus vulgaris: comparative analysis. Int. J. Biochem. Cell Biol. 31, 463-477.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 463-477
    • Wojtaszek, P.1    Smith, C.G.2    Bolwell, G.P.3
  • 45
    • 0032289116 scopus 로고    scopus 로고
    • Phytochrome regulation and differential expression of gibberellin 3-hydroxylase genes in germinating Arabidopsis seeds
    • Yamaguchi, S., Smith, M.W., Brown, R.G., Kamiya, Y. and Sun, T. (1998) Phytochrome regulation and differential expression of gibberellin 3-hydroxylase genes in germinating Arabidopsis seeds. Plant Cell, 10, 2126-2155.
    • (1998) Plant Cell , vol.10 , pp. 2126-2155
    • Yamaguchi, S.1    Smith, M.W.2    Brown, R.G.3    Kamiya, Y.4    Sun, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.