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Volumn 7, Issue 4, 2003, Pages 388-400

Peroxisome biogenesis and the role of protein import

Author keywords

Peroxin; Peroxisome biogenesis; Proliferation; Protein import

Indexed keywords

MEMBRANE PROTEIN; PROTEIN;

EID: 1842853027     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2003.tb00241.x     Document Type: Review
Times cited : (56)

References (96)
  • 1
    • 0021272337 scopus 로고
    • Peroxisomes in sebaceous glands V. Complex peroxisomes in the mouse preputial gland: Serial sectioning and 3-dimensional reconstruction studies
    • Gorgas K., Peroxisomes in sebaceous glands V. Complex peroxisomes in the mouse preputial gland: Serial sectioning and 3-dimensional reconstruction studies, Anat. Embryol., 169: 261-270, 1984
    • (1984) Anat. Embryol. , vol.169 , pp. 261-270
    • Gorgas, K.1
  • 2
    • 0033739889 scopus 로고    scopus 로고
    • Real time imaging reveals a peroxisomal reticulum in living cells
    • Schrader M., King S.J., Stroh T.A., Schroer T.A., Real time imaging reveals a peroxisomal reticulum in living cells, J. Cell Sci., 113: 3663-3671, 2000
    • (2000) J. Cell Sci. , vol.113 , pp. 3663-3671
    • Schrader, M.1    King, S.J.2    Stroh, T.A.3    Schroer, T.A.4
  • 3
    • 0033762717 scopus 로고    scopus 로고
    • Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes
    • Zolman B.K., Yoder A., Bartel B., Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes, Genetics, 156: 1323-1337, 2000
    • (2000) Genetics , vol.156 , pp. 1323-1337
    • Zolman, B.K.1    Yoder, A.2    Bartel, B.3
  • 4
    • 0034641758 scopus 로고    scopus 로고
    • The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis
    • Stintzi A., Browse J., The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis, Proc. Natl. Acad. Sci. U. S. A., 97: 10625-10630, 2000
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10625-10630
    • Stintzi, A.1    Browse, J.2
  • 5
    • 0035212728 scopus 로고    scopus 로고
    • Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells
    • Corpas F.J., Barroso J.B., del Rio L.A., Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells, Trends Plant Sci., 6: 145-150, 2001
    • (2001) Trends Plant Sci. , vol.6 , pp. 145-150
    • Corpas, F.J.1    Barroso, J.B.2    Del Rio, L.A.3
  • 6
    • 0034717058 scopus 로고    scopus 로고
    • Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids
    • Baes M., Huyghe S., Carmeliet P., Declercq P.E., Collen D., Mannaerts G.P., Van Veldhoven P.P., Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids, J. Biol. Chem., 275: 16329-16336, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 16329-16336
    • Baes, M.1    Huyghe, S.2    Carmeliet, P.3    Declercq, P.E.4    Collen, D.5    Mannaerts, G.P.6    Van Veldhoven, P.P.7
  • 9
    • 0036158980 scopus 로고    scopus 로고
    • Absence of functional peroxisomes does not lead to deficiency of enzymes involved in cholesterol biosynthesis
    • Hogenboom S., Romeijn G.J., Houten S.M., Baes M., Wanders R.J.A., Waterham H.R., Absence of functional peroxisomes does not lead to deficiency of enzymes involved in cholesterol biosynthesis, J. Lipid Res., 43: 90-98, 2002
    • (2002) J. Lipid Res. , vol.43 , pp. 90-98
    • Hogenboom, S.1    Romeijn, G.J.2    Houten, S.M.3    Baes, M.4    Wanders, R.J.A.5    Waterham, H.R.6
  • 11
    • 0032509362 scopus 로고    scopus 로고
    • The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it
    • Lametschwandtner G., Brocard C., Fransen M., Van Veldhoven P., Berger J., Hartig A., The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it, J. Biol. Chem., 273: 33635-33643, 1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 33635-33643
    • Lametschwandtner, G.1    Brocard, C.2    Fransen, M.3    Van Veldhoven, P.4    Berger, J.5    Hartig, A.6
  • 12
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto G.J., Geisbrecht B.V., Gould S.J., Berg J.M., Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5, Nat. Struct. Biol., 7: 1091-1095, 2000
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1091-1095
    • Gatto, G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 13
    • 0035805574 scopus 로고    scopus 로고
    • Recognition of peroxisomal targeting signal type 1 by the import receptor Pex5p
    • Klein A.T.J., Barnett P., Bottger G., Konings D., Tabak H.F., Distel B., Recognition of peroxisomal targeting signal type 1 by the import receptor Pex5p, J. Biol. Chem., 276: 15034-15041, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 15034-15041
    • Klein, A.T.J.1    Barnett, P.2    Bottger, G.3    Konings, D.4    Tabak, H.F.5    Distel, B.6
  • 14
    • 0036179374 scopus 로고    scopus 로고
    • Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: Conserved Pex5p WXXYF/Y motifs are critical for matrix protein import
    • Otera H., Setoguchi K., Hamasaki M., Kumashiro T., Shimizu N., Fujiki Y., Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: Conserved Pex5p WXXYF/Y motifs are critical for matrix protein import, Mol. Cell. Biol., 22: 1639-1655, 2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1639-1655
    • Otera, H.1    Setoguchi, K.2    Hamasaki, M.3    Kumashiro, T.4    Shimizu, N.5    Fujiki, Y.6
  • 15
    • 0035860787 scopus 로고    scopus 로고
    • The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14
    • Saidowsky J., Dodt G., Kirchberg K., Wegner A., Nastainczyk W., Kunau W.H., Schliebs W., The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14, J. Biol. Chem., 276: 34524-34529, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 34524-34529
    • Saidowsky, J.1    Dodt, G.2    Kirchberg, K.3    Wegner, A.4    Nastainczyk, W.5    Kunau, W.H.6    Schliebs, W.7
  • 16
    • 0037067768 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non- PTS1, import pathway into peroxisomes that is dependent on Pex5p
    • Klein A.T.J., van den Berg M., Bottger G., Tabak H.F., Distel B., Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non- PTS1, import pathway into peroxisomes that is dependent on Pex5p, J. Biol. Chem., 277: 25011-25019, 2002
    • (2002) J. Biol. Chem. , vol.277 , pp. 25011-25019
    • Klein, A.T.J.1    Van Den Berg, M.2    Bottger, G.3    Tabak, H.F.4    Distel, B.5
  • 17
    • 0035018777 scopus 로고    scopus 로고
    • PTS2 protein import into mammalian peroxisomes
    • Legakis J.E., Terlecky S.R., PTS2 protein import into mammalian peroxisomes, Traffic, 2: 252-260, 2001
    • (2001) Traffic , vol.2 , pp. 252-260
    • Legakis, J.E.1    Terlecky, S.R.2
  • 18
    • 0036646057 scopus 로고    scopus 로고
    • Functional studies on human Pex7p: Subcellular localization and interaction with proteins containing a peroxisome-targeting signal type 2 and other peroxins
    • Ghys K., Fransen M., Mannaerts G.P., Van Velhoven P.P., Functional studies on human Pex7p: subcellular localization and interaction with proteins containing a peroxisome-targeting signal type 2 and other peroxins, Biochem. J., 365: 41-50, 2002
    • (2002) Biochem. J. , vol.365 , pp. 41-50
    • Ghys, K.1    Fransen, M.2    Mannaerts, G.P.3    Van Velhoven, P.P.4
  • 19
    • 0028053931 scopus 로고
    • PAS7 encodes a novel yeast member of the WD-40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into peroxisomes
    • Marzioch M., Erdmann R., Veenhuis M., Kunau W.H., PAS7 encodes a novel yeast member of the WD-40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into peroxisomes, EMBO J., 13: 4908-4918, 1994
    • (1994) EMBO J. , vol.13 , pp. 4908-4918
    • Marzioch, M.1    Erdmann, R.2    Veenhuis, M.3    Kunau, W.H.4
  • 20
    • 0036013390 scopus 로고    scopus 로고
    • Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana
    • Nito K., Hayashi M., Nishimura M., Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana, Plant Cell Physiol., 43: 355-366, 2002
    • (2002) Plant Cell Physiol. , vol.43 , pp. 355-366
    • Nito, K.1    Hayashi, M.2    Nishimura, M.3
  • 21
    • 1842335689 scopus 로고    scopus 로고
    • Rhizomelic chondrodysplasia punctata is caused by deficiency of human PEX7, a homologue of the yeast PTS2 receptor
    • Purdue P.E., Zhang J.W., Skoneczny M., Lazarow P.B., Rhizomelic chondrodysplasia punctata is caused by deficiency of human PEX7, a homologue of the yeast PTS2 receptor, Nature Genet., 15: 381-384, 1997
    • (1997) Nature Genet. , vol.15 , pp. 381-384
    • Purdue, P.E.1    Zhang, J.W.2    Skoneczny, M.3    Lazarow, P.B.4
  • 23
    • 0034231261 scopus 로고    scopus 로고
    • Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes
    • Motley A.M., Hettema E.H., Ketting R., Plasterk R., Tabak H.F., Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes, EMBO Rep., 1: 40-46, 2000
    • (2000) EMBO Rep. , vol.1 , pp. 40-46
    • Motley, A.M.1    Hettema, E.H.2    Ketting, R.3    Plasterk, R.4    Tabak, H.F.5
  • 24
    • 0036337231 scopus 로고    scopus 로고
    • Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: Implications for the first steps in PTS2 protein import
    • Stein K., Schell-Steven A., Erdmann R., Rottensteiner H., Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: Implications for the first steps in PTS2 protein import, Mol. Cell. Biol., 11: 6056-6069, 2002
    • (2002) Mol. Cell. Biol. , vol.11 , pp. 6056-6069
    • Stein, K.1    Schell-Steven, A.2    Erdmann, R.3    Rottensteiner, H.4
  • 25
    • 0035861688 scopus 로고    scopus 로고
    • Pex18p is constitutively degraded during peroxisome biogenesis
    • Purdue P.E., Lazarow P.B., Pex18p is constitutively degraded during peroxisome biogenesis, J. Biol. Chem., 276: 47684-47689, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 47684-47689
    • Purdue, P.E.1    Lazarow, P.B.2
  • 26
    • 0034647937 scopus 로고    scopus 로고
    • The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates the Pex7p-PTS2 protein complex into peroxisomes via its initial docking site, Pex14p
    • Otera H., Harano T., Honsho M., Ghaedi K., Mukai S., Tanaka A., Kawai A., Shimizu N., Fujiki Y., The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates the Pex7p-PTS2 protein complex into peroxisomes via its initial docking site, Pex14p, J. Biol. Chem., 275: 21703-21714, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 21703-21714
    • Otera, H.1    Harano, T.2    Honsho, M.3    Ghaedi, K.4    Mukai, S.5    Tanaka, A.6    Kawai, A.7    Shimizu, N.8    Fujiki, Y.9
  • 27
    • 0034647529 scopus 로고    scopus 로고
    • Disruption of the interaction of the longer isoform of Pex5p, Pex5pL, with Pex7p abolishes peroxisome targeting signal type 2 - Study with a novel PEX5-impaired Chinese hamster ovary cell mutant
    • Matsumura T., Ofera H., Fujiki Y., Disruption of the interaction of the longer isoform of Pex5p, Pex5pL, with Pex7p abolishes peroxisome targeting signal type 2 - Study with a novel PEX5-impaired Chinese hamster ovary cell mutant, J. Biol. Chem., 275: 21715-21721, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 21715-21721
    • Matsumura, T.1    Ofera, H.2    Fujiki, Y.3
  • 28
    • 0035203058 scopus 로고    scopus 로고
    • Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and mammalian Pex5pL fulfil a common function in the early steps of the peroxisomal PTS2 import pathway
    • Einwachter H., Sowinski S., Kunau W.H., Schliebs W., Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and mammalian Pex5pL fulfil a common function in the early steps of the peroxisomal PTS2 import pathway, EMBO Rep., 2: 1035-1039, 2001
    • (2001) EMBO Rep. , vol.2 , pp. 1035-1039
    • Einwachter, H.1    Sowinski, S.2    Kunau, W.H.3    Schliebs, W.4
  • 29
    • 0037326247 scopus 로고    scopus 로고
    • Pex7p and Pex20p of Neurospora crassa function together in PTS2-dependent protein import into peroxisomes
    • Sichting M., Schell-Steven A., Prokisch H., Erdmann R., Rottensteiner H., Pex7p and Pex20p of Neurospora crassa function together in PTS2-dependent protein import into peroxisomes, Mol. Biol. Cell, 14: 810-821, 2003
    • (2003) Mol. Biol. Cell , vol.14 , pp. 810-821
    • Sichting, M.1    Schell-Steven, A.2    Prokisch, H.3    Erdmann, R.4    Rottensteiner, H.5
  • 31
    • 0031953256 scopus 로고    scopus 로고
    • Pex17p of Saccharomyces cerevisiae is a novel peroxin and component of the peroxisomal protein translocation machinery
    • Huhse B., Rehling P., Albertini M., Blank L., Meller K., Kunau W.H., Pex17p of Saccharomyces cerevisiae is a novel peroxin and component of the peroxisomal protein translocation machinery, J. Cell Biol., 140: 49-60, 1998
    • (1998) J. Cell Biol. , vol.140 , pp. 49-60
    • Huhse, B.1    Rehling, P.2    Albertini, M.3    Blank, L.4    Meller, K.5    Kunau, W.H.6
  • 32
    • 0037053374 scopus 로고    scopus 로고
    • Peroxisomal membrane protein import does not require Pex17p
    • Harper C.C., South S.T., McCaffery J.M., Gould S.J., Peroxisomal membrane protein import does not require Pex17p, J. Biol. Chem., 277: 16498-16504, 2002
    • (2002) J. Biol. Chem. , vol.277 , pp. 16498-16504
    • Harper, C.C.1    South, S.T.2    McCaffery, J.M.3    Gould, S.J.4
  • 34
    • 0030890954 scopus 로고    scopus 로고
    • Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways
    • Albertini M., Rehling P., Erdmann R., Girzalsky W., Kiel J., Veenhuis M., Kunau W.H., Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways, Cell, 89: 83-92, 1997
    • (1997) Cell , vol.89 , pp. 83-92
    • Albertini, M.1    Rehling, P.2    Erdmann, R.3    Girzalsky, W.4    Kiel, J.5    Veenhuis, M.6    Kunau, W.H.7
  • 35
    • 0033800536 scopus 로고    scopus 로고
    • The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import
    • Collins C.S., Kalish J.E., Morrell J.C., McCaffery J.M., Gould S.J., The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import, Mol. Cell, Biol., 20: 7516-7526, 2000
    • (2000) Mol. Cell, Biol. , vol.20 , pp. 7516-7526
    • Collins, C.S.1    Kalish, J.E.2    Morrell, J.C.3    McCaffery, J.M.4    Gould, S.J.5
  • 36
    • 0034682844 scopus 로고    scopus 로고
    • Molecular anatomy of the peroxin Pex12p - Ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p
    • Okumoto K., Abe I., Fujiki V., Molecular anatomy of the peroxin Pex12p - Ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p, J. Biol. Chem., 275: 25700-25710, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 25700-25710
    • Okumoto, K.1    Abe, I.2    Fujiki, V.3
  • 37
    • 0035037510 scopus 로고    scopus 로고
    • Pex12p of Saccharomyces cerevisiae is a component of a multi- Protein complex essential for peroxisomal matrix protein import
    • Albertini M., Girzalsky W., Veenhuis M., Kunau W.H., Pex12p of Saccharomyces cerevisiae is a component of a multi- protein complex essential for peroxisomal matrix protein import, Eur. J. Cell Biol., 80: 257-270, 2001
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 257-270
    • Albertini, M.1    Girzalsky, W.2    Veenhuis, M.3    Kunau, W.H.4
  • 38
    • 0033571690 scopus 로고    scopus 로고
    • PEX12 interacts with PEX5 and PEX10 and acts down-stream of receptor docking in peroxisomal matrix protein import
    • Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J., PEX12 interacts with PEX5 and PEX10 and acts down-stream of receptor docking in peroxisomal matrix protein import, J. Cell Biol., 147: 761-773, 1999
    • (1999) J. Cell Biol. , vol.147 , pp. 761-773
    • Chang, C.C.1    Warren, D.S.2    Sacksteder, K.A.3    Gould, S.J.4
  • 39
    • 0036663192 scopus 로고    scopus 로고
    • Peroxisome biogenesis and protein import in plants, animals and yeasts: Enigma and variations?
    • Sparkes I.A., Baker A., Peroxisome biogenesis and protein import in plants, animals and yeasts: enigma and variations? (review), Mol. Membr. Biol., 19: 171-185, 2002
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 171-185
    • Sparkes, I.A.1    Baker, A.2
  • 40
    • 0036668807 scopus 로고    scopus 로고
    • Peroxisome remnants in pex3-delta cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes
    • Hazra P.P., Suriapranata I., Snyder W.B., Subramani S., Peroxisome remnants in pex3-delta cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes, Traffic, 3: 560-574, 2002
    • (2002) Traffic , vol.3 , pp. 560-574
    • Hazra, P.P.1    Suriapranata, I.2    Snyder, W.B.3    Subramani, S.4
  • 41
    • 0035805208 scopus 로고    scopus 로고
    • Peroxisomal protein import: The paradigm shifts
    • Smith M.D., Schnell D.J., Peroxisomal protein import: The paradigm shifts, Cell, 105: 293-296, 2001
    • (2001) Cell , vol.105 , pp. 293-296
    • Smith, M.D.1    Schnell, D.J.2
  • 42
    • 0028783455 scopus 로고
    • How proteins penetrate peroxisomes
    • Rachubinski R.A., Subramani S., How proteins penetrate peroxisomes, Cell, 83: 525-528, 1995
    • (1995) Cell , vol.83 , pp. 525-528
    • Rachubinski, R.A.1    Subramani, S.2
  • 43
    • 0035928730 scopus 로고    scopus 로고
    • Peroxisomes: The extended shuttle to the peroxisome matrix
    • Kunau W.H., Peroxisomes: The extended shuttle to the peroxisome matrix, Curr. Biol., 11: R659-R662, 2001
    • (2001) Curr. Biol. , vol.11
    • Kunau, W.H.1
  • 44
    • 0036273592 scopus 로고    scopus 로고
    • Peroxisomal-protein import: Is it really that complex?
    • Gould S.J., Collins C.S., Peroxisomal-protein import: is it really that complex?, Nat. Rev. Mol. Cell Biol., 3: 382-389, 2002
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 382-389
    • Gould, S.J.1    Collins, C.S.2
  • 46
    • 0035917528 scopus 로고    scopus 로고
    • The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol
    • Dammai V., Subramani S., The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol, Cell, 105: 187-196, 2001
    • (2001) Cell , vol.105 , pp. 187-196
    • Dammai, V.1    Subramani, S.2
  • 48
    • 0033549487 scopus 로고    scopus 로고
    • Pex22p of Pichia pastoris, essential for peroxisomal matrix protein import, anchors the ubiquitin-conjugating enzyme, Pex4p, on the peroxisomal membrane
    • Koller A., Snyder W.B., Faber K.N., Wenzel T.J., Rangell L., Keller G.A., Subramani S., Pex22p of Pichia pastoris, essential for peroxisomal matrix protein import, anchors the ubiquitin-conjugating enzyme, Pex4p, on the peroxisomal membrane, J. Cell Biol., 146: 99-112, 1999
    • (1999) J. Cell Biol. , vol.146 , pp. 99-112
    • Koller, A.1    Snyder, W.B.2    Faber, K.N.3    Wenzel, T.J.4    Rangell, L.5    Keller, G.A.6    Subramani, S.7
  • 49
    • 0032127487 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzyme Pex4p of Hansenula polymorpha is required for efficient functioning of the PTS1 import machinery
    • van der Klei I.J., Hilbrands R.E., Kiel J., Rasmussen S.W., Cregg J.M., Veenhuis M., The ubiquitin-conjugating enzyme Pex4p of Hansenula polymorpha is required for efficient functioning of the PTS1 import machinery, EMBO J., 17: 3608-3618, 1998
    • (1998) EMBO J. , vol.17 , pp. 3608-3618
    • Van Der Klei, I.J.1    Hilbrands, R.E.2    Kiel, J.3    Rasmussen, S.W.4    Cregg, J.M.5    Veenhuis, M.6
  • 50
    • 0041827355 scopus 로고    scopus 로고
    • Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import machinery of the peroxisome
    • Eckert J.H., Johnsson N., Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import machinery of the peroxisome, J. Cell Sci., 116: 3623-3634, 2003
    • (2003) J. Cell Sci. , vol.116 , pp. 3623-3634
    • Eckert, J.H.1    Johnsson, N.2
  • 52
    • 0023632725 scopus 로고
    • Proton ionophores prevent assembly of a peroxisomal protein
    • Bellion E., Goodman J.M., Proton ionophores prevent assembly of a peroxisomal protein, Cell, 48: 165-173, 1987
    • (1987) Cell , vol.48 , pp. 165-173
    • Bellion, E.1    Goodman, J.M.2
  • 53
    • 0030021833 scopus 로고    scopus 로고
    • Insertion of the 70kDa peroxisomal membrane protein into peroxisomal membrane in vivo and in vitro
    • Imanaka T., Shinina Y., Takano Y., Hashimoto T., Osumi T., Insertion of the 70kDa peroxisomal membrane protein into peroxisomal membrane in vivo and in vitro, J. Biol. Chem., 271: 3706-3713, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 3706-3713
    • Imanaka, T.1    Shinina, Y.2    Takano, Y.3    Hashimoto, T.4    Osumi, T.5
  • 54
    • 0027759463 scopus 로고
    • In vitro insertion of the 22kDa peroxisomal membrane protein into isolated rat liver peroxisomes
    • Diestelkotter P., Just W.W., In vitro insertion of the 22kDa peroxisomal membrane protein into isolated rat liver peroxisomes., J. Biol. Chem., 123: 1717-1725, 1993
    • (1993) J. Biol. Chem. , vol.123 , pp. 1717-1725
    • Diestelkotter, P.1    Just, W.W.2
  • 55
    • 0345403569 scopus 로고    scopus 로고
    • Characterization of intermediates in the process of plant peroxisomal protein import
    • Pool M.R., Lopez-Huertas E., Baker A., Characterization of intermediates in the process of plant peroxisomal protein import, EMBO J., 17: 6854-6862, 1998
    • (1998) EMBO J. , vol.17 , pp. 6854-6862
    • Pool, M.R.1    Lopez-Huertas, E.2    Baker, A.3
  • 57
    • 0034615921 scopus 로고    scopus 로고
    • A stretch of positively charged amino acids at the N terminus of Hansenula polymorpha Pex3p is involved in incorporation of the protein into the peroxisomal membrane
    • Baerends R.J.S., Faber K.N., Kram A.M., Kiel J., van der Klei I.J., Veenhuis M., A stretch of positively charged amino acids at the N terminus of Hansenula polymorpha Pex3p is involved in incorporation of the protein into the peroxisomal membrane, J. Biol. Chem., 275: 9986-9995, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 9986-9995
    • Baerends, R.J.S.1    Faber, K.N.2    Kram, A.M.3    Kiel, J.4    Van Der Klei, I.J.5    Veenhuis, M.6
  • 58
    • 0029879509 scopus 로고    scopus 로고
    • The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop
    • Dyer J.M., McNew J.A., Goodman J.M., The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop, J. Cell Biol., 133: 269-280, 1996
    • (1996) J. Cell Biol. , vol.133 , pp. 269-280
    • Dyer, J.M.1    McNew, J.A.2    Goodman, J.M.3
  • 59
    • 0035815693 scopus 로고    scopus 로고
    • Discrete targeting signals direct Pmp47 to oleate-induced peroxisomes in Saccharomyces cerevisiae
    • Wang X.D., Unruh M.J., Goodman J.M., Discrete targeting signals direct Pmp47 to oleate-induced peroxisomes in Saccharomyces cerevisiae, J. Biol. Chem., 276: 10897-10905, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 10897-10905
    • Wang, X.D.1    Unruh, M.J.2    Goodman, J.M.3
  • 60
    • 0035937842 scopus 로고    scopus 로고
    • Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments - Study using human membrane protein PMP34
    • Honsho M., Fujiki Y., Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments - Study using human membrane protein PMP34, J. Biol. Chem., 276: 9375-9382, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 9375-9382
    • Honsho, M.1    Fujiki, Y.2
  • 61
    • 0035844874 scopus 로고    scopus 로고
    • Multiple distinct targeting signals in integral peroxisomal membrane proteins
    • Jones J.M., Morrell J.C., Gould S.J., Multiple distinct targeting signals in integral peroxisomal membrane proteins, J. Cell Biol., 153: 1141-1149, 2001
    • (2001) J. Cell Biol. , vol.153 , pp. 1141-1149
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 62
    • 0034717248 scopus 로고    scopus 로고
    • The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail
    • Mullen R.T., Trelease R.N., The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail, J. Biol. Chem., 275: 16337-16344, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 16337-16344
    • Mullen, R.T.1    Trelease, R.N.2
  • 64
    • 0037458610 scopus 로고    scopus 로고
    • M-LP, Mpv17-like protein, has a peroxisomal membrane targeting signal comprising a transmembrane domain and a positively charged loop and up-regulates expression of the manganese superoxide dismutase gene
    • Iida R., Yasuda T., Tsubota E., Takatsuka H., Masuyama M., Matsuki T., Kishi K., M-LP, Mpv17-like protein, has a peroxisomal membrane targeting signal comprising a transmembrane domain and a positively charged loop and up-regulates expression of the manganese superoxide dismutase gene, J. Biol. Chem., 278: 6301-6306, 2003
    • (2003) J. Biol. Chem. , vol.278 , pp. 6301-6306
    • Iida, R.1    Yasuda, T.2    Tsubota, E.3    Takatsuka, H.4    Masuyama, M.5    Matsuki, T.6    Kishi, K.7
  • 65
    • 0034616064 scopus 로고    scopus 로고
    • Targeting of the 22 kDa integral peroxisomal membrane protein
    • Pause B., Saffrich R., Hunziker A., Ansorge W., Just W.W., Targeting of the 22 kDa integral peroxisomal membrane protein, FEBS Lett., 471: 23-28, 2000
    • (2000) FEBS Lett. , vol.471 , pp. 23-28
    • Pause, B.1    Saffrich, R.2    Hunziker, A.3    Ansorge, W.4    Just, W.W.5
  • 66
    • 0142245609 scopus 로고    scopus 로고
    • Characterization of the targeting signal of the Arabidopsis 22- KD integral peroxisomal membrane protein
    • Murphy M.A., Phillipson B.A., Baker A., Mullen R.T., Characterization of the targeting signal of the Arabidopsis 22- kD integral peroxisomal membrane protein, Plant Physiol., 133: 813-828, 2003
    • (2003) Plant Physiol. , vol.133 , pp. 813-828
    • Murphy, M.A.1    Phillipson, B.A.2    Baker, A.3    Mullen, R.T.4
  • 67
    • 0035196588 scopus 로고    scopus 로고
    • Yarrowia lipolytica cells mutant for the peroxisomal peroxin Pex19p contain structures resembling wild-type peroxisomes
    • Lambkin G.R., Rachubinski R.A., Yarrowia lipolytica cells mutant for the peroxisomal peroxin Pex19p contain structures resembling wild-type peroxisomes, Mol. Biol. Cell, 12: 3353-3364, 2001
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3353-3364
    • Lambkin, G.R.1    Rachubinski, R.A.2
  • 69
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • Sacksteder K.A., Jones J.M., South S.T., Li X.L., Liu Y.F., Gould S.J., PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis, J. Cell Biol., 148: 931-944, 2000
    • (2000) J. Cell Biol. , vol.148 , pp. 931-944
    • Sacksteder, K.A.1    Jones, J.M.2    South, S.T.3    Li, X.L.4    Liu, Y.F.5    Gould, S.J.6
  • 70
    • 0034641098 scopus 로고    scopus 로고
    • The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane
    • Snyder W.B., Koller A., Choy A.J., Subramani S., The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane, J. Cell Biol., 149: 1171-1177, 2000
    • (2000) J. Cell Biol. , vol.149 , pp. 1171-1177
    • Snyder, W.B.1    Koller, A.2    Choy, A.J.3    Subramani, S.4
  • 71
    • 0034677197 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Pex3p and Pcx19p are required for proper localization and stability of peroxisomal membrane proteins
    • Hettema E.H., Girzalsky W., van den Berg M., Erdmann R., Distel B., Saccharomyces cerevisiae Pex3p and Pcx19p are required for proper localization and stability of peroxisomal membrane proteins, EMBO J., 19: 223-233, 2000
    • (2000) EMBO J. , vol.19 , pp. 223-233
    • Hettema, E.H.1    Girzalsky, W.2    Van Den Berg, M.3    Erdmann, R.4    Distel, B.5
  • 72
    • 0034972812 scopus 로고    scopus 로고
    • Human Pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences
    • Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P., Human Pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences, Mol. Cell. Biol., 21: 4413-4424, 2001
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4413-4424
    • Fransen, M.1    Wylin, T.2    Brees, C.3    Mannaerts, G.P.4    Van Veldhoven, P.P.5
  • 73
    • 0037113975 scopus 로고    scopus 로고
    • The membrane biogenesis peroxin Pexlop - Topogenesis and functional roles in peroxisomal membrane assembly
    • Honsho M., Hiroshige T., Fujiki Y., The membrane biogenesis peroxin Pexlop - Topogenesis and functional roles in peroxisomal membrane assembly, J. Biol. Chem., 277: 44513-44524, 2002
    • (2002) J. Biol. Chem. , vol.277 , pp. 44513-44524
    • Honsho, M.1    Hiroshige, T.2    Fujiki, Y.3
  • 76
    • 0041765775 scopus 로고    scopus 로고
    • Peroxisome biogenesis: Advances and conundrums
    • Lazarow P.B., Peroxisome biogenesis: advances and conundrums, Curr. Opin. Cell Biol., 15: 489-497, 2003
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 489-497
    • Lazarow, P.B.1
  • 78
    • 0028859252 scopus 로고
    • Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane-protein Pmp27p
    • Erdmann R., Blobel G., Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane-protein Pmp27p, J. Cell Biol., 128: 509-523, 1995
    • (1995) J. Cell Biol. , vol.128 , pp. 509-523
    • Erdmann, R.1    Blobel, G.2
  • 79
    • 0028783419 scopus 로고
    • The Candida boidinii peroxisomal membrane-protein Pmp30 has a role in peroxisomal proliferation and is functionally homologous to Pmp27 from Saccharomyces cerevisiae
    • Sakai Y., Marshall P.A., Saiganji A., Takabe K., Saiki H., Kato N., Goodman J.M., The Candida boidinii peroxisomal membrane-protein Pmp30 has a role in peroxisomal proliferation and is functionally homologous to Pmp27 from Saccharomyces cerevisiae, J. Bacteriol., 177: 6773-6781, 1995
    • (1995) J. Bacteriol. , vol.177 , pp. 6773-6781
    • Sakai, Y.1    Marshall, P.A.2    Saiganji, A.3    Takabe, K.4    Saiki, H.5    Kato, N.6    Goodman, J.M.7
  • 80
    • 0032545023 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p
    • Abe I., Fujiki Y., cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p, Biochem. Biophys. Res. Commun., 252: 529-533, 1998
    • (1998) Biochem. Biophys. Res. Commun , vol.252 , pp. 529-533
    • Abe, I.1    Fujiki, Y.2
  • 82
    • 0036882106 scopus 로고    scopus 로고
    • PEX11-alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation
    • Li X.L., Baumgart E., Dong G.X., Morrell J.C., Jimenez-Sanchez G., Valle D., Smith K.D., Gould S.J., PEX11-alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation, Mol. Cell. Biol., 22: 8226-8240, 2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8226-8240
    • Li, X.L.1    Baumgart, E.2    Dong, G.X.3    Morrell, J.C.4    Jimenez-Sanchez, G.5    Valle, D.6    Smith, K.D.7    Gould, S.J.8
  • 85
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vpslp, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • S5. Hoepfner D., van den Berg M., Philippsen P., Tabak H.F., Hettema E.H., A role for Vpslp, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae, J. Cell Biol., 155: 979-990, 2001
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    Van Den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 88
    • 0034782175 scopus 로고    scopus 로고
    • Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings
    • Germain V., Rylott E.L., Larson T.R., Sherson S.M., Bechtold N., Carde J.P., Bryce J.H., Graham I.A., Smith S.M., Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings, Plant J., 28: 1-12, 2001
    • (2001) Plant J. , vol.28 , pp. 1-12
    • Germain, V.1    Rylott, E.L.2    Larson, T.R.3    Sherson, S.M.4    Bechtold, N.5    Carde, J.P.6    Bryce, J.H.7    Graham, I.A.8    Smith, S.M.9
  • 89
    • 0034820746 scopus 로고    scopus 로고
    • Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant
    • Hayashi Y., Hayashi M., Hayashi H., Hara-Nishimura I., Nishimura M., Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant, Protoplasma, 218: 83-94, 2001
    • (2001) Protoplasma , vol.218 , pp. 83-94
    • Hayashi, Y.1    Hayashi, M.2    Hayashi, H.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 90
    • 0034733570 scopus 로고    scopus 로고
    • Regulation of peroxisome size and number by fatty acid beta- Oxidation in the yeast Yarrowia lipolytica
    • Smith J.J., Brown T.W., Eitzen G.A., Rachubinski R.A., Regulation of peroxisome size and number by fatty acid beta- oxidation in the yeast Yarrowia lipolytica, J. Biol. Chem., 275: 20168-20178, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 20168-20178
    • Smith, J.J.1    Brown, T.W.2    Eitzen, G.A.3    Rachubinski, R.A.4
  • 91
    • 0034617992 scopus 로고    scopus 로고
    • Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae
    • van Roermund C.W.T., Tabak H.F., van den Berg M., Wanders R.J.A., Hettema E.H., Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae, J. Cell Biol., 150: 489-497, 2000
    • (2000) J. Cell Biol. , vol.150 , pp. 489-497
    • Van Roermund, C.W.T.1    Tabak, H.F.2    Van Den Berg, M.3    Wanders, R.J.A.4    Hettema, E.H.5
  • 93
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of Pex11p and the novel Pex25p and Pex27p in peroxisome biogenesis
    • Rottensteiner H., Stein K., Sonnenhol E., Erdmann R., Conserved function of Pex11p and the novel Pex25p and Pex27p in peroxisome biogenesis, Mol. Biol. Cell, 14: 4316-4328, 2003
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 94
    • 0141764783 scopus 로고    scopus 로고
    • Pex11-related proteins in peroxisome dynamics: A role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae
    • Tam Y.Y.C., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M., Aitchison J.D., Rachubinski R.A., Pex11-related proteins in peroxisome dynamics: A role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae, Mol. Biol. Cell, 14: 4089-4102, 2003
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4089-4102
    • Tam, Y.Y.C.1    Torres-Guzman, J.C.2    Vizeacoumar, F.J.3    Smith, J.J.4    Marelli, M.5    Aitchison, J.D.6    Rachubinski, R.A.7
  • 95
    • 0037632981 scopus 로고    scopus 로고
    • Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes
    • Birschmann I., Stroobants A.K., van den Berg M., Schafer A., Rosenkranz K., Kunau W.H., Tabak H.F., Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes, Mol. Biol. Cell, 14: 2226-2236, 2003
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2226-2236
    • Birschmann, I.1    Stroobants, A.K.2    Van Den Berg, M.3    Schafer, A.4    Rosenkranz, K.5    Kunau, W.H.6    Tabak, H.F.7
  • 96
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • Matsumoto N., Tamura S., Fujiki Y., The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes, Nat. Cell Biol., 5: 454-460, 2003
    • (2003) Nat. Cell Biol. , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3


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