메뉴 건너뛰기




Volumn 24, Issue 20, 2004, Pages 8895-8906

Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5p

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; DOCKING PROTEIN; MATRIX PROTEIN; PEROXISOMAL TARGETING SIGNAL 1; PEROXISOMAL TARGETING SIGNAL 2; PROTEIN PEX5P; PROTENI PEX18P; RECEPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 4744375324     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.20.8895-8906.2004     Document Type: Article
Times cited : (90)

References (81)
  • 3
    • 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., W. Girzalsky, M. Veenhuis, and W.-H. Kunau. 2001. 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) Eur. J. Cell Biol. , vol.80 , pp. 257-270
    • Albertini, M.1    Girzalsky, W.2    Veenhuis, M.3    Kunau, W.-H.4
  • 4
    • 0030890954 scopus 로고    scopus 로고
    • Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways
    • Albertini, M., P. Rehling, R. Erdmann, W. Girzalsky, J. A. K. W. Kiel, M. Veenhuis, and W.-H. Kunau. 1997. Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways. Cell 89:83-92.
    • (1997) Cell , vol.89 , pp. 83-92
    • Albertini, M.1    Rehling, P.2    Erdmann, R.3    Girzalsky, W.4    Kiel, J.A.K.W.5    Veenhuis, M.6    Kunau, W.-H.7
  • 5
    • 0034383397 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction
    • Barnett, P., G. Bottger, A. T. J. Klein, H. F. Tabak, and B. Distel. 2000. The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction. EMBO J. 19:6382-6391.
    • (2000) EMBO J. , vol.19 , pp. 6382-6391
    • Barnett, P.1    Bottger, G.2    Klein, A.T.J.3    Tabak, H.F.4    Distel, B.5
  • 6
    • 0016369243 scopus 로고
    • Isolation of rat liver peroxisomes
    • Baudhuin, P. 1974. Isolation of rat liver peroxisomes. Methods Enzymol. 31:356-368.
    • (1974) Methods Enzymol. , vol.31 , pp. 356-368
    • Baudhuin, P.1
  • 7
    • 0033739464 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner
    • Bottger, G., P. Barnett, A. T. Klein, A. Kragt, H. F. Tabak, and B. Distel. 2000. Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner. Mol. Biol. Cell 11:3963-3976.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3963-3976
    • Bottger, G.1    Barnett, P.2    Klein, A.T.3    Kragt, A.4    Tabak, H.F.5    Distel, B.6
  • 8
    • 0031854532 scopus 로고    scopus 로고
    • An isoform of Pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes
    • Braverman, N., G. Dodt, S. J. Gould, and D. Valle. 1998. An isoform of Pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes. Hum. Mol. Genet. 7:1195-1205.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1195-1205
    • Braverman, N.1    Dodt, G.2    Gould, S.J.3    Valle, D.4
  • 9
    • 0030946632 scopus 로고    scopus 로고
    • Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata
    • Braverman, N., G. Steel, C. Obie, A. Moser, H. Moser, S. J. Gould, and D. Valle. 1997. Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata. Nat. Genet. 15:369-370.
    • (1997) Nat. Genet. , vol.15 , pp. 369-370
    • Braverman, N.1    Steel, G.2    Obie, C.3    Moser, A.4    Moser, H.5    Gould, S.J.6    Valle, D.7
  • 10
    • 0027996438 scopus 로고
    • The tetratricopeptide repeat-domain of the Pas10 protein of Saccharomyces cerevisiae is essential for binding the peroxisomal targeting signal SKL
    • Brocard, C., F. Kragler, M. M. Simon, T. Schuster, and A. Hartig. 1994. The tetratricopeptide repeat-domain of the Pas10 protein of Saccharomyces cerevisiae is essential for binding the peroxisomal targeting signal SKL. Biochem. Biophys. Res. Commun. 204:1016-1022.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 1016-1022
    • Brocard, C.1    Kragler, F.2    Simon, M.M.3    Schuster, T.4    Hartig, A.5
  • 11
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast: Identification of mammalian proteins that react with the leucine zipper of Jun
    • Chevray, P. M., and D. Nathans. 1992. Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc. Natl. Acad. Sci. USA 89:5789-5793.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2
  • 12
    • 0034697983 scopus 로고    scopus 로고
    • Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases
    • Chudzik, D. M., P. A. Michels, S. de Walque, and W. G. Hol. 2000. Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases. J. Mol. Biol. 300:697-707.
    • (2000) J. Mol. Biol. , vol.300 , pp. 697-707
    • Chudzik, D.M.1    Michels, P.A.2    De Walque, S.3    Hol, W.G.4
  • 13
    • 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., and S. Subramani. 2001. The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol. Cell 105:187-196.
    • (2001) Cell , vol.105 , pp. 187-196
    • Dammai, V.1    Subramani, S.2
  • 15
    • 0025335782 scopus 로고
    • Structure and transcriptional control of the Saccharomyces cerevisiae POX1 gene encoding acyl-coenzyme A oxidase
    • Dmochowska, A., D. Dignard, R. Maleszka, and D. Y. Thomas. 1990. Structure and transcriptional control of the Saccharomyces cerevisiae POX1 gene encoding acyl-coenzyme A oxidase. Gene 88:247-252.
    • (1990) Gene , vol.88 , pp. 247-252
    • Dmochowska, A.1    Dignard, D.2    Maleszka, R.3    Thomas, D.Y.4
  • 16
    • 0028817372 scopus 로고
    • Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders
    • Dodt, G., N. Braverman, C. Wong, A. Moser, H. W. Moser, P. Watkins, D. Valle, and S. J. Gould. 1995. Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders. Nat. Genet. 9:115-125.
    • (1995) Nat. Genet. , vol.9 , pp. 115-125
    • Dodt, G.1    Braverman, N.2    Wong, C.3    Moser, A.4    Moser, H.W.5    Watkins, P.6    Valle, D.7    Gould, S.J.8
  • 17
    • 0030459304 scopus 로고    scopus 로고
    • Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: Evidence that PTS1 protein import is mediated by a cycling receptor
    • Dodt, G., and S. J. Gould. 1996. Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor. J. Cell Biol. 135:1763-1774.
    • (1996) J. Cell Biol. , vol.135 , pp. 1763-1774
    • Dodt, G.1    Gould, S.J.2
  • 18
    • 0035834711 scopus 로고    scopus 로고
    • Domain mapping of human PEX5 reveals functional and structural similarities to Saccharomyces cerevisiae Pex18p and Pex21p
    • Dodt, G., D. Warren, E. Becker, P. Rehling, and S. J. Gould. 2001. Domain mapping of human PEX5 reveals functional and structural similarities to Saccharomyces cerevisiae Pex18p and Pex21p. J. Biol. Chem. 276:41769-41781.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41769-41781
    • Dodt, G.1    Warren, D.2    Becker, E.3    Rehling, P.4    Gould, S.J.5
  • 21
    • 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
    • Einwächter, H., S. Sowinski, W. H. Kunau, and W. Schliebs. 2001. 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) EMBO Rep. , vol.2 , pp. 1035-1039
    • Einwächter, H.1    Sowinski, S.2    Kunau, W.H.3    Schliebs, W.4
  • 23
    • 0029840399 scopus 로고    scopus 로고
    • The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import of PTS1 containing proteins
    • Elgersma, Y., L. Kwast, A. Klein, T. Voorn-Brouwer, M. van den Berg, B. Metzig, T. America, H. F. Tabak, and B. Distel. 1996. The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import of PTS1 containing proteins. J. Cell Biol. 135:97-109.
    • (1996) J. Cell Biol. , vol.135 , pp. 97-109
    • Elgersma, Y.1    Kwast, L.2    Klein, A.3    Voorn-Brouwer, T.4    Van Den Berg, M.5    Metzig, B.6    America, T.7    Tabak, H.F.8    Distel, B.9
  • 24
    • 0029795490 scopus 로고    scopus 로고
    • Identification of Pex13p, a peroxisomal membrane receptor for the PTS1 recognition factor
    • Erdmann, R., and G. Blobel. 1996. Identification of Pex13p, a peroxisomal membrane receptor for the PTS1 recognition factor. J. Cell Biol. 135:111-121.
    • (1996) J. Cell Biol. , vol.135 , pp. 111-121
    • Erdmann, R.1    Blobel, G.2
  • 25
    • 0028131544 scopus 로고
    • Purification and immunolocalization of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae
    • Erdmann, R., and W.-H. Kunau. 1994. Purification and immunolocalization of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae. Yeast 10:1173-1182.
    • (1994) Yeast , vol.10 , pp. 1173-1182
    • Erdmann, R.1    Kunau, W.-H.2
  • 26
  • 28
    • 0032493298 scopus 로고    scopus 로고
    • Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import
    • Fransen, M., S. R. Terlecky, and S. Subramani. 1998. Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import. Proc. Natl. Acad. Sci. USA 95:8087-8092.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8087-8092
    • Fransen, M.1    Terlecky, S.R.2    Subramani, S.3
  • 29
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto, G. J., B. V. Geisbrecht, S. J. Gould, and J. M. Berg. 2000. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat. Struct. Biol. 7:1091-1095.
    • (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
  • 30
    • 0029795686 scopus 로고    scopus 로고
    • Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor
    • Gould, S. J., J. E. Kalish, J. C. Morrell, J. Bjorkman, A. J. Urquhart, and D. I. Crane. 1996. Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor. J. Cell Biol. 135:85-95.
    • (1996) J. Cell Biol. , vol.135 , pp. 85-95
    • Gould, S.J.1    Kalish, J.E.2    Morrell, J.C.3    Bjorkman, J.4    Urquhart, A.J.5    Crane, D.I.6
  • 32
    • 0036668807 scopus 로고    scopus 로고
    • Peroxisome remnants in pex3delta cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes
    • Hazra, P. P., I. Suriapranata, W. B. Snyder, and S. Subramani. 2002. Peroxisome remnants in pex3delta cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes. Traffic 3:560-574.
    • (2002) Traffic , vol.3 , pp. 560-574
    • Hazra, P.P.1    Suriapranata, I.2    Snyder, W.B.3    Subramani, S.4
  • 33
    • 0034677197 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins
    • Hettema, E. H., W. Girzalsky, M. van Den Berg, R. Erdmann, and B. Distel. 2000. Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins. EMBO J. 19: 223-233.
    • (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
  • 34
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., B. Krummel, and R. K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 37
    • 0034607980 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 receptor protein PEX5 from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization
    • Jardim, A., W. Liu, E. Zheleznova, and B. Ullman. 2000. Peroxisomal targeting signal-1 receptor protein PEX5 from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization. J. Biol. Chem. 275:13637-13644.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13637-13644
    • Jardim, A.1    Liu, W.2    Zheleznova, E.3    Ullman, B.4
  • 38
    • 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., M. van Den Berg, G. Bottger, H. F. Tabak, and B. Distel. 2002. 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) J. Biol. Chem. , vol.277 , pp. 25011-25019
    • Klein, A.T.1    Van Den Berg, M.2    Bottger, G.3    Tabak, H.F.4    Distel, B.5
  • 39
    • 0032775010 scopus 로고    scopus 로고
    • Epitope tagging of yeast genes using a PCR-based strategy: More tags and improved practical routines
    • Knop, M., K. Siegers, G. Pereira, W. Zachariae, B. Winsor, K. Nasmyth, and E. Schiebel. 1999. Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines. Yeast 15:963-972.
    • (1999) Yeast , vol.15 , pp. 963-972
    • Knop, M.1    Siegers, K.2    Pereira, G.3    Zachariae, W.4    Winsor, B.5    Nasmyth, K.6    Schiebel, E.7
  • 41
    • 0041765775 scopus 로고    scopus 로고
    • Peroxisome biogenesis: Advances and conundrums
    • Lazarow, P. B. 2003. Peroxisome biogenesis: advances and conundrums. Curr. Opin. Cell Biol. 15:489-497.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 489-497
    • Lazarow, P.B.1
  • 42
    • 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., R. Erdmann, M. Veenhuis, and W.-H. Kunau. 1994. 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) EMBO J. , vol.13 , pp. 4908-4918
    • Marzioch, M.1    Erdmann, R.2    Veenhuis, M.3    Kunau, W.-H.4
  • 43
    • 0034647529 scopus 로고    scopus 로고
    • Disruption of the interaction of the longer isoform of Pex5p, Pex5pL, with Pex7p abolishes peroxisome targeting signal type 2 protein import in mammals. Study with a novel Pex5-impaired Chinese hamster ovary cell mutant
    • Matsumura, T., H. Otera, and Y. Fujiki. 2000. Disruption of the interaction of the longer isoform of Pex5p, Pex5pL, with Pex7p abolishes peroxisome targeting signal type 2 protein import in mammals. Study with a novel Pex5-impaired Chinese hamster ovary cell mutant. J. Biol. Chem. 275:21715-21721.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21715-21721
    • Matsumura, T.1    Otera, H.2    Fujiki, Y.3
  • 44
    • 0027168271 scopus 로고
    • The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells - The Pas8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family
    • McCollum, D., E. Monosov, and S. Subramani. 1993. The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells - the Pas8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family. J. Cell Biol. 121:761-774.
    • (1993) J. Cell Biol. , vol.121 , pp. 761-774
    • McCollum, D.1    Monosov, E.2    Subramani, S.3
  • 45
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew, J. A., and J. M. Goodman. 1994. An oligomeric protein is imported into peroxisomes in vivo. J. Cell Biol. 127:1245-1257.
    • (1994) J. Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 46
    • 0016412389 scopus 로고
    • 3-Ketoacyl-CoA thiolases of mammalian tissues
    • Middleton, B. 1975. 3-Ketoacyl-CoA thiolases of mammalian tissues. Methods Enzymol. 35:128-136.
    • (1975) Methods Enzymol. , vol.35 , pp. 128-136
    • Middleton, B.1
  • 47
    • 0037414447 scopus 로고    scopus 로고
    • Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences
    • Neuberger, G., S. Maurer-Stroh, B. Eisenhaber, A. Hartig, and F. Eisenhaber. 2003. Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences. J. Mol. Biol. 328:567-579.
    • (2003) J. Mol. Biol. , vol.328 , pp. 567-579
    • Neuberger, G.1    Maurer-Stroh, S.2    Eisenhaber, B.3    Hartig, A.4    Eisenhaber, F.5
  • 48
    • 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., T. Harano, M. Honsho, K. Ghaedi, S. Mukai, A. Tanaka, A. Kawai, N. Shimizu, and Y. Fujiki. 2000. 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) 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
  • 49
    • 0036179374 scopus 로고    scopus 로고
    • Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: Conserved Pex5p WXXXF/Y motifs are critical for matrix protein import
    • Otera, H., K. Setoguchi, M. Hamasaki, T. Kumashiro, N. Shimizu, and Y. Fujiki. 2002. Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. Mol. Cell. Biol. 22:1639-1655.
    • (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
  • 50
    • 0028149887 scopus 로고
    • Peroxisome biogenesis: Multiple pathways of protein import
    • Purdue, P. E., and P. B. Lazarow. 1994. Peroxisome biogenesis: multiple pathways of protein import. J. Biol. Chem. 269:30065-30068.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30065-30068
    • Purdue, P.E.1    Lazarow, P.B.2
  • 51
    • 0035861688 scopus 로고    scopus 로고
    • Pex18p is constitutively degraded during peroxisome biogenesis
    • Purdue, P. E., and P. B. Lazarow. 2001. Pex18p is constitutively degraded during peroxisome biogenesis. J. Biol. Chem. 276:47684-47689.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47684-47689
    • Purdue, P.E.1    Lazarow, P.B.2
  • 52
    • 0032576614 scopus 로고    scopus 로고
    • Pex18p and Pex21p, a novel pair of related peroxins essential for peroxisomal targeting by the PTS2 pathway
    • Purdue, P. E., X. Yang, and P. B. Lazarow. 1998. Pex18p and Pex21p, a novel pair of related peroxins essential for peroxisomal targeting by the PTS2 pathway. J. Cell Biol. 143:1859-1869.
    • (1998) J. Cell Biol. , vol.143 , pp. 1859-1869
    • Purdue, P.E.1    Yang, X.2    Lazarow, P.B.3
  • 53
    • 0029903045 scopus 로고    scopus 로고
    • The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene
    • Rehling, P., M. Marzioch, F. Niesen, E. Wittke, M. Veenhuis, and W.-H. Kunau. 1996. The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene. EMBO J. 15:2901-2913.
    • (1996) EMBO J. , vol.15 , pp. 2901-2913
    • Rehling, P.1    Marzioch, M.2    Niesen, F.3    Wittke, E.4    Veenhuis, M.5    Kunau, W.-H.6
  • 56
    • 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., G. Dodt, K. Kirchberg, A. Wegner, W. Nastainczyk, W. H. Kunau, and W. Schliebs. 2001. 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) 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
  • 57
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H., and R. D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16:339-346.
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 58
    • 0033605116 scopus 로고    scopus 로고
    • Recombinant human peroxisomal targeting signal receptor PEX5. Structural basis for interaction of pex5 with pex14
    • Schliebs, W., J. Saidowsky, B. Agianian, G. Dodt, F. W. Herberg, and W. H. Kunau. 1999. Recombinant human peroxisomal targeting signal receptor PEX5. Structural basis for interaction of pex5 with pex14. J. Biol. Chem. 274:5666-5673.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5666-5673
    • Schliebs, W.1    Saidowsky, J.2    Agianian, B.3    Dodt, G.4    Herberg, F.W.5    Kunau, W.H.6
  • 59
    • 0037459073 scopus 로고    scopus 로고
    • Protein translocons: Multifunctional mediators of protein translocation across membranes
    • Schnell, D. J., and D. N. Hebert. 2003. Protein translocons: multifunctional mediators of protein translocation across membranes. Cell 112:491-505.
    • (2003) Cell , vol.112 , pp. 491-505
    • Schnell, D.J.1    Hebert, D.N.2
  • 60
    • 0033617195 scopus 로고    scopus 로고
    • The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis
    • Shimizu, N., R. Itoh, Y. Hirono, H. Otera, K. Ghaedi, K. Tateishi, S. Tamura, K. Okumoto, T. Harano, S. Mukai, and Y. Fujiki. 1999. The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J. Biol. Chem. 274:12593-12604.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12593-12604
    • Shimizu, N.1    Itoh, R.2    Hirono, Y.3    Otera, H.4    Ghaedi, K.5    Tateishi, K.6    Tamura, S.7    Okumoto, K.8    Harano, T.9    Mukai, S.10    Fujiki, Y.11
  • 61
    • 0037326247 scopus 로고    scopus 로고
    • Pex7p and Pex20p of Newospora crassa function together in PTS2-dependent protein import into peroxisomes
    • Sichting, M., A. Schell-Steven, H. Prokisch, R. Erdmann, and H. Rottensteiner. 2003. Pex7p and Pex20p of Newospora crassa function together in PTS2-dependent protein import into peroxisomes. Mol. Biol. Cell 14:810-821.
    • (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
  • 62
    • 0035846962 scopus 로고    scopus 로고
    • A role for the peroxin Pex8p in Pex20p-dependent thiolase import into peroxisomes of the yeast Yarrowia lipolytica
    • Smith, J. J., and R. A. Rachuhinski. 2001. A role for the peroxin Pex8p in Pex20p-dependent thiolase import into peroxisomes of the yeast Yarrowia lipolytica. J. Cell Biol. 276:1618-1625.
    • (2001) J. Cell Biol. , vol.276 , pp. 1618-1625
    • Smith, J.J.1    Rachuhinski, R.A.2
  • 63
    • 0036663192 scopus 로고    scopus 로고
    • Peroxisome biogenesis and protein import in plants, animals and yeasts: Enigma and variations?
    • Sparkes, I. A., and A. Baker. 2002. Peroxisome biogenesis and protein import in plants, animals and yeasts: enigma and variations? Mol. Membr. Biol. 19:171-185.
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 171-185
    • Sparkes, I.A.1    Baker, A.2
  • 64
    • 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., A. Schell-Steven, R. Erdmann, and H. Rottensteiner. 2002. Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: implications for the first steps in PTS2 protein import. Mol. Cell. Biol. 22:6056-6069.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6056-6069
    • Stein, K.1    Schell-Steven, A.2    Erdmann, R.3    Rottensteiner, H.4
  • 65
    • 0025941962 scopus 로고
    • A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase
    • Swinkels, B. W., S. J. Gould, A. G. Bodnar, R. A. Rachubinski, and S. Subramani. 1991. A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase. EMBO J. 10:3255-3262.
    • (1991) EMBO J. , vol.10 , pp. 3255-3262
    • Swinkels, B.W.1    Gould, S.J.2    Bodnar, A.G.3    Rachubinski, R.A.4    Subramani, S.5
  • 66
    • 0034652255 scopus 로고    scopus 로고
    • Tetratricopeptide repeat domain of Yarrowia lipolytica Pex5p is essential for recognition of the type 1 peroxisomal targeting signal but does not confer full biological activity on Pex5p
    • Szilard, R. K., and R. A. Rachubinski. 2000. Tetratricopeptide repeat domain of Yarrowia lipolytica Pex5p is essential for recognition of the type 1 peroxisomal targeting signal but does not confer full biological activity on Pex5p. Biochem. J. 346:177-184.
    • (2000) Biochem. J. , vol.346 , pp. 177-184
    • Szilard, R.K.1    Rachubinski, R.A.2
  • 67
    • 0029087571 scopus 로고
    • The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal
    • Terlecky, S. R., W. M. Nuttley, D. McCollnm, E. Sock, and S. Subramani. 1995. The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal. EMBO J. 14:3627-3634.
    • (1995) EMBO J. , vol.14 , pp. 3627-3634
    • Terlecky, S.R.1    Nuttley, W.M.2    McCollnm, D.3    Sock, E.4    Subramani, S.5
  • 68
    • 0032572580 scopus 로고    scopus 로고
    • Pex20p of the yeast Yarrowia lipolytica is required for the oligomerization of thiolase in the cytosol and for its targeting to the peroxisome
    • Titorenko, V. I., J. J. Smith, R. K. Szilard, and R. A. Rachubinski. 1998. Pex20p of the yeast Yarrowia lipolytica is required for the oligomerization of thiolase in the cytosol and for its targeting to the peroxisome. J. Cell Biol. 142:403-420.
    • (1998) J. Cell Biol. , vol.142 , pp. 403-420
    • Titorenko, V.I.1    Smith, J.J.2    Szilard, R.K.3    Rachubinski, R.A.4
  • 69
    • 0016369244 scopus 로고
    • Isolation of subcellular organelles of metabolism on isopycnic sucrose gradients
    • Tolbert, N. E. 1974. Isolation of subcellular organelles of metabolism on isopycnic sucrose gradients. Methods Enzymol. 31:734-746.
    • (1974) Methods Enzymol. , vol.31 , pp. 734-746
    • Tolbert, N.E.1
  • 70
    • 0034635364 scopus 로고    scopus 로고
    • Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p
    • Urquhart, A. J., D. Kennedy, S. J. Gould, and D. I. Crane. 2000. Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p. J. Biol. Chem. 275:4127-4136.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4127-4136
    • Urquhart, A.J.1    Kennedy, D.2    Gould, S.J.3    Crane, D.I.4
  • 71
    • 0036702163 scopus 로고    scopus 로고
    • Peroxisomes: Flexible and dynamic organelles
    • van der Klei, I., and M. Veenhuis. 2002. Peroxisomes: flexible and dynamic organelles. Curr. Opin. Cell Biol. 14:500-505.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 500-505
    • Van Der Klei, I.1    Veenhuis, M.2
  • 73
    • 0027138676 scopus 로고
    • PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae
    • Van der Leij, I., M. M. Franse, Y. Elgersma, B. Distel, and H. F. Tabak. 1993. PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 90:11782-11786.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11782-11786
    • Van Der Leij, I.1    Franse, M.M.2    Elgersma, Y.3    Distel, B.4    Tabak, H.F.5
  • 74
    • 0026709058 scopus 로고
    • Isolation of peroxisome assembly mutants from Saccharomyces cerevisiae with different morphologies using a novel positive selection procedure
    • van der Leij, I., M. van den Berg, R. Boot, M. M. Franse, B. Distel, and H. F. Tabak. 1992. Isolation of peroxisome assembly mutants from Saccharomyces cerevisiae with different morphologies using a novel positive selection procedure. J. Cell Biol. 119:153-162.
    • (1992) J. Cell Biol. , vol.119 , pp. 153-162
    • Van Der Leij, I.1    Van Den Berg, M.2    Boot, R.3    Franse, M.M.4    Distel, B.5    Tabak, H.F.6
  • 75
    • 0242353302 scopus 로고    scopus 로고
    • Physical interactions of the peroxisomal targeting signal 1 receptor Pex5p, studied by fluorescence correlation spectroscopy
    • Wang, D., N. V. Visser, M. Veenhuis, and I. J. van der Klei. 2003. Physical interactions of the peroxisomal targeting signal 1 receptor Pex5p, studied by fluorescence correlation spectroscopy. J. Biol. Chem. 278:43340-43345.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43340-43345
    • Wang, D.1    Visser, N.V.2    Veenhuis, M.3    Van Der Klei, I.J.4
  • 76
    • 0028061714 scopus 로고
    • The Hansenula polymorpha PER1 gene is essential for peroxisome biogenesis and encodes a peroxisomal matrix protein with both carboxy- and amino-terminal targeting signals
    • Waterham, H. R., V. I. Titorenko, P. Haima, J. M. Cregg, W. Harder, and M. Veenhuis. 1994. The Hansenula polymorpha PER1 gene is essential for peroxisome biogenesis and encodes a peroxisomal matrix protein with both carboxy- and amino-terminal targeting signals. J. Cell Biol. 127:737-749.
    • (1994) J. Cell Biol. , vol.127 , pp. 737-749
    • Waterham, H.R.1    Titorenko, V.I.2    Haima, P.3    Cregg, J.M.4    Harder, W.5    Veenhuis, M.6
  • 77
    • 0033672549 scopus 로고    scopus 로고
    • Mitochondria-targeted green fluorescent proteins: Convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae
    • Westermann, B., and W. Neupert. 2000. Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae. Yeast 16:1421-1427.
    • (2000) Yeast , vol.16 , pp. 1421-1427
    • Westermann, B.1    Neupert, W.2
  • 78
    • 0029024783 scopus 로고
    • Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders
    • Wiemer, E. A. C., W. M. Nuttley, B. L. Bertolaet, Li, X., U. Francke, M. J. Wheelock, J. Anné, K. R., and S. Subramani. 1995. Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders. J. Cell Biol. 130:51-65.
    • (1995) J. Cell Biol. , vol.130 , pp. 51-65
    • Wiemer, E.A.C.1    Nuttley, W.M.2    Bertolaet, B.L.3    Li, X.4    Francke, U.5    Wheelock, M.J.6    Anné, J.7    Ro, K.8    Subramani, S.9
  • 79
    • 0032213098 scopus 로고    scopus 로고
    • The plant PTS1 receptor: Similarities and differences to its human and yeast counterparts
    • Wimmer, C., M. Schmid, M. Veenhuis, and C. Gietl. 1998. The plant PTS1 receptor: similarities and differences to its human and yeast counterparts. Plant J. 16:453-464.
    • (1998) Plant J. , vol.16 , pp. 453-464
    • Wimmer, C.1    Schmid, M.2    Veenhuis, M.3    Gietl, C.4
  • 80
    • 0035115053 scopus 로고    scopus 로고
    • Eci1p uses a PTS1 to enter peroxisomes: Either its own or that of a partner, Dci1p
    • Yang, X., P. E. Purdue, and P. B. Lazarow. 2001. Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a partner, Dci1p. Eur. J. Cell Biol. 80:126-138.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 126-138
    • Yang, X.1    Purdue, P.E.2    Lazarow, P.B.3
  • 81
    • 0030071815 scopus 로고    scopus 로고
    • PEB1 (PAS7) is an intraperoxisomal receptor for the NH2-terminal, type 2, peroxisomal targeting sequence of thiolase: Peb1p itself is targeted to peroxisomes by an NH2-terminal peptide
    • Zhang, J. W., and P. B. Lazarow. 1996. PEB1 (PAS7) is an intraperoxisomal receptor for the NH2-terminal, type 2, peroxisomal targeting sequence of thiolase: Peb1p itself is targeted to peroxisomes by an NH2-terminal peptide. J. Cell Biol. 132:325-334.
    • (1996) J. Cell Biol. , vol.132 , pp. 325-334
    • Zhang, J.W.1    Lazarow, P.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.