메뉴 건너뛰기




Volumn 12, Issue 8, 2011, Pages 1067-1083

Cysteine ubiquitination of PTS1 receptor Pex5p regulates Pex5p recycling

Author keywords

CHO cell mutant; Dominant negative mutant; Peroxin; Peroxisome biogenesis; Peroxisome targeting signal; Pex5p; Protein import; PTS1 receptor; Ubiquitination

Indexed keywords

ALANINE; CYSTEINE; CYTOSOL RECEPTOR; DITHIOTHREITOL; PEROXISOME TARGETING SIGNAL TYPE 1 PROTEIN; PEROXISOME TARGETING SIGNAL TYPE 2 PROTEIN; PEX5P RECEPTOR; PROTEIN; UNCLASSIFIED DRUG;

EID: 79960172953     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2011.01217.x     Document Type: Article
Times cited : (93)

References (51)
  • 1
    • 0028817372 scopus 로고
    • Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders.
    • Dodt G, Braverman N, Wong CS, Moser A, Moser HW, Watkins P, Valle D, Gould SJ. Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders. Nat Genet 1995;9:115-125.
    • (1995) Nat Genet , vol.9 , pp. 115-125
    • Dodt, G.1    Braverman, N.2    Wong, C.S.3    Moser, A.4    Moser, H.W.5    Watkins, P.6    Valle, D.7    Gould, S.J.8
  • 3
    • 0030946632 scopus 로고    scopus 로고
    • Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata.
    • Braverman N, Steel G, Obie C, Moser A, Moser H, Gould SJ, Valle D. Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata. Nat Genet 1997;15:369-376.
    • (1997) Nat Genet , vol.15 , pp. 369-376
    • Braverman, N.1    Steel, G.2    Obie, C.3    Moser, A.4    Moser, H.5    Gould, S.J.6    Valle, D.7
  • 5
    • 1842335689 scopus 로고    scopus 로고
    • Rhizomelic chondrodysplasia punctata is caused by deficiency of human PEX7, a homologue of the yeast PTS2 receptor.
    • Purdue PE, Zhang JW, Skoneczny M, Lazarow PB. Rhizomelic chondrodysplasia punctata is caused by deficiency of human PEX7, a homologue of the yeast PTS2 receptor. Nat Genet 1997;15:381-384.
    • (1997) Nat Genet , vol.15 , pp. 381-384
    • Purdue, P.E.1    Zhang, J.W.2    Skoneczny, M.3    Lazarow, P.B.4
  • 6
    • 0037088664 scopus 로고    scopus 로고
    • Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells.
    • Mukai S, Ghaedi K, Fujiki Y. Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells. J Biol Chem 2002;277:9548-9561.
    • (2002) J Biol Chem , vol.277 , pp. 9548-9561
    • Mukai, S.1    Ghaedi, K.2    Fujiki, Y.3
  • 7
    • 34249908934 scopus 로고    scopus 로고
    • The peroxisomal protein import machinery.
    • Platta HW, Erdmann R. The peroxisomal protein import machinery. FEBS Lett 2007;581:2811-2819.
    • (2007) FEBS Lett , vol.581 , pp. 2811-2819
    • Platta, H.W.1    Erdmann, R.2
  • 9
    • 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 2001;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
  • 10
    • 0034647937 scopus 로고    scopus 로고
    • The mammalian peroxin Pex5pL, the longer isoform of the mobile PTS1-transporter, translocates 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 PTS1-transporter, translocates Pex7p-PTS2 protein complex into peroxisomes via its initial docking site, Pex14p. J Biol Chem 2000;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
  • 11
    • 0034647529 scopus 로고    scopus 로고
    • Disruption of interaction of the longer isoform of Pex5p, Pex5pL, with Pex7p abolishes the PTS2 protein import in mammals: study with a novel PEX5-impaired Chinese hamster ovary cell mutant.
    • Matsumura T, Otera H, Fujiki Y. Disruption of interaction of the longer isoform of Pex5p, Pex5pL, with Pex7p abolishes the PTS2 protein import in mammals: study with a novel PEX5-impaired Chinese hamster ovary cell mutant. J Biol Chem 2000;275:21715-21721.
    • (2000) J Biol Chem , vol.275 , pp. 21715-21721
    • Matsumura, T.1    Otera, H.2    Fujiki, Y.3
  • 12
    • 33845982949 scopus 로고    scopus 로고
    • Molecular mechanisms of import of peroxisome-targeting signal type 2 (PTS2) proteins by PTS2 receptor Pex7p and PTS1 receptor Pex5pL.
    • Mukai S, Fujiki Y. Molecular mechanisms of import of peroxisome-targeting signal type 2 (PTS2) proteins by PTS2 receptor Pex7p and PTS1 receptor Pex5pL. J Biol Chem 2006;281:37311-37320.
    • (2006) J Biol Chem , vol.281 , pp. 37311-37320
    • Mukai, S.1    Fujiki, Y.2
  • 13
    • 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, 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 WXXXF/Y motifs are critical for matrix protein import. Mol Cell Biol 2002;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
  • 16
    • 28544451220 scopus 로고    scopus 로고
    • Shuttling mechanism of peroxisome targeting signal type 1 receptor, Pex5: ATP-independent import and ATP-dependent export.
    • Miyata N, Fujiki Y. Shuttling mechanism of peroxisome targeting signal type 1 receptor, Pex5: ATP-independent import and ATP-dependent export. Mol Cell Biol 2005;25:10822-10832.
    • (2005) Mol Cell Biol , vol.25 , pp. 10822-10832
    • Miyata, N.1    Fujiki, Y.2
  • 17
    • 23144446970 scopus 로고    scopus 로고
    • Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol.
    • Platta HW, Grunau S, Rosenkranz K, Girzalsky W, Erdmann R. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat Cell Biol 2005;7:817-822.
    • (2005) Nat Cell Biol , vol.7 , pp. 817-822
    • Platta, H.W.1    Grunau, S.2    Rosenkranz, K.3    Girzalsky, W.4    Erdmann, R.5
  • 21
    • 0031586033 scopus 로고    scopus 로고
    • Isolation and characterization of peroxisome-deficient Chinese hamster ovary cell mutants representing human complementation group III.
    • Okumoto K, Bogaki A, Tateishi K, Tsukamoto T, Osumi T, Shimozawa N, Suzuki Y, Orii T, Fujiki Y. Isolation and characterization of peroxisome-deficient Chinese hamster ovary cell mutants representing human complementation group III. Exp Cell Res 1997;233:11-20.
    • (1997) Exp Cell Res , vol.233 , pp. 11-20
    • Okumoto, K.1    Bogaki, A.2    Tateishi, K.3    Tsukamoto, T.4    Osumi, T.5    Shimozawa, N.6    Suzuki, Y.7    Orii, T.8    Fujiki, Y.9
  • 22
    • 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, Gould SJ. 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 1996;135:1763-1774.
    • (1996) J Cell Biol , vol.135 , pp. 1763-1774
    • Dodt, G.1    Gould, S.J.2
  • 23
    • 34547957271 scopus 로고    scopus 로고
    • A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p.
    • Williams C, van den Berg M, Sprenger RR, Distel B. A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p. J Biol Chem 2007;282:22534-22543.
    • (2007) J Biol Chem , vol.282 , pp. 22534-22543
    • Williams, C.1    van den Berg, M.2    Sprenger, R.R.3    Distel, B.4
  • 24
    • 0024528893 scopus 로고
    • Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus.
    • Miyazawa S, Osumi T, Hashimoto T, Ohno K, Miura S, Fujiki Y. Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus. Mol Cell Biol 1989;9:83-91.
    • (1989) Mol Cell Biol , vol.9 , pp. 83-91
    • Miyazawa, S.1    Osumi, T.2    Hashimoto, T.3    Ohno, K.4    Miura, S.5    Fujiki, Y.6
  • 25
    • 0023655257 scopus 로고
    • Structural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase.
    • Hijikata M, Ishii N, Kagamiyama H, Osumi T, Hashimoto T. Structural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase. J Biol Chem 1987;262:8151-8158.
    • (1987) J Biol Chem , vol.262 , pp. 8151-8158
    • Hijikata, M.1    Ishii, N.2    Kagamiyama, H.3    Osumi, T.4    Hashimoto, T.5
  • 26
    • 0031862579 scopus 로고    scopus 로고
    • PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p.
    • Okumoto K, Shimozawa N, Kawai A, Tamura S, Tsukamoto T, Osumi T, Moser H, Wanders RJA, Suzuki Y, Kondo N, Fujiki Y. PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p. Mol Cell Biol 1998;18:4324-4336.
    • (1998) Mol Cell Biol , vol.18 , pp. 4324-4336
    • Okumoto, K.1    Shimozawa, N.2    Kawai, A.3    Tamura, S.4    Tsukamoto, T.5    Osumi, T.6    Moser, H.7    Wanders, R.J.A.8    Suzuki, Y.9    Kondo, N.10    Fujiki, Y.11
  • 27
    • 0028916868 scopus 로고
    • Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor.
    • Fransen M, Brees C, Baumgart E, Vanhooren JC, Baes M, Mannaerts GP, Veldhoven PPV. Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor. J Biol Chem 1995;270:7731-7736.
    • (1995) J Biol Chem , vol.270 , pp. 7731-7736
    • Fransen, M.1    Brees, C.2    Baumgart, E.3    Vanhooren, J.C.4    Baes, M.5    Mannaerts, G.P.6    Veldhoven, P.P.V.7
  • 30
    • 1842853027 scopus 로고    scopus 로고
    • Peroxisome biogenesis and the role of protein import.
    • Brown LA, Baker A. Peroxisome biogenesis and the role of protein import. J Cell Mol Med 2003;7:388-400.
    • (2003) J Cell Mol Med , vol.7 , pp. 388-400
    • Brown, L.A.1    Baker, A.2
  • 33
    • 34147175418 scopus 로고    scopus 로고
    • A conserved cysteine residue of Pichia pastoris Pex20p is essential for its recycling from the peroxisome to the cytosol.
    • Léon S, Subramani S. A conserved cysteine residue of Pichia pastoris Pex20p is essential for its recycling from the peroxisome to the cytosol. J Biol Chem 2007;282:7424-7430.
    • (2007) J Biol Chem , vol.282 , pp. 7424-7430
    • Léon, S.1    Subramani, S.2
  • 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 CS, Kalish JE, Morrell JC, McCaffery JM, Gould SJ. The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import. Mol Cell Biol 2000;20:7516-7526.
    • (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
  • 37
    • 12544259938 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import.
    • Kiel JAKW, Emmrich K, Meyer HE, Kunau W-H. Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import. J Biol Chem 2005;280:1921-1930.
    • (2005) J Biol Chem , vol.280 , pp. 1921-1930
    • Kiel, J.A.K.W.1    Emmrich, K.2    Meyer, H.E.3    Kunau, W.-H.4
  • 38
    • 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 WB, Faber KN, Wenzel TJ, Rangell L, Keller GA, 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 1999;146:99-112.
    • (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
  • 39
    • 1242274571 scopus 로고    scopus 로고
    • An Arabidopsis indole-3-butyric acid-response mutant defective in PEROXIN6, an apparent ATPase implicated in peroxisomal function.
    • Zolman BK, Bartel B. An Arabidopsis indole-3-butyric acid-response mutant defective in PEROXIN6, an apparent ATPase implicated in peroxisomal function. Proc Natl Acad Sci U S A 2004;101:1786-1791.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1786-1791
    • Zolman, B.K.1    Bartel, B.2
  • 40
    • 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, Itoh R, Hirono Y, Otera H, Ghaedi K, Tateishi K, Tamura S, Okumoto K, Harano T, Mukai S, Fujiki Y. The peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J Biol Chem 1999;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
  • 42
    • 33744519453 scopus 로고    scopus 로고
    • Functional domains and dynamic assembly of the peroxin Pex14p, the entry site of matrix proteins.
    • Itoh R, Fujiki Y. Functional domains and dynamic assembly of the peroxin Pex14p, the entry site of matrix proteins. J Biol Chem 2006;281:10196-10205.
    • (2006) J Biol Chem , vol.281 , pp. 10196-10205
    • Itoh, R.1    Fujiki, Y.2
  • 45
    • 0026492894 scopus 로고
    • Animal cell mutants represent two complementation groups of peroxisome-defective Zellweger syndrome.
    • Shimozawa N, Tsukamoto T, Suzuki Y, Orii T, Fujiki Y. Animal cell mutants represent two complementation groups of peroxisome-defective Zellweger syndrome. J Clin Invest 1992;90:1864-1870.
    • (1992) J Clin Invest , vol.90 , pp. 1864-1870
    • Shimozawa, N.1    Tsukamoto, T.2    Suzuki, Y.3    Orii, T.4    Fujiki, Y.5
  • 46
    • 0345861756 scopus 로고    scopus 로고
    • PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins.
    • Jones JM, Morrell JC, Gould SJ. PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J Cell Biol 2004;164:57-67.
    • (2004) J Cell Biol , vol.164 , pp. 57-67
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 47
    • 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 Y. 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 2000;275:25700-25710.
    • (2000) J Biol Chem , vol.275 , pp. 25700-25710
    • Okumoto, K.1    Abe, I.2    Fujiki, Y.3
  • 48
    • 0025342563 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes.
    • Tsukamoto T, Yokota S, Fujiki Y. Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes. J Cell Biol 1990;110:651-660.
    • (1990) J Cell Biol , vol.110 , pp. 651-660
    • Tsukamoto, T.1    Yokota, S.2    Fujiki, Y.3
  • 49
    • 0035951877 scopus 로고    scopus 로고
    • Biogenesis of nonspecific lipid transfer protein and sterol carrier protein x: studies using peroxisome assembly-defective pex cell mutants.
    • Otera H, Nishimura M, Setoguchi K, Mori T, Fujiki Y. Biogenesis of nonspecific lipid transfer protein and sterol carrier protein x: studies using peroxisome assembly-defective pex cell mutants. J Biol Chem 2001;276:2858-2864.
    • (2001) J Biol Chem , vol.276 , pp. 2858-2864
    • Otera, H.1    Nishimura, M.2    Setoguchi, K.3    Mori, T.4    Fujiki, Y.5
  • 50
    • 50849121067 scopus 로고    scopus 로고
    • Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: localization and transport of plasmalogens to post-Golgi compartments.
    • Honsho M, Yagita Y, Kinoshita N, Fujiki Y. Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: localization and transport of plasmalogens to post-Golgi compartments. Biochim Biophys Acta Mol Cell Res 2008;1783:1857-1865.
    • (2008) Biochim Biophys Acta Mol Cell Res , vol.1783 , pp. 1857-1865
    • Honsho, M.1    Yagita, Y.2    Kinoshita, N.3    Fujiki, Y.4
  • 51
    • 0032515992 scopus 로고    scopus 로고
    • Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I.
    • Tamura S, Okumoto K, Toyama R, Shimozawa N, Tsukamoto T, Suzuki Y, Osumi T, Kondo N, Fujiki Y. Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I. Proc Natl Acad Sci U S A 1998;95:4350-4355.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4350-4355
    • Tamura, S.1    Okumoto, K.2    Toyama, R.3    Shimozawa, N.4    Tsukamoto, T.5    Suzuki, Y.6    Osumi, T.7    Kondo, N.8    Fujiki, Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.