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Volumn 10, Issue 1, 2014, Pages

PEX5 and Ubiquitin Dynamics on Mammalian Peroxisome Membranes

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CYTOLOGY; MAMMALS; PROTEINS; STOCHASTIC MODELS; STOCHASTIC SYSTEMS;

EID: 84896728961     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003426     Document Type: Article
Times cited : (16)

References (66)
  • 1
    • 41149158491 scopus 로고    scopus 로고
    • The peroxisome: still a mysterious organelle
    • Schrader M, Fahimi HD, (2008) The peroxisome: still a mysterious organelle. Histochem Cell Biol 129: 421-440.
    • (2008) Histochem Cell Biol , vol.129 , pp. 421-440
    • Schrader, M.1    Fahimi, H.D.2
  • 2
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders RJA, Waterham HR, (2006) Biochemistry of mammalian peroxisomes revisited. Annu Rev Biochem 75: 295-332.
    • (2006) Annu Rev Biochem , vol.75 , pp. 295-332
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 3
    • 84864029381 scopus 로고    scopus 로고
    • Genetics and molecular basis of human peroxisome biogenesis disorders
    • Waterham HR, Ebberink MS, (2012) Genetics and molecular basis of human peroxisome biogenesis disorders. Biochim Biophys Acta 1822: 1430-1441.
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 1430-1441
    • Waterham, H.R.1    Ebberink, M.S.2
  • 5
    • 0013854955 scopus 로고
    • Nature of the hepatomegalic effect produced by ethylchlorophenoxy-isobutyrate in the rat
    • Hess R, Staubli W, Riess W, (1965) Nature of the hepatomegalic effect produced by ethylchlorophenoxy-isobutyrate in the rat. Nature 208: 856-858.
    • (1965) Nature , vol.208 , pp. 856-858
    • Hess, R.1    Staubli, W.2    Riess, W.3
  • 6
    • 0017174403 scopus 로고
    • Morphometric analysis of the ultrastructural changes in rat liver induced by the peroxisome proliferator SaH 42-348
    • Moody DE, Reddy JK, (1976) Morphometric analysis of the ultrastructural changes in rat liver induced by the peroxisome proliferator SaH 42-348. J Cell Biol 71: 768-780.
    • (1976) J Cell Biol , vol.71 , pp. 768-780
    • Moody, D.E.1    Reddy, J.K.2
  • 7
    • 33645221489 scopus 로고    scopus 로고
    • Excess peroxisomes are degraded by autophagic machinery in mammals
    • Iwata J, Ezaki J, Komatsu M, Yokota S, Ueno T, et al. (2006) Excess peroxisomes are degraded by autophagic machinery in mammals. J Biol Chem 281: 4035-4041.
    • (2006) J Biol Chem , vol.281 , pp. 4035-4041
    • Iwata, J.1    Ezaki, J.2    Komatsu, M.3    Yokota, S.4    Ueno, T.5
  • 8
    • 0020772844 scopus 로고
    • Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes
    • Veenhuis M, Douma A, Harder W, Osumi M, (1983) Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes. Arch Microbiol 134: 193-203.
    • (1983) Arch Microbiol , vol.134 , pp. 193-203
    • Veenhuis, M.1    Douma, A.2    Harder, W.3    Osumi, M.4
  • 9
    • 84884536709 scopus 로고    scopus 로고
    • Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives
    • Nordgren M, Wang B, Apanasets O, Fransen M, (2013) Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives. Front Physiol 4: 145.
    • (2013) Front Physiol , vol.4 , pp. 145
    • Nordgren, M.1    Wang, B.2    Apanasets, O.3    Fransen, M.4
  • 10
    • 84859741506 scopus 로고    scopus 로고
    • Pexophagy: the selective degradation of peroxisomes
    • Article ID 512721
    • Till A, Lakhani R, Burnett SF, Subramani S, (2012) Pexophagy: the selective degradation of peroxisomes. Intl J Cell Biol 2012: Article ID 512721.
    • (2012) Intl J Cell Biol , vol.2012
    • Till, A.1    Lakhani, R.2    Burnett, S.F.3    Subramani, S.4
  • 11
    • 0038558137 scopus 로고    scopus 로고
    • Degradation of normal and proliferated peroxisomes in rat hepatocytes: regulation of peroxisomes quantity in cells
    • Yokota S, (2003) Degradation of normal and proliferated peroxisomes in rat hepatocytes: regulation of peroxisomes quantity in cells. Micosc Res Tech 61: 151-160.
    • (2003) Micosc Res Tech , vol.61 , pp. 151-160
    • Yokota, S.1
  • 12
  • 14
    • 84865279926 scopus 로고    scopus 로고
    • Recent advances in peroxisomal matrix protein import
    • Liu X, Ma C, Subramani S, (2012) Recent advances in peroxisomal matrix protein import. Curr Opin Cell Biol 24: 484-489.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 484-489
    • Liu, X.1    Ma, C.2    Subramani, S.3
  • 15
    • 84870936161 scopus 로고    scopus 로고
    • Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101
    • Natsuyama R, Okumoto K, Fujiki Y, (2013) Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101. Biochem J 449: 195-207.
    • (2013) Biochem J , vol.449 , pp. 195-207
    • Natsuyama, R.1    Okumoto, K.2    Fujiki, Y.3
  • 16
    • 69949152541 scopus 로고    scopus 로고
    • Solution structure of human Pex5·Pex14·PTS1 protein complexes obtained by small angle X-ray scattering
    • Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI, (2009) Solution structure of human Pex5·Pex14·PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284: 25334-25342.
    • (2009) J Biol Chem , vol.284 , pp. 25334-25342
    • Shiozawa, K.1    Konarev, P.V.2    Neufeld, C.3    Wilmanns, M.4    Svergun, D.I.5
  • 17
    • 16244407724 scopus 로고    scopus 로고
    • Identification of a novel, intraperoxisomal Pex14-binding site in Pex13: Association of Pex13 with the docking complex is essential for peroxisomal matrix protein import
    • Schell-Steven A, Stein K, Amoros M, Landgraf C, Volkmer-Engert R, et al. (2005) Identification of a novel, intraperoxisomal Pex14-binding site in Pex13: Association of Pex13 with the docking complex is essential for peroxisomal matrix protein import. Mol Cell Biol 25: 3007-3018.
    • (2005) Mol Cell Biol , vol.25 , pp. 3007-3018
    • Schell-Steven, A.1    Stein, K.2    Amoros, M.3    Landgraf, C.4    Volkmer-Engert, R.5
  • 18
    • 77649267086 scopus 로고    scopus 로고
    • The peroxisomal importomer constitutes a large and highly dynamic pore
    • Meinecke M, Cizmowski C, Schliebs W, Kruger V, Beck S, et al. (2010) The peroxisomal importomer constitutes a large and highly dynamic pore. Nat Cell Biol 12: 273-277.
    • (2010) Nat Cell Biol , vol.12 , pp. 273-277
    • Meinecke, M.1    Cizmowski, C.2    Schliebs, W.3    Kruger, V.4    Beck, S.5
  • 19
    • 9444290733 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal import receptor Pex5p
    • Platta HW, Girzalsky W, Erdmann R, (2004) Ubiquitination of the peroxisomal import receptor Pex5p. Biochem J 384: 37-45.
    • (2004) Biochem J , vol.384 , pp. 37-45
    • Platta, H.W.1    Girzalsky, W.2    Erdmann, R.3
  • 20
    • 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 H, Kunau W, (2005) 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 280: 1921-1930.
    • (2005) J Biol Chem , vol.280 , pp. 1921-1930
    • Kiel, J.A.K.W.1    Emmrich, K.2    Meyer, H.3    Kunau, W.4
  • 21
    • 27744523622 scopus 로고    scopus 로고
    • Peroxisomal matrix protein import: the transient pore model
    • Erdmann R, Schliebs W, (2005) Peroxisomal matrix protein import: the transient pore model. Nat Rev Mol Cell Biol 6: 738-742.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 738-742
    • Erdmann, R.1    Schliebs, W.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, (2007) A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p. J Biol Chem 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
    • 34247487864 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling
    • Platta HW, el Magraoui F, Schlee D, Grunau S, Girzalsky W, et al. (2007) Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling. J Cell Biol 177: 197-204.
    • (2007) J Cell Biol , vol.177 , pp. 197-204
    • Platta, H.W.1    el Magraoui, F.2    Schlee, D.3    Grunau, S.4    Girzalsky, W.5
  • 25
    • 84859762823 scopus 로고    scopus 로고
    • Identification of ubiquitin-specific protease 9X (Usp9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate
    • Grou CP, Francisco T, Rodrigues TA, Freitas MO, Pinto MP, et al. (2012) Identification of ubiquitin-specific protease 9X (Usp9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate. J Biol Chem 287: 12815-12827.
    • (2012) J Biol Chem , vol.287 , pp. 12815-12827
    • Grou, C.P.1    Francisco, T.2    Rodrigues, T.A.3    Freitas, M.O.4    Pinto, M.P.5
  • 26
    • 70350450553 scopus 로고    scopus 로고
    • Mapping the cargo protein membrane translocation step into the PEX5 cycling pathway
    • Alencastre IS, Rodrigues TA, Grou CP, Fransen M, Sá-Miranda C, et al. (2009) Mapping the cargo protein membrane translocation step into the PEX5 cycling pathway. J Biol Chem 284: 27243-27251.
    • (2009) J Biol Chem , vol.284 , pp. 27243-27251
    • Alencastre, I.S.1    Rodrigues, T.A.2    Grou, C.P.3    Fransen, M.4    Sá-Miranda, C.5
  • 27
    • 59149083150 scopus 로고    scopus 로고
    • The peroxisomal protein import machinery - a case report of transient ubiquitination with a new flavor
    • Grou CP, Carvalho AF, Pinto MP, Alencastre IS, Rodrigues TA, et al. (2009) The peroxisomal protein import machinery - a case report of transient ubiquitination with a new flavor. Cell Mol Life Sci 66: 254-262.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 254-262
    • Grou, C.P.1    Carvalho, A.F.2    Pinto, M.P.3    Alencastre, I.S.4    Rodrigues, T.A.5
  • 28
    • 78649403829 scopus 로고    scopus 로고
    • Peroxisomal protein import and ERAD: variations on a common theme
    • Schliebs W, Girzalsky W, Erdmann R, (2010) Peroxisomal protein import and ERAD: variations on a common theme. Nat Rev Mol Cell Biol 11: 885-890.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 885-890
    • Schliebs, W.1    Girzalsky, W.2    Erdmann, R.3
  • 29
    • 84876684927 scopus 로고    scopus 로고
    • The exportomer: the peroxisomal receptor export machinery
    • Platta HW, Hagen S, Erdmann R, (2013) The exportomer: the peroxisomal receptor export machinery. Cell Mol Life Sci 70: 1393-1411.
    • (2013) Cell Mol Life Sci , vol.70 , pp. 1393-1411
    • Platta, H.W.1    Hagen, S.2    Erdmann, R.3
  • 31
    • 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, (2005) Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export. Mol Cell Biol 25: 10822-10832.
    • (2005) Mol Cell Biol , vol.25 , pp. 10822-10832
    • Miyata, N.1    Fujiki, Y.2
  • 32
    • 33845336503 scopus 로고    scopus 로고
    • Pex14p, more than just a docking protein
    • Azevedo JE, Schliebs W, (2006) Pex14p, more than just a docking protein. Biochim Biophys Acta 1763: 1574-1584.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1574-1584
    • Azevedo, J.E.1    Schliebs, W.2
  • 33
    • 84855195598 scopus 로고    scopus 로고
    • New insights into dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p in shuttling of PTS1-receptor Pex5p during peroxisome biogenesis
    • Fujiki Y, Nashiro C, Miyata N, Tamura S, Okumoto K, (2012) New insights into dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p in shuttling of PTS1-receptor Pex5p during peroxisome biogenesis. Biochim Biophys Acta 1823: 145-149.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 145-149
    • Fujiki, Y.1    Nashiro, C.2    Miyata, N.3    Tamura, S.4    Okumoto, K.5
  • 34
    • 67349090991 scopus 로고    scopus 로고
    • In vitro import of peroxisome-targeting signal type 2 (PTS2) receptor Pex7p into peroxisomes
    • Miyata N, Hosoi K, Mukai S, Fujiki Y, (2009) In vitro import of peroxisome-targeting signal type 2 (PTS2) receptor Pex7p into peroxisomes. Biochim Biophys Acta 1793: 860-870.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 860-870
    • Miyata, N.1    Hosoi, K.2    Mukai, S.3    Fujiki, Y.4
  • 35
    • 83355169741 scopus 로고    scopus 로고
    • Cysteine-dependent ubiquitination of Pex18p is linked to cargo translocation across the peroxisomal membrane
    • Hensel A, Beck S, el Magraoui F, Platta HW, Girzalsky W, et al. (2011) Cysteine-dependent ubiquitination of Pex18p is linked to cargo translocation across the peroxisomal membrane. J Biol Chem 286: 43495-43505.
    • (2011) J Biol Chem , vol.286 , pp. 43495-43505
    • Hensel, A.1    Beck, S.2    el Magraoui, F.3    Platta, H.W.4    Girzalsky, W.5
  • 36
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • Gillespie DT, (1977) Exact stochastic simulation of coupled chemical reactions. J Phys Chem 81: 2340-2361.
    • (1977) J Phys Chem , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 38
    • 33746720114 scopus 로고    scopus 로고
    • Functional association of the AAA complex and the peroxisomal importomer
    • Rosenkranz K, Birschmann I, Grunau S, Girzalsky W, Kunau W, et al. (2006) Functional association of the AAA complex and the peroxisomal importomer. FEBS J 273: 3804-3815.
    • (2006) FEBS J , vol.273 , pp. 3804-3815
    • Rosenkranz, K.1    Birschmann, I.2    Grunau, S.3    Girzalsky, W.4    Kunau, W.5
  • 39
    • 47249159844 scopus 로고    scopus 로고
    • Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor
    • Grou CP, Carvalho AF, Pinto MP, Wiese S, Piechura H, et al. (2008) Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor. J Biol Chem 283: 14190-14197.
    • (2008) J Biol Chem , vol.283 , pp. 14190-14197
    • Grou, C.P.1    Carvalho, A.F.2    Pinto, M.P.3    Wiese, S.4    Piechura, H.5
  • 40
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • Berg HC, Purcell EM, (1977) Physics of chemoreception. Biophy J 20: 193-219.
    • (1977) Biophy J , vol.20 , pp. 193-219
    • Berg, H.C.1    Purcell, E.M.2
  • 43
    • 81755181731 scopus 로고    scopus 로고
    • PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14
    • Freitas MO, Francisco T, Rodrigues TA, Alencastre IS, Pinto MP, et al. (2011) PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14. J Biol Chem 286: 40509-40519.
    • (2011) J Biol Chem , vol.286 , pp. 40509-40519
    • Freitas, M.O.1    Francisco, T.2    Rodrigues, T.A.3    Alencastre, I.S.4    Pinto, M.P.5
  • 44
    • 0028607435 scopus 로고
    • Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
    • Scheffner M, Huibregtse JM, Howley PM, (1994) Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc Natl Acad Sci USA 91: 8797-8801.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8797-8801
    • Scheffner, M.1    Huibregtse, J.M.2    Howley, P.M.3
  • 45
    • 0029588670 scopus 로고
    • Identification of a family of closely related human ubiquitin conjugating enzymes
    • Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM, (1995) Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem 270: 30408-30414.
    • (1995) J Biol Chem , vol.270 , pp. 30408-30414
    • Jensen, J.P.1    Bates, P.W.2    Yang, M.3    Vierstra, R.D.4    Weissman, A.M.5
  • 46
    • 49349089823 scopus 로고    scopus 로고
    • The unique N terminus of the UbcH10 E2 enzyme controls the threshold for the APC activation and enhances checkpoint regulation of the APC
    • Summers MK, Pan B, Mukhyala K, Jackson PK, (2008) The unique N terminus of the UbcH10 E2 enzyme controls the threshold for the APC activation and enhances checkpoint regulation of the APC. Mol Cell 31: 544-556.
    • (2008) Mol Cell , vol.31 , pp. 544-556
    • Summers, M.K.1    Pan, B.2    Mukhyala, K.3    Jackson, P.K.4
  • 47
    • 0242334251 scopus 로고    scopus 로고
    • Lateral diffusion of membrane lipid-anchored probes before and after aggregation of cell surface IgE-receptors
    • Pyenta PS, Schwille P, Webb WW, Holowka D, Baird B, (2003) Lateral diffusion of membrane lipid-anchored probes before and after aggregation of cell surface IgE-receptors. J Phys Chem A 107: 8310-8318.
    • (2003) J Phys Chem A , vol.107 , pp. 8310-8318
    • Pyenta, P.S.1    Schwille, P.2    Webb, W.W.3    Holowka, D.4    Baird, B.5
  • 48
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • Valdez-Taubas J, Pelham HRB, (2003) Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr Biol 13: 1636-1640.
    • (2003) Curr Biol , vol.13 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.B.2
  • 49
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity
    • Marco E, Wedlich-Soldner R, Li R, Altschuler SJ, Wu LF, (2007) Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell 129: 411-422.
    • (2007) Cell , vol.129 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 50
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    • Erickson HP, (2009) Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol Proced Online 11: 32-51.
    • (2009) Biol Proced Online , vol.11 , pp. 32-51
    • Erickson, H.P.1
  • 51
    • 84055190883 scopus 로고    scopus 로고
    • Peroxisome degradation in mammals
    • Ezaki J, Kominami E, Ueno T, (2011) Peroxisome degradation in mammals. IUBMB Life 63: 1001-1008.
    • (2011) IUBMB Life , vol.63 , pp. 1001-1008
    • Ezaki, J.1    Kominami, E.2    Ueno, T.3
  • 53
    • 0028817372 scopus 로고
    • Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders
    • Dodt G, Braverman N, Wong C, Moser A, Moser HW, et al. (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
  • 55
    • 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, (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
  • 56
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
    • Lazarou M, Jin SM, Kane LA, Youle RJ, (2012) Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev Cell 22: 320-333.
    • (2012) Dev Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 57
    • 55149097659 scopus 로고    scopus 로고
    • The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes
    • Hara-Kuge S, Fujiki Y, (2008) The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes. Exp Cell Res 314: 3531-3541.
    • (2008) Exp Cell Res , vol.314 , pp. 3531-3541
    • Hara-Kuge, S.1    Fujiki, Y.2
  • 58
    • 0034802710 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mouse liver response to the peroxisome proliferator diethylhexylphthalate (DEHP)
    • Macdonald N, Chevalier S, Tonge R, Davison M, Rowlinson R, et al. (2001) Quantitative proteomic analysis of mouse liver response to the peroxisome proliferator diethylhexylphthalate (DEHP). Arch Toxicol 75: 415-424.
    • (2001) Arch Toxicol , vol.75 , pp. 415-424
    • Macdonald, N.1    Chevalier, S.2    Tonge, R.3    Davison, M.4    Rowlinson, R.5
  • 59
    • 78349283454 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha target genes
    • Rakhshandehroo M, Knoch B, Müller M, Kersten S, (2010) Peroxisome proliferator-activated receptor alpha target genes. PPAR Research 2010: 612089.
    • (2010) PPAR Research , vol.2010 , pp. 612089
    • Rakhshandehroo, M.1    Knoch, B.2    Müller, M.3    Kersten, S.4
  • 60
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • Matsumoto N, Tamura S, Fujiki Y, (2003) The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes. Nat Cell Biol 5: 454-460.
    • (2003) Nat Cell Biol , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 61
    • 78349298325 scopus 로고    scopus 로고
    • Gene expression profiling in wildtype and and PPARα-null mice exposed to perfluorooctane sulfonate reveals PPARα-independent effects
    • Rosen MB, Schmid JR, Corton JC, Zehr RD, Das KP, et al. (2010) Gene expression profiling in wildtype and and PPARα-null mice exposed to perfluorooctane sulfonate reveals PPARα-independent effects. PPAR Res 2010: 794739.
    • (2010) PPAR Res , vol.2010 , pp. 794739
    • Rosen, M.B.1    Schmid, J.R.2    Corton, J.C.3    Zehr, R.D.4    Das, K.P.5
  • 62
    • 39449102122 scopus 로고    scopus 로고
    • The AAA peroxins Pex1p and Pex6p function as dislocases for the ubiquitinated peroxisomal import receptor Pex5p
    • Platta HW, Debelyy MO, Magraoui FE, Erdmann R, (2008) The AAA peroxins Pex1p and Pex6p function as dislocases for the ubiquitinated peroxisomal import receptor Pex5p. Biochem Soc Trans 36: 99-104.
    • (2008) Biochem Soc Trans , vol.36 , pp. 99-104
    • Platta, H.W.1    Debelyy, M.O.2    Magraoui, F.E.3    Erdmann, R.4
  • 63
    • 83255185006 scopus 로고    scopus 로고
    • AWP1/ZFAND6 functions in Pex5 export by interacting with cys-monoubiquitinated Pex5 and Pex6 AAA ATPase
    • Miyata N, Okumoto K, Mukai S, Noguchi M, Fujiki Y, (2012) AWP1/ZFAND6 functions in Pex5 export by interacting with cys-monoubiquitinated Pex5 and Pex6 AAA ATPase. Traffic 13: 168-183.
    • (2012) Traffic , vol.13 , pp. 168-183
    • Miyata, N.1    Okumoto, K.2    Mukai, S.3    Noguchi, M.4    Fujiki, Y.5
  • 64
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: ubiquitin-mediated recognition and beyond
    • Kraft C, Peter M, Hofmann K, (2010) Selective autophagy: ubiquitin-mediated recognition and beyond. Nat Cell Biol 12: 836-841.
    • (2010) Nat Cell Biol , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 65
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley AM, Nuttall JM, Hettema EH, (2012) Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J 31: 2852-2868.
    • (2012) EMBO J , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 66
    • 84882641004 scopus 로고    scopus 로고
    • Pexophagy-linked degradation of the peroxisomal membrane protein Pex3p involves the ubiquitin-proteasome system
    • Williams C, van der Klei IJ, (2013) Pexophagy-linked degradation of the peroxisomal membrane protein Pex3p involves the ubiquitin-proteasome system. Biochem Biophys Res Commun 438: 395-401.
    • (2013) Biochem Biophys Res Commun , vol.438 , pp. 395-401
    • Williams, C.1    van der Klei, I.J.2


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