메뉴 건너뛰기
Journal of Cell Biology
Volumn 204, Issue 5, 2014, Pages 659-668
Preperoxisomal vesicles can form in the absence of Pex3
Author keywords

FM, fluorescence microscopy; Iem, immuno electron microscopy; PMP, peroxisomal membrane protein; WB, Western blot; WT, wild type
Indexed keywords

ALCOHOL; DOCKING PROTEIN; MATRIX PROTEIN; MEMBRANE PROTEIN; OXIDOREDUCTASE; PEROXIN;
EID: 84895750542     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201310148     Document Type: Article
Times cited : (69)
References (40)
  • 1
    • 79959370908 scopus 로고    scopus 로고
    • Cell-free sorting of peroxisomal membrane proteins from the endoplasmic reticulum
    • Agrawal, G., S. Joshi, and S. Subramani. 2011. Cell-free sorting of peroxisomal membrane proteins from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 108:9113-9118. http://dx.doi.org/10.1073/pnas.1018749108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 9113-9118
    • Agrawal, G.1    Joshi, S.2    Subramani, S.3
  • 3
    • 0030659441 scopus 로고    scopus 로고
    • Deviant Pex3p levels affect normal peroxisome formation in Hansenula polymorpha: high steady-state levels of the protein fully abolish matrix protein import
    • Baerends, R.J., F.A. Salomons, K.N. Faber, J.A. Kiel, I.J. Van der Klei, and M. Veenhuis. 1997. Deviant Pex3p levels affect normal peroxisome formation in Hansenula polymorpha: high steady-state levels of the protein fully abolish matrix protein import. Yeast. 13:1437-1448. http://dx.doi.org/10.1002/(SICI)1097-0061(199712)13:15<1437::AID-YEA192>3.0.CO;2-U
    • (1997) Yeast. , vol.13 , pp. 1437-1448
    • Baerends, R.J.1    Salomons, F.A.2    Faber, K.N.3    Kiel, J.A.4    Van der Klei, I.J.5    Veenhuis, M.6
  • 4
    • 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., K.N. Faber, A.M. Kram, J.A. Kiel, I.J. van der Klei, and M. Veenhuis. 2000. 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. http://dx.doi.org/10.1074/jbc.275.14.9986
    • (2000) J. Biol. Chem. , vol.275 , pp. 9986-9995
    • Baerends, R.J.1    Faber, K.N.2    Kram, A.M.3    Kiel, J.A.4    van der Klei, I.J.5    Veenhuis, M.6
  • 5
    • 0037044768 scopus 로고    scopus 로고
    • Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha
    • Bellu, A.R., F.A. Salomons, J.A. Kiel, M. Veenhuis, and I.J. Van Der Klei. 2002. Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 277:42875-42880. http://dx.doi.org/10.1074/jbc. M205437200
    • (2002) J. Biol. Chem. , vol.277 , pp. 42875-42880
    • Bellu, A.R.1    Salomons, F.A.2    Kiel, J.A.3    Veenhuis, M.4    Van Der Klei, I.J.5
  • 6
    • 79958767409 scopus 로고    scopus 로고
    • Peroxisome fission is associated with reorganization of specific membrane proteins
    • Cepinska, M.N., M. Veenhuis, I.J. van der Klei, and S. Nagotu. 2011. Peroxisome fission is associated with reorganization of specific membrane proteins. Traffic. 12:925-937. http://dx.doi.org/10.1111/j.1600-0854.2011.01198.x
    • (2011) Traffic. , vol.12 , pp. 925-937
    • Cepinska, M.N.1    Veenhuis, M.2    van der Klei, I.J.3    Nagotu, S.4
  • 7
    • 0028217090 scopus 로고
    • Highly-efficient electrotransformation of the yeast Hansenula polymorpha
    • Faber, K.N., P. Haima, W. Harder, M. Veenhuis, and G. Ab. 1994. Highly-efficient electrotransformation of the yeast Hansenula polymorpha. Curr. Genet. 25:305-310. http://dx.doi.org/10.1007/BF00351482
    • (1994) Curr. Genet. , vol.25 , pp. 305-310
    • Faber, K.N.1    Haima, P.2    Harder, W.3    Veenhuis, M.4    Ab, G.5
  • 8
    • 84964902417 scopus 로고    scopus 로고
    • Intra-ER sorting of the peroxisomal membrane protein Pex3 relies on its luminal domain
    • Fakieh, M.H., P.J. Drake, J. Lacey, J.M. Munck, A.M. Motley, and E.H. Hettema. 2013. Intra-ER sorting of the peroxisomal membrane protein Pex3 relies on its luminal domain. Biol. Open. 2:829-837. http://dx.doi.org/10.1242/bio.20134788
    • (2013) Biol. Open. , vol.2 , pp. 829-837
    • Fakieh, M.H.1    Drake, P.J.2    Lacey, J.3    Munck, J.M.4    Motley, A.M.5    Hettema, E.H.6
  • 9
    • 1642394134 scopus 로고    scopus 로고
    • PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
    • Fang, Y., J.C. Morrell, J.M. Jones, and S.J. Gould. 2004. PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins. J. Cell Biol. 164:863-875. http://dx.doi.org/10.1083/jcb.200311131
    • (2004) J. Cell Biol. , vol.164 , pp. 863-875
    • Fang, Y.1    Morrell, J.C.2    Jones, J.M.3    Gould, S.J.4
  • 10
    • 33645070532 scopus 로고    scopus 로고
    • Reassembly of peroxisomes in Hansenula polymorpha pex3 cells on reintroduction of Pex3p involves the nuclear envelope
    • Haan, G.J., R.J. Baerends, A.M. Krikken, M. Otzen, M. Veenhuis, and I.J. van der Klei. 2006. Reassembly of peroxisomes in Hansenula polymorpha pex3 cells on reintroduction of Pex3p involves the nuclear envelope. FEMS Yeast Res. 6:186-194. http://dx.doi.org/10.1111/j.1567-1364.2006.00037.x
    • (2006) FEMS Yeast Res. , vol.6 , pp. 186-194
    • Haan, G.J.1    Baerends, R.J.2    Krikken, A.M.3    Otzen, M.4    Veenhuis, M.5    van der Klei, I.J.6
  • 11
    • 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. http://dx.doi.org/10.1034/j.1600-0854.2002.30806.x
    • (2002) Traffic. , vol.3 , pp. 560-574
    • Hazra, P.P.1    Suriapranata, I.2    Snyder, W.B.3    Subramani, S.4
  • 12
    • 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. http://dx.doi.org/10.1093/emboj/19.2.223
    • (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
  • 14
    • 34548554581 scopus 로고    scopus 로고
    • A comparative study of peroxisomal structures in Hansenula polymorpha pex mutants
    • Koek, A., M. Komori, M. Veenhuis, and I.J. van der Klei. 2007. A comparative study of peroxisomal structures in Hansenula polymorpha pex mutants. FEMS Yeast Res. 7:1126-1133. http://dx.doi.org/10.1111/j.1567-1364.2007.00261.x
    • (2007) FEMS Yeast Res. , vol.7 , pp. 1126-1133
    • Koek, A.1    Komori, M.2    Veenhuis, M.3    van der Klei, I.J.4
  • 15
    • 84871820511 scopus 로고    scopus 로고
    • Lipid droplets and peroxisomes: key players in cellular lipid homeostasis or a matter of fat-store 'em up or burn 'em down
    • Kohlwein, S.D., M. Veenhuis, and I.J. van der Klei. 2013. Lipid droplets and peroxisomes: key players in cellular lipid homeostasis or a matter of fat-store 'em up or burn 'em down. Genetics. 193:1-50. http://dx.doi.org/10.1534/genetics.112.143362
    • (2013) Genetics. , vol.193 , pp. 1-50
    • Kohlwein, S.D.1    Veenhuis, M.2    van der Klei, I.J.3
  • 16
    • 0037371332 scopus 로고    scopus 로고
    • The Hansenula polymorpha PDD7 gene is essential for macropexophagy and microautophagy
    • Komduur, J.A., M. Veenhuis, and J.A. Kiel. 2003. The Hansenula polymorpha PDD7 gene is essential for macropexophagy and microautophagy. FEMS Yeast Res. 3:27-34.
    • (2003) FEMS Yeast Res. , vol.3 , pp. 27-34
    • Komduur, J.A.1    Veenhuis, M.2    Kiel, J.A.3
  • 17
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J.R., D.N. Mastronarde, and J.R. McIntosh. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116: 71-76. http://dx.doi.org/10.1006/jsbi.1996.0013
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 18
    • 78650729949 scopus 로고    scopus 로고
    • A vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum
    • Lam, S.K., N. Yoda, and R. Schekman. 2010. A vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 107:21523-21528. http://dx.doi.org/10.1073/pnas.1013397107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 21523-21528
    • Lam, S.K.1    Yoda, N.2    Schekman, R.3
  • 19
    • 69949102267 scopus 로고    scopus 로고
    • The peroxisomal matrix import of Pex8p requires only PTS receptors and Pex14p
    • Ma, C., U. Schumann, N. Rayapuram, and S. Subramani. 2009. The peroxisomal matrix import of Pex8p requires only PTS receptors and Pex14p. Mol. Biol. Cell. 20:3680-3689. http://dx.doi.org/10.1091/mbc. E09-01-0037
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 3680-3689
    • Ma, C.1    Schumann, U.2    Rayapuram, N.3    Subramani, S.4
  • 20
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D.N. 2005. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152:36-51. http://dx.doi.org/10.1016/j.jsb.2005.07.007
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 21
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley, A.M., E.H. Hettema. 2007. Yeast peroxisomes multiply by growth and division. J. Cell Biol. 178:399-410. http://dx.doi.org/10.1083/jcb.200702167
    • (2007) J. Cell Biol. , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 22
    • 41949118972 scopus 로고    scopus 로고
    • Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation
    • Nagotu, S., R. Saraya, M. Otzen, M. Veenhuis, and I.J. van der Klei. 2008. Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation. Biochim. Biophys. Acta. 1783:760-769. http://dx.doi.org/10.1016/j.bbamcr.2007.10.018
    • (2008) Biochim. Biophys. Acta. , vol.1783 , pp. 760-769
    • Nagotu, S.1    Saraya, R.2    Otzen, M.3    Veenhuis, M.4    van der Klei, I.J.5
  • 23
    • 79851510200 scopus 로고    scopus 로고
    • Protein import machineries of peroxisomes
    • Rucktäschel, R., W. Girzalsky, and R. Erdmann. 2011. Protein import machineries of peroxisomes. Biochim. Biophys. Acta. 1808:892-900. http://dx.doi.org/10.1016/j.bbamem.2010.07.020
    • (2011) Biochim. Biophys. Acta. , vol.1808 , pp. 892-900
    • Rucktäschel, R.1    Girzalsky, W.2    Erdmann, R.3
  • 24
    • 0029902286 scopus 로고    scopus 로고
    • The absence of Pmp47, a putative yeast peroxisomal transporter, causes a defect in transport and folding of a specific matrix enzyme
    • Sakai, Y., A. Saiganji, H. Yurimoto, K. Takabe, H. Saiki, and N. Kato. 1996. The absence of Pmp47, a putative yeast peroxisomal transporter, causes a defect in transport and folding of a specific matrix enzyme. J. Cell Biol. 134:37-51. http://dx.doi.org/10.1083/jcb.134.1.37
    • (1996) J. Cell Biol. , vol.134 , pp. 37-51
    • Sakai, Y.1    Saiganji, A.2    Yurimoto, H.3    Takabe, K.4    Saiki, H.5    Kato, N.6
  • 26
    • 79959462996 scopus 로고    scopus 로고
    • Peroxisome reintroduction in Hansenula polymorpha requires Pex25 and Rho1
    • Saraya, R., A.M. Krikken, M. Veenhuis, and I.J. van der Klei. 2011. Peroxisome reintroduction in Hansenula polymorpha requires Pex25 and Rho1. J. Cell Biol. 193:885-900. http://dx.doi.org/10.1083/jcb.201012083
    • (2011) J. Cell Biol. , vol.193 , pp. 885-900
    • Saraya, R.1    Krikken, A.M.2    Veenhuis, M.3    van der Klei, I.J.4
  • 27
    • 3042695949 scopus 로고    scopus 로고
    • Peroxisome membrane biogenesis: the stage is set
    • Schliebs, W., and W.H. Kunau. 2004. Peroxisome membrane biogenesis: the stage is set. Curr. Biol. 14:R397-R399. http://dx.doi.org/10.1016/j.cub.2004.05.017
    • (2004) Curr. Biol. , vol.14
    • Schliebs, W.1    Kunau, W.H.2
  • 28
    • 0034641604 scopus 로고    scopus 로고
    • Identification of PEX3 as the gene mutated in a Zellweger syndrome patient lacking peroxisomal remnant structures
    • Shimozawa, N., Y. Suzuki, Z. Zhang, A. Imamura, K. Ghaedi, Y. Fujiki, and N. Kondo. 2000. Identification of PEX3 as the gene mutated in a Zellweger syndrome patient lacking peroxisomal remnant structures. Hum. Mol. Genet. 9:1995-1999. http://dx.doi.org/10.1093/hmg/9.13.1995
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1995-1999
    • Shimozawa, N.1    Suzuki, Y.2    Zhang, Z.3    Imamura, A.4    Ghaedi, K.5    Fujiki, Y.6    Kondo, N.7
  • 29
    • 38449099776 scopus 로고    scopus 로고
    • Cryosectioning and immunolabeling
    • Slot, J.W., and H.J. Geuze. 2007. Cryosectioning and immunolabeling. Nat. Protoc. 2:2480-2491. http://dx.doi.org/10.1038/nprot.2007.365
    • (2007) Nat. Protoc. , vol.2 , pp. 2480-2491
    • Slot, J.W.1    Geuze, H.J.2
  • 30
    • 0034717704 scopus 로고    scopus 로고
    • Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis
    • South, S.T., K.A. Sacksteder, X. Li, Y. Liu, and S.J. Gould. 2000. Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis. J. Cell Biol. 149:1345-1360. http://dx.doi.org/10.1083/jcb.149.7.1345
    • (2000) J. Cell Biol. , vol.149 , pp. 1345-1360
    • South, S.T.1    Sacksteder, K.A.2    Li, X.3    Liu, Y.4    Gould, S.J.5
  • 32
    • 84878954796 scopus 로고    scopus 로고
    • Peroxisome formation and maintenance are dependent on the endoplasmic reticulum
    • Tabak, H.F., I. Braakman, and A. van der Zand. 2013. Peroxisome formation and maintenance are dependent on the endoplasmic reticulum. Annu. Rev. Biochem. 82:723-744. http://dx.doi.org/10.1146/annurev-biochem- 081111-125123
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 723-744
    • Tabak, H.F.1    Braakman, I.2    van der Zand, A.3
  • 33
    • 27144513797 scopus 로고    scopus 로고
    • Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation
    • Thoms, S., and R. Erdmann. 2005. Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation. FEBS J. 272:5169-5181. http://dx.doi.org/10.1111/j.1742-4658.2005.04939.x
    • (2005) FEBS J. , vol.272 , pp. 5169-5181
    • Thoms, S.1    Erdmann, R.2
  • 34
    • 77953507085 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins insert into the endoplasmic reticulum
    • van der Zand, A., I. Braakman, and H.F. Tabak. 2010. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol. Biol. Cell. 21:2057-2065. http://dx.doi.org/10.1091/mbc. E10-02-0082
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 2057-2065
    • van der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 35
    • 84859745968 scopus 로고    scopus 로고
    • Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes
    • van der Zand, A., J. Gent, I. Braakman, and H.F. Tabak. 2012. Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell. 149:397-409. http://dx.doi.org/10.1016/j.cell.2012.01.054
    • (2012) Cell. , vol.149 , pp. 397-409
    • van der Zand, A.1    Gent, J.2    Braakman, I.3    Tabak, H.F.4
  • 36
    • 0017151579 scopus 로고
    • Growth of Hansenula polymorpha in a methanol-limited chemostat
    • Van Dijken, J.P., R. Otto, and W. Harder. 1976. Growth of Hansenula polymorpha in a methanol-limited chemostat. Arch. Microbiol. 111:137-144. http://dx.doi.org/10.1007/BF00446560
    • (1976) Arch. Microbiol. , vol.111 , pp. 137-144
    • Van Dijken, J.P.1    Otto, R.2    Harder, W.3
  • 37
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders, R.J., and H.R. Waterham. 2006. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 75:295-332. http://dx.doi.org/10.1146/annurev.biochem.74.082803.133329
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 38
    • 0029744977 scopus 로고    scopus 로고
    • Isolation and characterization of Pas2p, a peroxisomal membrane protein essential for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris
    • Wiemer, E.A., G.H. Lüers, K.N. Faber, T. Wenzel, M. Veenhuis, and S. Subramani. 1996. Isolation and characterization of Pas2p, a peroxisomal membrane protein essential for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris. J. Biol. Chem. 271:18973-18980. http://dx.doi.org/10.1074/jbc.271.31.18973
    • (1996) J. Biol. Chem. , vol.271 , pp. 18973-18980
    • Wiemer, E.A.1    Lüers, G.H.2    Faber, K.N.3    Wenzel, T.4    Veenhuis, M.5    Subramani, S.6
  • 39
    • 84882641004 scopus 로고    scopus 로고
    • Pexophagy-linked degradation of the peroxisomal membrane protein Pex3p involves the ubiquitin-proteasome system
    • Williams, C., and I.J. van der Klei. 2013. Pexophagy-linked degradation of the peroxisomal membrane protein Pex3p involves the ubiquitin-proteasome system. Biochem. Biophys. Res. Commun. 438:395-401. http://dx.doi.org/10.1016/j.bbrc.2013.07.086
    • (2013) Biochem. Biophys. Res. Commun. , vol.438 , pp. 395-401
    • Williams, C.1    van der Klei, I.J.2
  • 40
    • 31944451252 scopus 로고    scopus 로고
    • Two independent pathways traffic the intraperoxisomal peroxin PpPex8p into peroxisomes: mechanism and evolutionary implications
    • Zhang, L., S. Léon, and S. Subramani. 2006. Two independent pathways traffic the intraperoxisomal peroxin PpPex8p into peroxisomes: mechanism and evolutionary implications. Mol. Biol. Cell. 17:690-699. http://dx.doi.org/10.1091/mbc. E05-08-0758
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 690-699
    • Zhang, L.1    Léon, S.2    Subramani, S.3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.