메뉴 건너뛰기




Volumn 174, Issue 1, 2006, Pages 11-17

Peroxisome biogenesis: The peroxisomal endomembrane system and the role of the ER

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN COMPLEX I; COAT PROTEIN COMPLEX II; MEMBRANE PROTEIN; PROTEIN PEROXISOMAL MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 33745632081     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200604036     Document Type: Short Survey
Times cited : (73)

References (49)
  • 3
    • 0037343124 scopus 로고    scopus 로고
    • Peroxisome biogenesis occurs in an unsynchronized manner in close association with the endoplasmic reticulum in temperature-sensitive Yarrowia lipolytica Pex3p mutants
    • Bascom, R.A., H. Chan, and R.A. Rachubinski. 2003. Peroxisome biogenesis occurs in an unsynchronized manner in close association with the endoplasmic reticulum in temperature-sensitive Yarrowia lipolytica Pex3p mutants. Mol. Biol. Cell. 14:939-957.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 939-957
    • Bascom, R.A.1    Chan, H.2    Rachubinski, R.A.3
  • 4
    • 0001124810 scopus 로고
    • Microbodies in higher plants
    • Beevers, H. 1979. Microbodies in higher plants. Annu. Rev. Plant Physiol. 30:159-193.
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 159-193
    • Beevers, H.1
  • 6
    • 0026341459 scopus 로고
    • Acquisition of membrane lipids by differentiating glyoxysomes: Role of lipid bodies
    • Chapman, K.D., and R.N. Trelease. 1991. Acquisition of membrane lipids by differentiating glyoxysomes: role of lipid bodies. J. Cell Biol. 115:995-1007.
    • (1991) J. Cell Biol. , vol.115 , pp. 995-1007
    • Chapman, K.D.1    Trelease, R.N.2
  • 7
    • 0031448780 scopus 로고    scopus 로고
    • Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane
    • Elgersma, Y., L. Kwast, M. van den Berg, W.B. Snyder, B. Distel, S. Subramani, and H.F. Tabak. 1997. Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane. EMBO J. 16:7326-7341.
    • (1997) EMBO J. , vol.16 , pp. 7326-7341
    • Elgersma, Y.1    Kwast, L.2    Van Den Berg, M.3    Snyder, W.B.4    Distel, B.5    Subramani, S.6    Tabak, H.F.7
  • 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.S. 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.
    • (2006) FEMS Yeast Res. , vol.6 , pp. 186-194
    • Haan, G.-J.1    Baerends, R.J.S.2    Krikken, A.M.3    Otzen, M.4    Veenhuis, M.5    Van Der Klei, I.J.6
  • 11
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond, A.T., and B.S. Glick. 2000. Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell. 11:3013-3030.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 12
    • 15844404207 scopus 로고    scopus 로고
    • Crossing the divide - Transport between the endoplasmic reticulum and Golgi apparatus in plants
    • Hanton, S.L., L.E. Bortolotti, L. Renna, G. Stefano, and F. Brandizzi. 2005. Crossing the divide - transport between the endoplasmic reticulum and Golgi apparatus in plants. Traffic. 6:267-277.
    • (2005) Traffic , vol.6 , pp. 267-277
    • Hanton, S.L.1    Bortolotti, L.E.2    Renna, L.3    Stefano, G.4    Brandizzi, F.5
  • 13
    • 22144465170 scopus 로고    scopus 로고
    • Contribution of the endoplasmic reticulum to peroxisome formation
    • Hoepfner, D., D. Schildknegt, I. Braakman, P. Philippsen, and H.F. Tabak. 2005. Contribution of the endoplasmic reticulum to peroxisome formation. Cell. 122:85-95.
    • (2005) Cell , vol.122 , pp. 85-95
    • Hoepfner, D.1    Schildknegt, D.2    Braakman, I.3    Philippsen, P.4    Tabak, H.F.5
  • 14
    • 33646791462 scopus 로고    scopus 로고
    • The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER
    • Kim, P.K., R.T. Mullen, W. Schumann, and J. Lippincott-Schwartz. 2006. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 173:521-532.
    • (2006) J. Cell Biol. , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, W.3    Lippincott-Schwartz, J.4
  • 15
    • 26644475449 scopus 로고    scopus 로고
    • Endoplasmic reticulum-directed Pex3p routes to peroxisomes and restores peroxisome formation in a Saccharomyces cerevisiae pex3Δ strain
    • Kragt, A., T. Voorn-Brouwer, M. van den Berg, and B. Distel. 2005. Endoplasmic reticulum-directed Pex3p routes to peroxisomes and restores peroxisome formation in a Saccharomyces cerevisiae pex3Δ strain. J. Biol. Chem. 280:34350-34357.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34350-34357
    • Kragt, A.1    Voorn-Brouwer, T.2    Van Den Berg, M.3    Distel, B.4
  • 16
    • 24944520856 scopus 로고    scopus 로고
    • Peroxisome biogenesis: End of the debate
    • Kunau, W.-H. 2005. Peroxisome biogenesis: end of the debate. Curr. Biol. 15:R774-R776.
    • (2005) Curr. Biol. , vol.15
    • Kunau, W.-H.1
  • 17
    • 27144508207 scopus 로고    scopus 로고
    • Binding and functions of ADP-ribosylation factor on mammalian and yeast peroxisomes
    • Lay, D., B.L. Grosshans, H. Heid, K. Gorgas, and W.W. Just. 2005. Binding and functions of ADP-ribosylation factor on mammalian and yeast peroxisomes. J. Biol. Chem. 280:34489-34499.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34489-34499
    • Lay, D.1    Grosshans, B.L.2    Heid, H.3    Gorgas, K.4    Just, W.W.5
  • 18
    • 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
  • 21
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine, T. 2004. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14:483-490.
    • (2004) Trends Cell Biol. , vol.14 , pp. 483-490
    • Levine, T.1
  • 22
    • 0037832556 scopus 로고    scopus 로고
    • Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells
    • Lisenbee, C.S., M. Heinze, and R.N. Trelease. 2003. Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells. Plant Physiol. 132:870-882.
    • (2003) Plant Physiol. , vol.132 , pp. 870-882
    • Lisenbee, C.S.1    Heinze, M.2    Trelease, R.N.3
  • 24
    • 33644816419 scopus 로고    scopus 로고
    • Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway
    • McCartney, A.W., J.S. Greenwood, M.R. Fabian, K.A. White, and R.T. Mullen. 2005. Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway. Plant Cell. 17:3513-3531.
    • (2005) Plant Cell. , vol.17 , pp. 3513-3531
    • McCartney, A.W.1    Greenwood, J.S.2    Fabian, M.R.3    White, K.A.4    Mullen, R.T.5
  • 25
    • 0034717248 scopus 로고    scopus 로고
    • The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail
    • Mullen, R.T., and R.N. Trelease. 2000. The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail. J. Biol. Chem. 275:16337-16344.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16337-16344
    • Mullen, R.T.1    Trelease, R.N.2
  • 26
    • 0033231111 scopus 로고    scopus 로고
    • Peroxisomal membrane ascorbate peroxidase is sorted to a membranous network that resembles a subdomain of the endoplasmic reticulum
    • Mullen, R.T., C.S. Lisenbee, J.A. Miernyk, and R.N. Trelease. 1999. Peroxisomal membrane ascorbate peroxidase is sorted to a membranous network that resembles a subdomain of the endoplasmic reticulum. Plant Cell. 11:2167-2185.
    • (1999) Plant Cell. , vol.11 , pp. 2167-2185
    • Mullen, R.T.1    Lisenbee, C.S.2    Miernyk, J.A.3    Trelease, R.N.4
  • 27
    • 0035210089 scopus 로고    scopus 로고
    • How are peroxisomes formed? the role of the endoplasmic reticulum and peroxins
    • Mullen, R.T., C.R. Flynn, and R.N. Trelease. 2001. How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins. Trends Plant Sci. 6:256-261.
    • (2001) Trends Plant Sci. , vol.6 , pp. 256-261
    • Mullen, R.T.1    Flynn, C.R.2    Trelease, R.N.3
  • 28
    • 33745597353 scopus 로고    scopus 로고
    • Peroxisome biogenesis and the formation of multivesicular peroxisomes during tombusvirus infection: A role for ESCRT?
    • Mullen, R.T., A.W. McCartney, C.R. Flynn, and G.S.T. Smith. 2006. Peroxisome biogenesis and the formation of multivesicular peroxisomes during tombusvirus infection: a role for ESCRT? Can. J. Bot. 84:551-564.
    • (2006) Can. J. Bot. , vol.84 , pp. 551-564
    • Mullen, R.T.1    McCartney, A.W.2    Flynn, C.R.3    Smith, G.S.T.4
  • 31
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese, O.W., J. Soderholm, B.J. Bevis, I.B. Sears, J. O'Connor, E.K. Williamson, and B.S. Glick. 1999. Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 145:69-81.
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 32
    • 0030810961 scopus 로고    scopus 로고
    • Brefeldin a interferes with peroxisomal protein sorting in the yeast Hansenula polymorpha
    • Salomons, F.A., I.J. van der Klei, A.M. Kram, W. Harder, and M. Veenhuis. 1997. Brefeldin A interferes with peroxisomal protein sorting in the yeast Hansenula polymorpha. FEBS Lett. 411:133-139.
    • (1997) FEBS Lett. , vol.411 , pp. 133-139
    • Salomons, F.A.1    Van Der Klei, I.J.2    Kram, A.M.3    Harder, W.4    Veenhuis, M.5
  • 33
    • 22144434043 scopus 로고    scopus 로고
    • Peroxisomes: Another branch of the secretory pathway?
    • Schekman, R. 2005. Peroxisomes: another branch of the secretory pathway? Cell. 122:1-2.
    • (2005) Cell , vol.122 , pp. 1-2
    • Schekman, R.1
  • 34
    • 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.
    • (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
  • 35
    • 0035834125 scopus 로고    scopus 로고
    • Inactivation of the endoplasmic reticulum protein translocation factor, Sec61p, or its homolog, Ssh1p, does not affect peroxisome biogenesis
    • South, S.T., E. Baumgart, and S.J. Gould. 2001. Inactivation of the endoplasmic reticulum protein translocation factor, Sec61p, or its homolog, Ssh1p, does not affect peroxisome biogenesis. Proc. Natl. Acad. Sci. USA. 98:12027-12031.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12027-12031
    • South, S.T.1    Baumgart, E.2    Gould, S.J.3
  • 36
    • 0041810193 scopus 로고    scopus 로고
    • Peroxisomes start their life in the endoplasmic reticulum
    • Tabak, H.F., J.L. Murk, I. Braakman, and H.J. Geuze. 2003. Peroxisomes start their life in the endoplasmic reticulum. Traffic. 4:512-518.
    • (2003) Traffic , vol.4 , pp. 512-518
    • Tabak, H.F.1    Murk, J.L.2    Braakman, I.3    Geuze, H.J.4
  • 37
    • 27144457472 scopus 로고    scopus 로고
    • Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae
    • Tam, Y.Y.C., A. Fagarasanu, M. Fagarasanu, and R.A. Rachubinski. 2005. Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae. J. Biol. Chem. 280:34933-34939.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34933-34939
    • Tam, Y.Y.C.1    Fagarasanu, A.2    Fagarasanu, M.3    Rachubinski, R.A.4
  • 38
    • 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.
    • (2005) FEBS J. , vol.272 , pp. 5169-5181
    • Thoms, S.1    Erdmann, R.2
  • 39
    • 0031895522 scopus 로고    scopus 로고
    • Mutants of the yeast Yarrowia lipolytica defective in protein exit from the endoplasmic reticulum are also defective in peroxisome biogenesis
    • Titorenko, V.I., and R.A. Rachubinski. 1998. Mutants of the yeast Yarrowia lipolytica defective in protein exit from the endoplasmic reticulum are also defective in peroxisome biogenesis. Mol. Cell. Biol. 18:2789-2803.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2789-2803
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 40
    • 0034698778 scopus 로고    scopus 로고
    • Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p
    • Titorenko, V.I., and R.A. Rachubinski. 2000. Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p. J. Cell Biol. 150:881-886.
    • (2000) J. Cell Biol. , vol.150 , pp. 881-886
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 41
    • 0035176257 scopus 로고    scopus 로고
    • Dynamics of peroxisome assembly and function
    • Titorenko, V.I., and R.A. Rachubinski. 2001. Dynamics of peroxisome assembly and function. Trends Cell Biol. 11:22-29.
    • (2001) Trends Cell Biol. , vol.11 , pp. 22-29
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 42
    • 0029786673 scopus 로고    scopus 로고
    • Mutations in the PAY5 gene of the yeast Yarrowia lipolytica cause the accumulation of multiple subpopulations of peroxisomes
    • Titorenko, V.I., G.A. Eitzen, and R.A. Rachubinski. 1996. Mutations in the PAY5 gene of the yeast Yarrowia lipolytica cause the accumulation of multiple subpopulations of peroxisomes. J. Biol. Chem. 271:20307-20314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20307-20314
    • Titorenko, V.I.1    Eitzen, G.A.2    Rachubinski, R.A.3
  • 43
    • 0030797545 scopus 로고    scopus 로고
    • Four distinct secretory pathways serve protein secretion, cell surface growth, and peroxisome biogenesis in the yeast Yarrowia lipolytica
    • Titorenko, V.I., D.M. Ogrydziak, and R.A. Rachubinski. 1997. Four distinct secretory pathways serve protein secretion, cell surface growth, and peroxisome biogenesis in the yeast Yarrowia lipolytica. Mol. Cell. Biol. 17:5210-5226.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5210-5226
    • Titorenko, V.I.1    Ogrydziak, D.M.2    Rachubinski, R.A.3
  • 44
    • 0034627808 scopus 로고    scopus 로고
    • Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multi-step peroxisome assembly pathway of Yarrowia lipolytica
    • Titorenko, V.I., H. Chan, and R.A. Rachubinski. 2000. Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multi-step peroxisome assembly pathway of Yarrowia lipolytica. J. Cell Biol. 148:29-43.
    • (2000) J. Cell Biol. , vol.148 , pp. 29-43
    • Titorenko, V.I.1    Chan, H.2    Rachubinski, R.A.3
  • 45
    • 0025103805 scopus 로고
    • Peroxisomal assembly: Membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii
    • Veenhuis, M., and J.M. Goodman. 1990. Peroxisomal assembly: membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii. J. Cell Sci. 96:583-590.
    • (1990) J. Cell Sci. , vol.96 , pp. 583-590
    • Veenhuis, M.1    Goodman, J.M.2
  • 46
    • 0034962022 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- and COPII-mediated vesicular transport
    • Voorn-Brouwer, T., A. Kragt, H.F. Tabak, and B. Distel. 2001. Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- and COPII-mediated vesicular transport. J. Cell Sci. 114:2199-2204.
    • (2001) J. Cell Sci. , vol.114 , pp. 2199-2204
    • Voorn-Brouwer, T.1    Kragt, A.2    Tabak, H.F.3    Distel, B.4
  • 47
    • 1642423544 scopus 로고    scopus 로고
    • Multiple targeting modules on peroxisomal proteins are not redundant: Discrete functions of targeting signals within Pmp47 and Pex8p
    • Wang, X., M.A. McMahon, S.N. Shelton, M. Nampaisansuk, J.L. Ballard, and J.M. Goodman. 2004. Multiple targeting modules on peroxisomal proteins are not redundant: discrete functions of targeting signals within Pmp47 and Pex8p. Mol. Biol. Cell. 15:1702-1710.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 1702-1710
    • Wang, X.1    McMahon, M.A.2    Shelton, S.N.3    Nampaisansuk, M.4    Ballard, J.L.5    Goodman, J.M.6
  • 48
    • 20544471158 scopus 로고    scopus 로고
    • ER-to-Golgi transport: Form and formation of vesicular and tubular carriers
    • Watson, P., and D.J. Stephens. 2005. ER-to-Golgi transport: form and formation of vesicular and tubular carriers. Biochim. Biophys. Acta. 1744:304-315.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 304-315
    • Watson, P.1    Stephens, D.J.2
  • 49
    • 22044444453 scopus 로고    scopus 로고
    • The control of peroxisome number and size during division and proliferation
    • Yan, M., N. Rayapuram, and S. Subramani. 2005. The control of peroxisome number and size during division and proliferation. Curr. Opin. Cell Biol. 17:376-383.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 376-383
    • Yan, M.1    Rayapuram, N.2    Subramani, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.