메뉴 건너뛰기




Volumn 272, Issue C, 2008, Pages 191-244

Chapter 5 Spatiotemporal Dynamics of the ER-derived Peroxisomal Endomembrane System

Author keywords

Endomembranes; Endoplasmic reticulum; Interorganellar vesicular flow; Organelle biogenesis; Organelle division and inheritance; Peroxisome; Protein and lipid sorting

Indexed keywords

MEMBRANE LIPID; MEMBRANE PROTEIN; PEROXISOMAL MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 58049170675     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(08)01605-5     Document Type: Review
Times cited : (24)

References (209)
  • 1
    • 0032545023 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p
    • Abe I., and Fujiki Y. cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p. Biochem. Biophys. Res. Commun. 252 (1998) 529-533
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 529-533
    • Abe, I.1    Fujiki, Y.2
  • 4
    • 0025876058 scopus 로고
    • Low-density particles (W-particles) containing catalase in Zellweger syndrome and normal fibroblasts
    • Aikawa J., Chen W.W., Kelley R.I., Tada K., Moser H.W., and Chen G.L. Low-density particles (W-particles) containing catalase in Zellweger syndrome and normal fibroblasts. Proc. Natl Acad. Sci. USA 88 (1991) 10084-10088
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10084-10088
    • Aikawa, J.1    Chen, W.W.2    Kelley, R.I.3    Tada, K.4    Moser, H.W.5    Chen, G.L.6
  • 5
    • 0347695021 scopus 로고    scopus 로고
    • Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat
    • Andag U., and Schmitt H.D. Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat. J. Biol. Chem. 278 (2003) 35172-35174
    • (2003) J. Biol. Chem. , vol.278 , pp. 35172-35174
    • Andag, U.1    Schmitt, H.D.2
  • 6
    • 0035914416 scopus 로고    scopus 로고
    • The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast
    • Andag U., Neumann T., and Schmitt H.D. The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J. Biol. Chem. 276 (2001) 39150-39160
    • (2001) J. Biol. Chem. , vol.276 , pp. 39150-39160
    • Andag, U.1    Neumann, T.2    Schmitt, H.D.3
  • 9
    • 0034192231 scopus 로고    scopus 로고
    • Nuclear receptors arose from pre-existing protein modules during evolution
    • Barnett P., Tabak H.F., and Hettema E.H. Nuclear receptors arose from pre-existing protein modules during evolution. Trends Biochem. Sci. 25 (2000) 227-228
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 227-228
    • Barnett, P.1    Tabak, H.F.2    Hettema, E.H.3
  • 10
    • 0036498859 scopus 로고    scopus 로고
    • The Golgi apparatus: Going round in circles?
    • Barr F.A. The Golgi apparatus: Going round in circles?. Trends Cell Biol. 12 (2002) 101-104
    • (2002) Trends Cell Biol. , vol.12 , pp. 101-104
    • Barr, F.A.1
  • 11
    • 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., Chan H., and Rachubinski R.A. 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 (2003) 939-957
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 939-957
    • Bascom, R.A.1    Chan, H.2    Rachubinski, R.A.3
  • 13
    • 0001124810 scopus 로고
    • Microbodies in higher plants
    • Beevers H. Microbodies in higher plants. Annu. Rev. Plant Physiol. 30 (1979) 159-193
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 159-193
    • Beevers, H.1
  • 14
    • 0036799651 scopus 로고    scopus 로고
    • De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
    • Bevis B.J., Hammond A.T., Reinke C.A., and Glick B.S. De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat. Cell Biol. 4 (2002) 750-756
    • (2002) Nat. Cell Biol. , vol.4 , pp. 750-756
    • Bevis, B.J.1    Hammond, A.T.2    Reinke, C.A.3    Glick, B.S.4
  • 16
    • 0024150892 scopus 로고
    • Assembly of phospholipids into cellular membranes: Biosynthesis, transmembrane movement and intracellular translocation
    • Bishop W.R., and Bell R.M. Assembly of phospholipids into cellular membranes: Biosynthesis, transmembrane movement and intracellular translocation. Annu. Rev. Cell Biol. 4 (1988) 579-610
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 579-610
    • Bishop, W.R.1    Bell, R.M.2
  • 18
    • 33845370100 scopus 로고    scopus 로고
    • Lipids and lipid domains in the peroxisomal membrane of the yeast Yarrowia lipolytica
    • Boukh-Viner T., and Titorenko V.I. Lipids and lipid domains in the peroxisomal membrane of the yeast Yarrowia lipolytica. Biochim. Biophys. Acta. 1763 (2006) 1688-1696
    • (2006) Biochim. Biophys. Acta. , vol.1763 , pp. 1688-1696
    • Boukh-Viner, T.1    Titorenko, V.I.2
  • 21
    • 0026341459 scopus 로고
    • Acquisition of membrane lipids by differentiating glyoxysomes: Role of lipid bodies
    • Chapman K.D., and Trelease R.N. Acquisition of membrane lipids by differentiating glyoxysomes: Role of lipid bodies. J. Cell Biol. 115 (1991) 995-1007
    • (1991) J. Cell Biol. , vol.115 , pp. 995-1007
    • Chapman, K.D.1    Trelease, R.N.2
  • 22
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik L.V., and Kozlov M.M. Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72 (2003) 175-207
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 23
    • 33745450483 scopus 로고    scopus 로고
    • Macromolecular assemblies regulate nonvesicular phosphatidylserine traffic in yeast
    • Choi J.Y., Riekhof W.R., Wu W.I., and Voelker D.R. Macromolecular assemblies regulate nonvesicular phosphatidylserine traffic in yeast. Biochem. Soc. Trans. 34 (2006) 404-408
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 404-408
    • Choi, J.Y.1    Riekhof, W.R.2    Wu, W.I.3    Voelker, D.R.4
  • 26
    • 33644821441 scopus 로고    scopus 로고
    • The multiple activities of CtBP/BARS proteins: The Golgi view
    • Corda D., Colanzi A., and Luini A. The multiple activities of CtBP/BARS proteins: The Golgi view. Trends Cell Biol. 16 (2006) 167-173
    • (2006) Trends Cell Biol. , vol.16 , pp. 167-173
    • Corda, D.1    Colanzi, A.2    Luini, A.3
  • 27
    • 33645863768 scopus 로고    scopus 로고
    • Transcriptional regulation of metabolism
    • Desvergne B., Michalik L., and Wahli W. Transcriptional regulation of metabolism. Physiol. Rev. 86 (2006) 465-514
    • (2006) Physiol. Rev. , vol.86 , pp. 465-514
    • Desvergne, B.1    Michalik, L.2    Wahli, W.3
  • 29
    • 0031007808 scopus 로고    scopus 로고
    • Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin
    • Eitzen G.A., Szilard R.K., and Rachubinski R.A. Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin. J. Cell Biol. 137 (1997) 1265-1278
    • (1997) J. Cell Biol. , vol.137 , pp. 1265-1278
    • Eitzen, G.A.1    Szilard, R.K.2    Rachubinski, R.A.3
  • 30
    • 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., Kwast L., van den Berg M., Snyder W.B., Distel B., Subramani S., and Tabak H.F. 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 (1997) 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
  • 31
    • 0028859252 scopus 로고
    • Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p
    • Erdmann R., and Blobel G. Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p. J. Cell Biol. 128 (1995) 509-523
    • (1995) J. Cell Biol. , vol.128 , pp. 509-523
    • Erdmann, R.1    Blobel, G.2
  • 32
    • 36549083069 scopus 로고    scopus 로고
    • Orchestrating organelle inheritance in Saccharomyces cerevisiae
    • Fagarasanu A., and Rachubinski R.A. Orchestrating organelle inheritance in Saccharomyces cerevisiae. Curr. Opin. Microbiol. 10 (2007) 528-538
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 528-538
    • Fagarasanu, A.1    Rachubinski, R.A.2
  • 33
    • 33646093006 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae
    • Fagarasanu A., Fagarasanu M., Eitzen G.A., Aitchison J.D., and Rachubinski R.A. The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae. Dev. Cell 10 (2006) 587-600
    • (2006) Dev. Cell , vol.10 , pp. 587-600
    • Fagarasanu, A.1    Fagarasanu, M.2    Eitzen, G.A.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 34
  • 35
    • 0032546929 scopus 로고    scopus 로고
    • Steatohepatitis, spontaneous peroxisome proliferation and liver tumors in mice lacking peroxisomal fatty acyl-CoA oxidase. Implications for peroxisome proliferator-activated receptor α natural ligand metabolism
    • Fan C.Y., Pan J., Usuda N., Yeldandi A.V., Rao M.S., and Reddy J.K. Steatohepatitis, spontaneous peroxisome proliferation and liver tumors in mice lacking peroxisomal fatty acyl-CoA oxidase. Implications for peroxisome proliferator-activated receptor α natural ligand metabolism. J. Biol. Chem. 273 (1998) 15639-15645
    • (1998) J. Biol. Chem. , vol.273 , pp. 15639-15645
    • Fan, C.Y.1    Pan, J.2    Usuda, N.3    Yeldandi, A.V.4    Rao, M.S.5    Reddy, J.K.6
  • 37
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • Fath S., Mancias J.D., Bi X., and Goldberg J. Structure and organization of coat proteins in the COPII cage. Cell 129 (2007) 1325-1336
    • (2007) Cell , vol.129 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 38
    • 32644460092 scopus 로고    scopus 로고
    • From molecular action to physiological outputs: Peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions
    • Feige J.N., Gelman L., Michalik L., Desvergne B., and Wahli W. From molecular action to physiological outputs: Peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions. Prog. Lipid Res. 45 (2006) 120-159
    • (2006) Prog. Lipid Res. , vol.45 , pp. 120-159
    • Feige, J.N.1    Gelman, L.2    Michalik, L.3    Desvergne, B.4    Wahli, W.5
  • 39
    • 22044441866 scopus 로고    scopus 로고
    • COPII-coated vesicles: Flexible enough for large cargo?
    • Fromme J.C., and Schekman R. COPII-coated vesicles: Flexible enough for large cargo?. Curr. Opin. Cell Biol. 17 (2005) 345-352
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 345-352
    • Fromme, J.C.1    Schekman, R.2
  • 40
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., and Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J. Cell Biol. 93 (1982) 97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 42
    • 0035339285 scopus 로고    scopus 로고
    • ER export: More than one way out
    • Glick B.S. ER export: More than one way out. Curr. Biol. 11 (2001) R361-R363
    • (2001) Curr. Biol. , vol.11
    • Glick, B.S.1
  • 43
    • 0036341243 scopus 로고    scopus 로고
    • Can the Golgi form de novo?
    • Glick B.S. Can the Golgi form de novo?. Nat. Rev. Mol. Cell Biol. 3 (2002) 615-619
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 615-619
    • Glick, B.S.1
  • 44
    • 34250838745 scopus 로고    scopus 로고
    • Dysferlin in membrane trafficking and patch repair
    • Glover L., and Brown Jr. R.H. Dysferlin in membrane trafficking and patch repair. Traffic 8 (2007) 785-794
    • (2007) Traffic , vol.8 , pp. 785-794
    • Glover, L.1    Brown Jr., R.H.2
  • 46
    • 0034255179 scopus 로고    scopus 로고
    • Peroxisome biogenesis disorders: Genetics and cell biology
    • Gould S.J., and Valle D. Peroxisome biogenesis disorders: Genetics and cell biology. Trends Genet. 16 (2000) 340-345
    • (2000) Trends Genet. , vol.16 , pp. 340-345
    • Gould, S.J.1    Valle, D.2
  • 50
    • 33645070532 scopus 로고    scopus 로고
    • Reassembly of peroxisomes in Hansenula polymorpha pex3 cells on reintroduction of Pex3p involves the nuclear envelope
    • Haan G.-J., Baerends R.J.S., Krikken A.M., Otzen M., Veenhuis M., and van der Klei I.J. Reassembly of peroxisomes in Hansenula polymorpha pex3 cells on reintroduction of Pex3p involves the nuclear envelope. FEMS Yeast Res. 6 (2006) 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
  • 51
    • 0037148531 scopus 로고    scopus 로고
    • A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway
    • Harsay E., and Schekman R. A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway. J. Cell Biol. 156 (2002) 271-285
    • (2002) J. Cell Biol. , vol.156 , pp. 271-285
    • Harsay, E.1    Schekman, R.2
  • 53
    • 0026511317 scopus 로고
    • Peroxisomal protein import. In vivo evidence for a novel translocation competent compartment
    • Heinemann P., and Just W.W. Peroxisomal protein import. In vivo evidence for a novel translocation competent compartment. FEBS Lett. 300 (1992) 179-182
    • (1992) FEBS Lett. , vol.300 , pp. 179-182
    • Heinemann, P.1    Just, W.W.2
  • 54
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner D., van den Berg M., Philippsen P., Tabak H.F., and Hettema E.H. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155 (2001) 979-990
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    van den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 55
  • 56
    • 14644393694 scopus 로고    scopus 로고
    • Lipid traffic: Floppy drives and a superhighway
    • Holthuis J.C., and Levine T.P. Lipid traffic: Floppy drives and a superhighway. Nat. Rev. Mol. Cell Biol. 6 (2005) 209-220
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 209-220
    • Holthuis, J.C.1    Levine, T.P.2
  • 57
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S., Lackner L., and Nunnari J. The machines that divide and fuse mitochondria. Annu. Rev. Biochem. 76 (2007) 751-780
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 58
    • 39149086740 scopus 로고    scopus 로고
    • Assembly, organization, and function of the COPII coat
    • Hughes H., and Stephens D.J. Assembly, organization, and function of the COPII coat. Histochem. Cell Biol. 129 (2008) 129-151
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 129-151
    • Hughes, H.1    Stephens, D.J.2
  • 59
    • 0035424718 scopus 로고    scopus 로고
    • Implications of lipid microdomains for membrane curvature, budding and fission
    • Huttner W.B., and Zimmerberg J. Implications of lipid microdomains for membrane curvature, budding and fission. Curr. Opin. Cell Biol. 13 (2001) 478-484
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 478-484
    • Huttner, W.B.1    Zimmerberg, J.2
  • 60
    • 26844566194 scopus 로고    scopus 로고
    • Arabidopsis peroxin 16 coexists at steady state in peroxisomes and endoplasmic reticulum
    • Karnik S.K., and Trelease R.N. Arabidopsis peroxin 16 coexists at steady state in peroxisomes and endoplasmic reticulum. Plant Physiol. 138 (2005) 1967-1981
    • (2005) Plant Physiol. , vol.138 , pp. 1967-1981
    • Karnik, S.K.1    Trelease, R.N.2
  • 61
    • 34547466205 scopus 로고    scopus 로고
    • Arabidopsis peroxin 16 trafficks through the ER and an intermediate compartment to pre-existing peroxisomes via overlapping molecular targeting signals
    • Karnik S.K., and Trelease R.N. Arabidopsis peroxin 16 trafficks through the ER and an intermediate compartment to pre-existing peroxisomes via overlapping molecular targeting signals. J. Exp. Bot. 58 (2007) 1677-1693
    • (2007) J. Exp. Bot. , vol.58 , pp. 1677-1693
    • Karnik, S.K.1    Trelease, R.N.2
  • 62
    • 0034713444 scopus 로고    scopus 로고
    • Roles of PPARs in health and disease
    • Kersten S., Desvergne B., and Wahli W. Roles of PPARs in health and disease. Nature 405 (2000) 421-424
    • (2000) Nature , vol.405 , pp. 421-424
    • Kersten, S.1    Desvergne, B.2    Wahli, W.3
  • 63
    • 12844252572 scopus 로고    scopus 로고
    • Overproduction of a single protein, Pc-Pex11p, results in 2-fold enhanced penicillin production by Penicillium chrysogenum
    • Kiel J.A., van der Klei I.J., van den Berg M.A., Bovenberg R.A., and Veenhuis M. Overproduction of a single protein, Pc-Pex11p, results in 2-fold enhanced penicillin production by Penicillium chrysogenum. Fungal Genet. Biol. 42 (2005) 154-164
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 154-164
    • Kiel, J.A.1    van der Klei, I.J.2    van den Berg, M.A.3    Bovenberg, R.A.4    Veenhuis, M.5
  • 64
    • 33748565936 scopus 로고    scopus 로고
    • PEX genes in fungal genomes: Common, rare or redundant
    • Kiel J.A., Veenhuis M., and van der Klei I.J. PEX genes in fungal genomes: Common, rare or redundant. Traffic 7 (2006) 1291-1303
    • (2006) Traffic , vol.7 , pp. 1291-1303
    • Kiel, J.A.1    Veenhuis, M.2    van der Klei, I.J.3
  • 65
    • 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., Mullen R.T., Schumann W., and Lippincott-Schwartz J. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 173 (2006) 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
  • 66
    • 0030698622 scopus 로고    scopus 로고
    • Major histocompatibility complex class II compartments in human and mouse B lymphoblasts represent conventional endocytic compartments
    • Kleijmeer M.J., Morkowski S., Griffith J.M., Rudensky A.Y., and Geuze H.J. Major histocompatibility complex class II compartments in human and mouse B lymphoblasts represent conventional endocytic compartments. J. Cell Biol. 139 (1997) 639-649
    • (1997) J. Cell Biol. , vol.139 , pp. 639-649
    • Kleijmeer, M.J.1    Morkowski, S.2    Griffith, J.M.3    Rudensky, A.Y.4    Geuze, H.J.5
  • 67
    • 0025802973 scopus 로고
    • Identification of a catalase-negative sub-population of peroxisomes induced in mouse liver by clofibrate
    • Klucis E., Crane D.I., Hughes J.L., Poulos A., and Masters C.J. Identification of a catalase-negative sub-population of peroxisomes induced in mouse liver by clofibrate. Biochim. Biophys. Acta 1074 (1991) 294-301
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 294-301
    • Klucis, E.1    Crane, D.I.2    Hughes, J.L.3    Poulos, A.4    Masters, C.J.5
  • 69
    • 4444236087 scopus 로고    scopus 로고
    • Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1
    • Koch A., Schneider G., Lüers G.H., and Schrader M. Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1. J. Cell Sci. 117 (2004) 3995-4006
    • (2004) J. Cell Sci. , vol.117 , pp. 3995-4006
    • Koch, A.1    Schneider, G.2    Lüers, G.H.3    Schrader, M.4
  • 70
    • 27144557499 scopus 로고    scopus 로고
    • A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
    • Koch A., Yoon Y., Bonekamp N.A., McNiven M.A., and Schrader M. A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 16 (2005) 5077-5086
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5077-5086
    • Koch, A.1    Yoon, Y.2    Bonekamp, N.A.3    McNiven, M.A.4    Schrader, M.5
  • 71
    • 0038662612 scopus 로고    scopus 로고
    • Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid
    • Kooijman E.E., Chupin V., de Kruijff B., and Burger K.N.J. Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid. Traffic 4 (2003) 162-174
    • (2003) Traffic , vol.4 , pp. 162-174
    • Kooijman, E.E.1    Chupin, V.2    de Kruijff, B.3    Burger, K.N.J.4
  • 72
    • 26644475449 scopus 로고    scopus 로고
    • Endoplasmic reticulum-directed Pex3p routes to peroxisomes and restores peroxisome formation in a Saccharomyces cerevisiae pex3 {up triangle, open} strain
    • Kragt A., Voorn-Brouwer T., van den Berg M., and Distel B. Endoplasmic reticulum-directed Pex3p routes to peroxisomes and restores peroxisome formation in a Saccharomyces cerevisiae pex3 {up triangle, open} strain. J. Biol. Chem. 280 (2005) 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
  • 73
    • 24344480456 scopus 로고    scopus 로고
    • Dsl1p, Tip20p, and the novel Dsl3 (Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
    • Kraynack B.A., Chan A., Rosenthal E., Essid M., Umansky B., Waters M.G., and Schmitt H.D. Dsl1p, Tip20p, and the novel Dsl3 (Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol. Biol. Cell 16 (2005) 3963-3967
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3963-3967
    • Kraynack, B.A.1    Chan, A.2    Rosenthal, E.3    Essid, M.4    Umansky, B.5    Waters, M.G.6    Schmitt, H.D.7
  • 74
    • 38849096602 scopus 로고    scopus 로고
    • Imaging of lipid biosynthesis: How a neutral lipid enters lipid droplets
    • Kuerschner L., Moessinger C., and Thiele C. Imaging of lipid biosynthesis: How a neutral lipid enters lipid droplets. Traffic 9 (2008) 338-352
    • (2008) Traffic , vol.9 , pp. 338-352
    • Kuerschner, L.1    Moessinger, C.2    Thiele, C.3
  • 76
    • 27144508207 scopus 로고    scopus 로고
    • Binding and functions of ADP-ribosylation factor on mammalian and yeast peroxisomes
    • Lay D., Grosshans B.L., Heid H., Gorgas K., and Just W.W. Binding and functions of ADP-ribosylation factor on mammalian and yeast peroxisomes. J. Biol. Chem. 280 (2005) 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
  • 77
    • 33845341438 scopus 로고    scopus 로고
    • Peroxisome biogenesis: Where Arf and coatomer might be involved
    • Lay D., Gorgas K., and Just W.W. Peroxisome biogenesis: Where Arf and coatomer might be involved. Biochim. Biophys. Acta 1763 (2006) 1678-1687
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1678-1687
    • Lay, D.1    Gorgas, K.2    Just, W.W.3
  • 78
    • 0006691520 scopus 로고
    • The peroxisomal membrane
    • Bittar E.E. (Ed), Wiley, New York
    • Lazarow P.B. The peroxisomal membrane. In: Bittar E.E. (Ed). Membrane Structure and function (1984), Wiley, New York 1-31
    • (1984) Membrane Structure and function , pp. 1-31
    • Lazarow, P.B.1
  • 79
    • 0041765775 scopus 로고    scopus 로고
    • Peroxisome biogenesis: Advances and conundrums
    • Lazarow P.B. Peroxisome biogenesis: Advances and conundrums. Curr. Opin. Cell Biol. 15 (2003) 489-497
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 489-497
    • Lazarow, P.B.1
  • 82
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • Lee M.C., Orci L., Hamamoto S., Futai E., Ravazzola M., and Schekman R. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122 (2005) 605-617
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 83
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine T. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14 (2004) 483-490
    • (2004) Trends Cell Biol. , vol.14 , pp. 483-490
    • Levine, T.1
  • 84
    • 0037128209 scopus 로고    scopus 로고
    • PEX11 promotes peroxisome division independently of peroxisome metabolism
    • Li X., and Gould S.J. PEX11 promotes peroxisome division independently of peroxisome metabolism. J. Cell Biol. 156 (2002) 643-651
    • (2002) J. Cell Biol. , vol.156 , pp. 643-651
    • Li, X.1    Gould, S.J.2
  • 85
    • 0037930873 scopus 로고    scopus 로고
    • The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11
    • Li X., and Gould S.J. The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11. J. Biol. Chem. 278 (2003) 17012-17020
    • (2003) J. Biol. Chem. , vol.278 , pp. 17012-17020
    • Li, X.1    Gould, S.J.2
  • 86
    • 0036882106 scopus 로고    scopus 로고
    • PEX11α is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation
    • Li X., Baumgart E., Dong G.X., Morrell J.C., Jimenez-Sanchez G., Valle D., Smith K.D., and Gould S.J. PEX11α is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation. Mol. Cell. Biol. 22 (2002) 8226-8240
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8226-8240
    • Li, X.1    Baumgart, E.2    Dong, G.X.3    Morrell, J.C.4    Jimenez-Sanchez, G.5    Valle, D.6    Smith, K.D.7    Gould, S.J.8
  • 87
    • 0036261777 scopus 로고    scopus 로고
    • PEX11 β deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function
    • Li X., Baumgart E., Morrell J.C., Jimenez-Sanchez G., Valle D., and Gould S.J. PEX11 β deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function. Mol. Cell. Biol. 22 (2002) 4358-4365
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4358-4365
    • Li, X.1    Baumgart, E.2    Morrell, J.C.3    Jimenez-Sanchez, G.4    Valle, D.5    Gould, S.J.6
  • 88
    • 0033537759 scopus 로고    scopus 로고
    • The Pex16p homolog SSE1 and storage organelle formation in Arabidopsis seeds
    • Lin Y., Sun L., Nguyen L.V., Rachubinski R.A., and Goodman H.M. The Pex16p homolog SSE1 and storage organelle formation in Arabidopsis seeds. Science 284 (1999) 328-330
    • (1999) Science , vol.284 , pp. 328-330
    • Lin, Y.1    Sun, L.2    Nguyen, L.V.3    Rachubinski, R.A.4    Goodman, H.M.5
  • 89
    • 33744519174 scopus 로고    scopus 로고
    • Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation
    • Lingard M.J., and Trelease R.N. Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation. J. Cell Sci. 119 (2006) 1961-1972
    • (2006) J. Cell Sci. , vol.119 , pp. 1961-1972
    • Lingard, M.J.1    Trelease, R.N.2
  • 90
    • 0037832556 scopus 로고    scopus 로고
    • Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells
    • Lisenbee C.S., Heinze M., and Trelease R.N. Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells. Plant Physiol. 132 (2003) 870-882
    • (2003) Plant Physiol. , vol.132 , pp. 870-882
    • Lisenbee, C.S.1    Heinze, M.2    Trelease, R.N.3
  • 92
    • 33845656956 scopus 로고    scopus 로고
    • Mitochondrial retrograde signaling
    • Liu Z., and Butow R.A. Mitochondrial retrograde signaling. Annu. Rev. Genet. 40 (2006) 159-185
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 159-185
    • Liu, Z.1    Butow, R.A.2
  • 94
    • 0032125799 scopus 로고    scopus 로고
    • Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p
    • Lorenz P., Maier A.G., Baumgart E., Erdmann R., and Clayton C. Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p. EMBO J. 17 (1998) 3542-3555
    • (1998) EMBO J. , vol.17 , pp. 3542-3555
    • Lorenz, P.1    Maier, A.G.2    Baumgart, E.3    Erdmann, R.4    Clayton, C.5
  • 95
    • 0027315501 scopus 로고
    • Biogenesis of peroxisomes: Isolation and characterization of two distinct peroxisomal populations from normal and regenerating rat liver
    • Lüers G., Hashimoto T., Fahimi H.D., and Völkl A. Biogenesis of peroxisomes: Isolation and characterization of two distinct peroxisomal populations from normal and regenerating rat liver. J. Cell Biol. 121 (1993) 1271-1280
    • (1993) J. Cell Biol. , vol.121 , pp. 1271-1280
    • Lüers, G.1    Hashimoto, T.2    Fahimi, H.D.3    Völkl, A.4
  • 96
    • 0029851719 scopus 로고    scopus 로고
    • The role of cytokines in functional regulation and differentiation of dendritic cells
    • Lutz M.B., Girolomoni G., and Ricciardi-Castagnoli P. The role of cytokines in functional regulation and differentiation of dendritic cells. Immunobiology 195 (1996) 431-455
    • (1996) Immunobiology , vol.195 , pp. 431-455
    • Lutz, M.B.1    Girolomoni, G.2    Ricciardi-Castagnoli, P.3
  • 97
    • 0031782969 scopus 로고    scopus 로고
    • Cell polarity and morphogenesis in budding yeast
    • Madden K., and Snyder M. Cell polarity and morphogenesis in budding yeast. Annu. Rev. Microbiol. 52 (1998) 687-744
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 687-744
    • Madden, K.1    Snyder, M.2
  • 98
    • 0035062359 scopus 로고    scopus 로고
    • An essential dimeric membrane protein of trypanosome glycosomes
    • Maier A., Lorenz P., Voncken F., and Clayton C. An essential dimeric membrane protein of trypanosome glycosomes. Mol. Microbiol. 39 (2001) 1443-1451
    • (2001) Mol. Microbiol. , vol.39 , pp. 1443-1451
    • Maier, A.1    Lorenz, P.2    Voncken, F.3    Clayton, C.4
  • 99
    • 2342539053 scopus 로고    scopus 로고
    • An Arabidopsis dynamin-related protein, DRP3A, controls both peroxisomal and mitochondrial division
    • Mano S., Nakamori C., Kondo M., Hayashi M., and Nishimura M. An Arabidopsis dynamin-related protein, DRP3A, controls both peroxisomal and mitochondrial division. Plant J. 38 (2004) 487-498
    • (2004) Plant J. , vol.38 , pp. 487-498
    • Mano, S.1    Nakamori, C.2    Kondo, M.3    Hayashi, M.4    Nishimura, M.5
  • 102
    • 0029792856 scopus 로고    scopus 로고
    • Redox-sensitive homodimerization of Pex11p: A proposed mechanism to regulate peroxisomal division
    • Marshall P.A., Dyer J.M., Quick M.E., and Goodman J.M. Redox-sensitive homodimerization of Pex11p: A proposed mechanism to regulate peroxisomal division. J. Cell Biol. 135 (1996) 123-137
    • (1996) J. Cell Biol. , vol.135 , pp. 123-137
    • Marshall, P.A.1    Dyer, J.M.2    Quick, M.E.3    Goodman, J.M.4
  • 103
    • 15944365201 scopus 로고    scopus 로고
    • Caveolin, cholesterol, and lipid bodies
    • Martin S., and Parton R.G. Caveolin, cholesterol, and lipid bodies. Semin. Cell Dev. Biol. 16 (2005) 163-174
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 163-174
    • Martin, S.1    Parton, R.G.2
  • 105
    • 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., Greenwood J.S., Fabian M.R., White K.A., and Mullen R.T. Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway. Plant Cell 17 (2005) 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
  • 106
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 107
    • 0035838984 scopus 로고    scopus 로고
    • Dendritic cells: Specialized and regulated antigen processing machines
    • Mellman I., and Steinman R.M. Dendritic cells: Specialized and regulated antigen processing machines. Cell 106 (2001) 255-258
    • (2001) Cell , vol.106 , pp. 255-258
    • Mellman, I.1    Steinman, R.M.2
  • 109
    • 0036200146 scopus 로고    scopus 로고
    • The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus
    • Morsomme P., and Riezman H. The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus. Dev. Cell. 2 (2002) 307-317
    • (2002) Dev. Cell. , vol.2 , pp. 307-317
    • Morsomme, P.1    Riezman, H.2
  • 110
    • 0042232377 scopus 로고    scopus 로고
    • The ER v-SNAREs are required for GPI-anchored protein sorting from other secretory proteins upon exit from the ER
    • Morsomme P., Prescianotto-Baschong C., and Riezman H. The ER v-SNAREs are required for GPI-anchored protein sorting from other secretory proteins upon exit from the ER. J. Cell Biol. 162 (2003) 403-412
    • (2003) J. Cell Biol. , vol.162 , pp. 403-412
    • Morsomme, P.1    Prescianotto-Baschong, C.2    Riezman, H.3
  • 111
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley A.M., and Hettema E.H. Yeast peroxisomes multiply by growth and division. J. Cell Biol. 178 (2007) 399-410
    • (2007) J. Cell Biol. , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 112
    • 46249130452 scopus 로고    scopus 로고
    • Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p
    • Motley A.M., Ward G.P., and Hettema E.H. Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. J. Cell Sci. 121 (2008) 1633-1640
    • (2008) J. Cell Sci. , vol.121 , pp. 1633-1640
    • Motley, A.M.1    Ward, G.P.2    Hettema, E.H.3
  • 113
    • 0034717248 scopus 로고    scopus 로고
    • The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail
    • Mullen R.T., and Trelease R.N. The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail. J. Biol. Chem. 275 (2000) 16337-16344
    • (2000) J. Biol. Chem. , vol.275 , pp. 16337-16344
    • Mullen, R.T.1    Trelease, R.N.2
  • 114
    • 33845341812 scopus 로고    scopus 로고
    • The ER-peroxisome connection in plants: Development of the "ER semi-autonomous peroxisome maturation and replication" model for plant peroxisome biogenesis
    • Mullen R.T., and Trelease R.N. The ER-peroxisome connection in plants: Development of the "ER semi-autonomous peroxisome maturation and replication" model for plant peroxisome biogenesis. Biochim. Biophys. Acta 1763 (2006) 1655-1668
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1655-1668
    • Mullen, R.T.1    Trelease, R.N.2
  • 115
    • 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., Lisenbee C.S., Miernyk J.A., and Trelease R.N. Peroxisomal membrane ascorbate peroxidase is sorted to a membranous network that resembles a subdomain of the endoplasmic reticulum. Plant Cell 11 (1999) 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
  • 116
    • 0035210089 scopus 로고    scopus 로고
    • How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins
    • Mullen R.T., Flynn C.R., and Trelease R.N. How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins. Trends Plant Sci. 6 (2001) 256-261
    • (2001) Trends Plant Sci. , vol.6 , pp. 256-261
    • Mullen, R.T.1    Flynn, C.R.2    Trelease, R.N.3
  • 117
    • 33745597353 scopus 로고    scopus 로고
    • Peroxisome biogenesis and the formation of multivesicular peroxisomes during tombusvirus infection: A role for ESCRT?
    • Mullen R.T., McCartney A.W., Flynn C.R., and Smith G.S.T. Peroxisome biogenesis and the formation of multivesicular peroxisomes during tombusvirus infection: A role for ESCRT?. Can. J. Bot. 84 (2006) 1-14
    • (2006) Can. J. Bot. , vol.84 , pp. 1-14
    • Mullen, R.T.1    McCartney, A.W.2    Flynn, C.R.3    Smith, G.S.T.4
  • 118
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muñiz M., Nuoffer C., Hauri H.P., and Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J. Cell Biol. 148 (2000) 925-930
    • (2000) J. Cell Biol. , vol.148 , pp. 925-930
    • Muñiz, M.1    Nuoffer, C.2    Hauri, H.P.3    Riezman, H.4
  • 119
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muñiz M., Morsomme P., and Riezman H. Protein sorting upon exit from the endoplasmic reticulum. Cell 104 (2001) 313-320
    • (2001) Cell , vol.104 , pp. 313-320
    • Muñiz, M.1    Morsomme, P.2    Riezman, H.3
  • 120
    • 0036796989 scopus 로고    scopus 로고
    • More than one way to replicate the Golgi apparatus
    • Munro S. More than one way to replicate the Golgi apparatus. Nat. Cell Biol. 4 (2002) E223-E224
    • (2002) Nat. Cell Biol. , vol.4
    • Munro, S.1
  • 121
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy D.J. The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Prog. Lipid Res. 40 (2001) 325-438
    • (2001) Prog. Lipid Res. , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 122
    • 41949118972 scopus 로고    scopus 로고
    • Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation
    • Nagotu S., Saraya R., Otzen M., Veenhuis M., and van der Klei I.J. Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation. Biochim. Biophys. Acta 1783 (2008) 760-769
    • (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
  • 123
    • 0033829447 scopus 로고    scopus 로고
    • Redistribution of Golgi stacks and other organelles during mitosis and cytokinesis in plant cells
    • Nebenführ A., Frohlick J.A., and Staehelin L.A. Redistribution of Golgi stacks and other organelles during mitosis and cytokinesis in plant cells. Plant Physiol. 124 (2000) 135-151
    • (2000) Plant Physiol. , vol.124 , pp. 135-151
    • Nebenführ, A.1    Frohlick, J.A.2    Staehelin, L.A.3
  • 124
    • 34547114033 scopus 로고    scopus 로고
    • Liver fatty acid-binding protein initiates budding of pre-chylomicron transport vesicles from intestinal endoplasmic reticulum
    • Neeli I., Siddiqi S.A., Siddiqi S., Mahan J., Lagakos W.S., Binas B., Gheyi T., Storch J., and Mansbach C.M. Liver fatty acid-binding protein initiates budding of pre-chylomicron transport vesicles from intestinal endoplasmic reticulum. J. Biol. Chem. 282 (2007) 17974-17984
    • (2007) J. Biol. Chem. , vol.282 , pp. 17974-17984
    • Neeli, I.1    Siddiqi, S.A.2    Siddiqi, S.3    Mahan, J.4    Lagakos, W.S.5    Binas, B.6    Gheyi, T.7    Storch, J.8    Mansbach, C.M.9
  • 126
    • 0015334792 scopus 로고
    • Peroxisomes in absorptive cells of mammalian small intestine
    • Novikoff P.M., and Novikoff A.B. Peroxisomes in absorptive cells of mammalian small intestine. J. Cell Biol. 53 (1972) 532-560
    • (1972) J. Cell Biol. , vol.53 , pp. 532-560
    • Novikoff, P.M.1    Novikoff, A.B.2
  • 127
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K., and Shaw J.M. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39 (2005) 503-536
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 128
    • 33750436981 scopus 로고    scopus 로고
    • In the yeast Hansenula polymorpha, peroxisome formation from the ER is independent of Pex19p, but involves the function of p24 proteins
    • Otzen M., Krikken A.M., Ozimek P.Z., Kurbatova E., Nagotu S., Veenhuis M., and van der Klei I.J. In the yeast Hansenula polymorpha, peroxisome formation from the ER is independent of Pex19p, but involves the function of p24 proteins. FEMS Yeast Res. 6 (2006) 1157-1166
    • (2006) FEMS Yeast Res. , vol.6 , pp. 1157-1166
    • Otzen, M.1    Krikken, A.M.2    Ozimek, P.Z.3    Kurbatova, E.4    Nagotu, S.5    Veenhuis, M.6    van der Klei, I.J.7
  • 129
    • 0442292206 scopus 로고    scopus 로고
    • Biogenesis of ER-to-Golgi transport carriers: Complex roles of COPII in ER export
    • Palmer K.J., and Stephens D.J. Biogenesis of ER-to-Golgi transport carriers: Complex roles of COPII in ER export. Trends Cell Biol. 14 (2004) 57-61
    • (2004) Trends Cell Biol. , vol.14 , pp. 57-61
    • Palmer, K.J.1    Stephens, D.J.2
  • 130
    • 15544363926 scopus 로고    scopus 로고
    • The role of microtubules in transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Palmer K.J., Watson P., and Stephens D.J. The role of microtubules in transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Biochem. Soc. Symp. 72 (2005) 1-13
    • (2005) Biochem. Soc. Symp. , vol.72 , pp. 1-13
    • Palmer, K.J.1    Watson, P.2    Stephens, D.J.3
  • 132
    • 0742269687 scopus 로고    scopus 로고
    • Golgi membranes remain segregated from the endoplasmic reticulum during mitosis in mammalian cells
    • Pecot M.Y., and Malhotra V. Golgi membranes remain segregated from the endoplasmic reticulum during mitosis in mammalian cells. Cell 116 (2004) 99-107
    • (2004) Cell , vol.116 , pp. 99-107
    • Pecot, M.Y.1    Malhotra, V.2
  • 135
    • 8844281541 scopus 로고    scopus 로고
    • Mutual control of membrane fission and fusion proteins
    • Peters C., Baars T.L., Bühler S., and Mayer A. Mutual control of membrane fission and fusion proteins. Cell 119 (2004) 667-678
    • (2004) Cell , vol.119 , pp. 667-678
    • Peters, C.1    Baars, T.L.2    Bühler, S.3    Mayer, A.4
  • 138
    • 0035215432 scopus 로고    scopus 로고
    • Novel protein domains and repeats in Drosophila melanogaster: Insights into structure, function, and evolution
    • Ponting C.P., Mott R., Bork P., and Copley R.R. Novel protein domains and repeats in Drosophila melanogaster: Insights into structure, function, and evolution. Genome Res. 11 (2001) 1996-2008
    • (2001) Genome Res. , vol.11 , pp. 1996-2008
    • Ponting, C.P.1    Mott, R.2    Bork, P.3    Copley, R.R.4
  • 141
    • 0035661564 scopus 로고    scopus 로고
    • Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit
    • Reilly B.A., Kraynack B.A., VanRheenen S.M., and Waters M.G. Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit. Mol. Biol. Cell 12 (2001) 3783-3796
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3783-3796
    • Reilly, B.A.1    Kraynack, B.A.2    VanRheenen, S.M.3    Waters, M.G.4
  • 142
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis
    • Rottensteiner H., Stein K., Sonnenhol E., and Erdmann R. Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis. Mol. Biol. Cell 14 (2003) 4316-4328
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 144
    • 0030810961 scopus 로고    scopus 로고
    • Brefeldin A interferes with peroxisomal protein sorting in the yeast Hansenula polymorpha
    • Salomons F.A., van der Klei I.J., Kram A.M., Harder W., and Veenhuis M. Brefeldin A interferes with peroxisomal protein sorting in the yeast Hansenula polymorpha. FEBS Lett. 411 (1997) 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
  • 145
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter R., Brugger B., Sandhoff R., Zellnig G., Leber A., Lampl M., Athenstaedt K., Hrastnik C., Eder S., Daum G., Paltauf F., Wieland F.T., et al. Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J. Cell Biol. 146 (1999) 741-754
    • (1999) J. Cell Biol. , vol.146 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10    Paltauf, F.11    Wieland, F.T.12
  • 146
    • 33745742255 scopus 로고    scopus 로고
    • Shared components of mitochondrial and peroxisomal division
    • Schrader M. Shared components of mitochondrial and peroxisomal division. Biochim. Biophys. Acta 1763 (2006) 531-541
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 531-541
    • Schrader, M.1
  • 147
    • 33845503273 scopus 로고    scopus 로고
    • Growth and division of peroxisomes
    • Schrader M., and Fahimi H.D. Growth and division of peroxisomes. Int. Rev. Cytol. 255 (2006) 237-290
    • (2006) Int. Rev. Cytol. , vol.255 , pp. 237-290
    • Schrader, M.1    Fahimi, H.D.2
  • 148
    • 41149158491 scopus 로고    scopus 로고
    • The peroxisome: Still a mysterious organelle
    • Schrader M., and Fahimi H.D. The peroxisome: Still a mysterious organelle. Histochem. Cell Biol. 129 (2008) 421-440
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 421-440
    • Schrader, M.1    Fahimi, H.D.2
  • 149
    • 35848932285 scopus 로고    scopus 로고
    • Mitochondria and peroxisomes: Are the "big brother" and the "little sister" closer than assumed?
    • Schrader M., and Yoon Y. Mitochondria and peroxisomes: Are the "big brother" and the "little sister" closer than assumed?. Bioessays 29 (2007) 1105-1114
    • (2007) Bioessays , vol.29 , pp. 1105-1114
    • Schrader, M.1    Yoon, Y.2
  • 151
    • 34249039944 scopus 로고    scopus 로고
    • A novel role of peroxin PEX6: Suppression of aging defects in mitochondria
    • Seo J.G., Lai C.Y., Miceli M.V., and Jazwinski S.M. A novel role of peroxin PEX6: Suppression of aging defects in mitochondria. Aging Cell 6 (2007) 405-413
    • (2007) Aging Cell , vol.6 , pp. 405-413
    • Seo, J.G.1    Lai, C.Y.2    Miceli, M.V.3    Jazwinski, S.M.4
  • 152
    • 0344119435 scopus 로고    scopus 로고
    • Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: A theoretical model
    • Shemesh T., Luini A., Malhotra V., Burger K.N., and Kozlov M.M. Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: A theoretical model. Biophys. J. 85 (2003) 3813-3827
    • (2003) Biophys. J. , vol.85 , pp. 3813-3827
    • Shemesh, T.1    Luini, A.2    Malhotra, V.3    Burger, K.N.4    Kozlov, M.M.5
  • 153
    • 0037439881 scopus 로고    scopus 로고
    • COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle
    • Siddiqi S.A., Gorelick F.S., Mahan J.T., and Mansbach C.M. COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle. J. Cell Sci. 116 (2003) 415-427
    • (2003) J. Cell Sci. , vol.116 , pp. 415-427
    • Siddiqi, S.A.1    Gorelick, F.S.2    Mahan, J.T.3    Mansbach, C.M.4
  • 155
    • 0034733570 scopus 로고    scopus 로고
    • Regulation of peroxisome size and number by fatty acid β-oxidation in the yeast Yarrowia lipolytica
    • Smith J.J., Brown T.W., Eitzen G.A., and Rachubinski R.A. Regulation of peroxisome size and number by fatty acid β-oxidation in the yeast Yarrowia lipolytica. J. Biol. Chem. 275 (2000) 20168-20178
    • (2000) J. Biol. Chem. , vol.275 , pp. 20168-20178
    • Smith, J.J.1    Brown, T.W.2    Eitzen, G.A.3    Rachubinski, R.A.4
  • 159
    • 0033601767 scopus 로고    scopus 로고
    • Peroxisome synthesis in the absence of preexisting peroxisomes
    • South S.T., and Gould S.J. Peroxisome synthesis in the absence of preexisting peroxisomes. J. Cell Biol. 144 (1999) 255
    • (1999) J. Cell Biol. , vol.144 , pp. 255
    • South, S.T.1    Gould, S.J.2
  • 160
    • 0034717704 scopus 로고    scopus 로고
    • Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis
    • South S.T., Sacksteder K.A., Li X.L., Liu Y., and Gould S.J. Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis. J. Cell Biol. 149 (2000) 1345-1359
    • (2000) J. Cell Biol. , vol.149 , pp. 1345-1359
    • South, S.T.1    Sacksteder, K.A.2    Li, X.L.3    Liu, Y.4    Gould, S.J.5
  • 161
    • 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., Baumgart E., and Gould S.J. Inactivation of the endoplasmic reticulum protein translocation factor, Sec61p, or its homolog, Ssh1p, does not affect peroxisome biogenesis. Proc. Natl Acad. Sci. USA 98 (2001) 12027-12031
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12027-12031
    • South, S.T.1    Baumgart, E.2    Gould, S.J.3
  • 163
    • 0037013167 scopus 로고    scopus 로고
    • Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells
    • Sütterlin C., Hsu P., Mallabiabarrena A., and Malhotra V. Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells. Cell 109 (2002) 359-369
    • (2002) Cell , vol.109 , pp. 359-369
    • Sütterlin, C.1    Hsu, P.2    Mallabiabarrena, A.3    Malhotra, V.4
  • 164
    • 0041810193 scopus 로고    scopus 로고
    • Peroxisomes start their life in the endoplasmic reticulum
    • Tabak H.F., Murk J.L., Braakman I., and Geuze H.J. Peroxisomes start their life in the endoplasmic reticulum. Traffic 4 (2003) 512-518
    • (2003) Traffic , vol.4 , pp. 512-518
    • Tabak, H.F.1    Murk, J.L.2    Braakman, I.3    Geuze, H.J.4
  • 166
    • 0141764783 scopus 로고    scopus 로고
    • Pex11-related proteins in peroxisome dynamics: A role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae
    • Tam Y.Y.C., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M., Aitchison J.D., and Rachubinski R.A. Pex11-related proteins in peroxisome dynamics: A role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae. Mol. Biol. Cell 14 (2003) 4089-4102
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4089-4102
    • Tam, Y.Y.C.1    Torres-Guzman, J.C.2    Vizeacoumar, F.J.3    Smith, J.J.4    Marelli, M.5    Aitchison, J.D.6    Rachubinski, R.A.7
  • 167
    • 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., Fagarasanu A., Fagarasanu M., and Rachubinski R.A. Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 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
  • 168
    • 0028911539 scopus 로고
    • The Hansenula polymorpha PER8 gene encodes a novel peroxisomal integral membrane protein involved in proliferation
    • Tan X., Waterham H.R., Veenhuis M., and Cregg J.M. The Hansenula polymorpha PER8 gene encodes a novel peroxisomal integral membrane protein involved in proliferation. J. Cell Biol. 128 (1995) 307-319
    • (1995) J. Cell Biol. , vol.128 , pp. 307-319
    • Tan, X.1    Waterham, H.R.2    Veenhuis, M.3    Cregg, J.M.4
  • 169
    • 0037462961 scopus 로고    scopus 로고
    • cDNA cloning and characterization of the third isoform of human peroxin Pex11p
    • Tanaka A., Okumoto K., and Fujiki Y. cDNA cloning and characterization of the third isoform of human peroxin Pex11p. Biochem. Biophys. Res. Commun. 300 (2003) 819-823
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 819-823
    • Tanaka, A.1    Okumoto, K.2    Fujiki, Y.3
  • 170
    • 27144513797 scopus 로고    scopus 로고
    • Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation
    • Thoms S., and Erdmann R. Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation. FEBS J. 272 (2005) 5169-5181
    • (2005) FEBS J. , vol.272 , pp. 5169-5181
    • Thoms, S.1    Erdmann, R.2
  • 171
    • 33745632081 scopus 로고    scopus 로고
    • Peroxisome biogenesis: The peroxisomal endomembrane system and the role of the ER
    • Titorenko V.I., and Mullen R.T. Peroxisome biogenesis: The peroxisomal endomembrane system and the role of the ER. J. Cell Biol. 174 (2006) 11-17
    • (2006) J. Cell Biol. , vol.174 , pp. 11-17
    • Titorenko, V.I.1    Mullen, R.T.2
  • 172
    • 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 Rachubinski R.A. Mutants of the yeast Yarrowia lipolytica defective in protein exit from the endoplasmic reticulum are also defective in peroxisome biogenesis. Mol. Cell. Biol. 18 (1998) 2789-2803
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2789-2803
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 173
    • 0031858109 scopus 로고    scopus 로고
    • The endoplasmic reticulum plays an essential role in peroxisome biogenesis
    • Titorenko V.I., and Rachubinski R.A. The endoplasmic reticulum plays an essential role in peroxisome biogenesis. Trends Biochem. Sci. 23 (1998) 231-233
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 231-233
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 174
    • 0034698778 scopus 로고    scopus 로고
    • Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p
    • Titorenko V.I., and Rachubinski R.A. Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p. J. Cell Biol. 150 (2000) 881-886
    • (2000) J. Cell Biol. , vol.150 , pp. 881-886
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 175
    • 0035176257 scopus 로고    scopus 로고
    • Dynamics of peroxisome assembly and function
    • Titorenko V.I., and Rachubinski R.A. Dynamics of peroxisome assembly and function. Trends Cell Biol. 11 (2001) 22-29
    • (2001) Trends Cell Biol. , vol.11 , pp. 22-29
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 177
    • 1442334370 scopus 로고    scopus 로고
    • The peroxisome: Orchestrating important developmental decisions from inside the cell
    • Titorenko V.I., and Rachubinski R.A. The peroxisome: Orchestrating important developmental decisions from inside the cell. J. Cell Biol. 164 (2004) 641-645
    • (2004) J. Cell Biol. , vol.164 , pp. 641-645
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 178
    • 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., Eitzen G.A., and Rachubinski R.A. Mutations in the PAY5 gene of the yeast Yarrowia lipolytica cause the accumulation of multiple subpopulations of peroxisomes. J. Biol. Chem. 271 (1996) 20307-20314
    • (1996) J. Biol. Chem. , vol.271 , pp. 20307-20314
    • Titorenko, V.I.1    Eitzen, G.A.2    Rachubinski, R.A.3
  • 179
    • 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., Ogrydziak D.M., and Rachubinski R.A. Four distinct secretory pathways serve protein secretion, cell surface growth, and peroxisome biogenesis in the yeast Yarrowia lipolytica. Mol. Cell. Biol. 17 (1997) 5210-5226
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5210-5226
    • Titorenko, V.I.1    Ogrydziak, D.M.2    Rachubinski, R.A.3
  • 180
    • 0034627808 scopus 로고    scopus 로고
    • Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica
    • Titorenko V.I., Chan H., and Rachubinski R.A. Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica. J. Cell Biol. 148 (2000) 29-44
    • (2000) J. Cell Biol. , vol.148 , pp. 29-44
    • Titorenko, V.I.1    Chan, H.2    Rachubinski, R.A.3
  • 182
    • 3042732458 scopus 로고    scopus 로고
    • Peroxisome biogenesis in the yeast Hansenula polymorpha: A structural and functional analysis
    • van der Klei I.J., and Veenhuis M. Peroxisome biogenesis in the yeast Hansenula polymorpha: A structural and functional analysis. Ann. N.Y. Acad. Sci. 804 (1996) 47-59
    • (1996) Ann. N.Y. Acad. Sci. , vol.804 , pp. 47-59
    • van der Klei, I.J.1    Veenhuis, M.2
  • 183
    • 33845321048 scopus 로고    scopus 로고
    • Yeast and filamentous fungi as model organisms in microbody research
    • van der Klei I.J., and Veenhuis M. Yeast and filamentous fungi as model organisms in microbody research. Biochim. Biophys. Acta 1763 (2006) 1364-1373
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1364-1373
    • van der Klei, I.J.1    Veenhuis, M.2
  • 186
    • 0028845973 scopus 로고
    • Localization of peroxisomal 3-oxoacyl-CoA thiolase in particles of varied density in rat liver: Implications for peroxisome biogenesis
    • van Roermund C.W.T., van den Berg M., and Wanders R.J.A. Localization of peroxisomal 3-oxoacyl-CoA thiolase in particles of varied density in rat liver: Implications for peroxisome biogenesis. Biochim. Biophys. Acta 1245 (1995) 348-358
    • (1995) Biochim. Biophys. Acta , vol.1245 , pp. 348-358
    • van Roermund, C.W.T.1    van den Berg, M.2    Wanders, R.J.A.3
  • 187
    • 0034617992 scopus 로고    scopus 로고
    • Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae
    • van Roermund C.W.T., Tabak H.F., van den Berg M., Wanders R.J.A., and Hettema E.H. Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae. J. Cell Biol. 150 (2000) 489-498
    • (2000) J. Cell Biol. , vol.150 , pp. 489-498
    • van Roermund, C.W.T.1    Tabak, H.F.2    van den Berg, M.3    Wanders, R.J.A.4    Hettema, E.H.5
  • 188
    • 0026471712 scopus 로고
    • The VPS1 protein, a homolog of dynamin required for vacuolar protein sorting in Saccharomyces cerevisiae, is a GTPase with two functionally separable domains
    • Vater C.A., Raymond C.K., Ekena K., Howald-Stevenson I., and Stevens T.H. The VPS1 protein, a homolog of dynamin required for vacuolar protein sorting in Saccharomyces cerevisiae, is a GTPase with two functionally separable domains. J. Cell Biol. 119 (1992) 773-786
    • (1992) J. Cell Biol. , vol.119 , pp. 773-786
    • Vater, C.A.1    Raymond, C.K.2    Ekena, K.3    Howald-Stevenson, I.4    Stevens, T.H.5
  • 189
    • 0025103805 scopus 로고
    • Peroxisomal assembly: Membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii
    • Veenhuis M., and Goodman J.M. Peroxisomal assembly: Membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii. J. Cell Sci. 96 (1990) 583-590
    • (1990) J. Cell Sci. , vol.96 , pp. 583-590
    • Veenhuis, M.1    Goodman, J.M.2
  • 190
    • 0038746700 scopus 로고    scopus 로고
    • YHR150w and YDR479c encode peroxisomal integral membrane proteins involved in the regulation of peroxisome number, size, and distribution in Saccharomyces cerevisiae
    • Vizeacoumar F.J., Torres-Guzman J.C., Tam Y.Y., Aitchison J.D., and Rachubinski R.A. YHR150w and YDR479c encode peroxisomal integral membrane proteins involved in the regulation of peroxisome number, size, and distribution in Saccharomyces cerevisiae. J. Cell Biol. 161 (2003) 321-332
    • (2003) J. Cell Biol. , vol.161 , pp. 321-332
    • Vizeacoumar, F.J.1    Torres-Guzman, J.C.2    Tam, Y.Y.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 191
    • 33744960494 scopus 로고    scopus 로고
    • The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner
    • Vizeacoumar F.J., Vreden W.N., Fagarasanu M., Eitzen G.A., Aitchison J.D., and Rachubinski R.A. The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner. J. Biol. Chem. 281 (2006) 12817-12823
    • (2006) J. Biol. Chem. , vol.281 , pp. 12817-12823
    • Vizeacoumar, F.J.1    Vreden, W.N.2    Fagarasanu, M.3    Eitzen, G.A.4    Aitchison, J.D.5    Rachubinski, R.A.6
  • 192
    • 0038620481 scopus 로고    scopus 로고
    • New perspectives on the regulation of intermembrane glycerophospholipid traffic
    • Voelker D.R. New perspectives on the regulation of intermembrane glycerophospholipid traffic. J. Lipid Res. 44 (2003) 441-449
    • (2003) J. Lipid Res. , vol.44 , pp. 441-449
    • Voelker, D.R.1
  • 193
    • 2342597726 scopus 로고    scopus 로고
    • Genetic analysis of intracellular aminoglycerophospholipid traffic
    • Voelker D.R. Genetic analysis of intracellular aminoglycerophospholipid traffic. Biochem. Cell Biol. 82 (2004) 156-169
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 156-169
    • Voelker, D.R.1
  • 194
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker D.R. Bridging gaps in phospholipid transport. Trends Biochem. Sci. 30 (2005) 396-404
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 195
    • 33847199803 scopus 로고    scopus 로고
    • Sheets, ribbons and tubules-How organelles get their shape
    • Voeltz G.K., and Prinz W.A. Sheets, ribbons and tubules-How organelles get their shape. Nat. Rev. Mol. Cell Biol. 8 (2007) 258-264
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 258-264
    • Voeltz, G.K.1    Prinz, W.A.2
  • 196
    • 0041816190 scopus 로고    scopus 로고
    • Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes
    • Voncken F., van Hellemond J.J., Pfisterer I., Maier A., Hillmer S., and Clayton C. Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes. J. Biol. Chem. 278 (2003) 35299-35310
    • (2003) J. Biol. Chem. , vol.278 , pp. 35299-35310
    • Voncken, F.1    van Hellemond, J.J.2    Pfisterer, I.3    Maier, A.4    Hillmer, S.5    Clayton, C.6
  • 197
    • 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., Kragt A., Tabak H.F., and Distel B. Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- and COPII-mediated vesicular transport. J. Cell Sci. 114 (2001) 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
  • 198
    • 0032859657 scopus 로고    scopus 로고
    • Evaluation of acyl coenzyme A oxidase (Aox) isozyme function in the n-alkane-assimilating yeast Yarrowia lipolytica
    • Wang H.J., Le Dall M.-T., Waché Y., Laroche C., Belin J.-M., Gaillardin C., and Nicaud J.-M. Evaluation of acyl coenzyme A oxidase (Aox) isozyme function in the n-alkane-assimilating yeast Yarrowia lipolytica. J. Bacteriol. 181 (1999) 5140-5148
    • (1999) J. Bacteriol. , vol.181 , pp. 5140-5148
    • Wang, H.J.1    Le Dall, M.-T.2    Waché, Y.3    Laroche, C.4    Belin, J.-M.5    Gaillardin, C.6    Nicaud, J.-M.7
  • 199
    • 33746054560 scopus 로고    scopus 로고
    • 2+-mediated membrane fusion during C. elegans spermatogenesis
    • 2+-mediated membrane fusion during C. elegans spermatogenesis. J. Cell Sci. 119 (2006) 2552-2562
    • (2006) J. Cell Sci. , vol.119 , pp. 2552-2562
    • Washington, N.L.1    Ward, S.2
  • 200
    • 3142624697 scopus 로고    scopus 로고
    • Differential ER exit in yeast and mammalian cells
    • Watanabe R., and Riezman H. Differential ER exit in yeast and mammalian cells. Curr. Opin. Cell Biol. 16 (2004) 350-355
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 350-355
    • Watanabe, R.1    Riezman, H.2
  • 201
    • 0037147230 scopus 로고    scopus 로고
    • Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast
    • Watanabe R., Funato K., Venkataraman K., Futerman A.H., and Riezman H. Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast. J. Biol. Chem. 277 (2002) 49538-49544
    • (2002) J. Biol. Chem. , vol.277 , pp. 49538-49544
    • Watanabe, R.1    Funato, K.2    Venkataraman, K.3    Futerman, A.H.4    Riezman, H.5
  • 203
    • 20544471158 scopus 로고    scopus 로고
    • ER-to-Golgi transport: Form and formation of vesicular and tubular carriers
    • Watson P., and Stephens D.J. ER-to-Golgi transport: Form and formation of vesicular and tubular carriers. Biochim. Biophys. Acta 1744 (2005) 304-315
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 304-315
    • Watson, P.1    Stephens, D.J.2
  • 204
    • 0035846977 scopus 로고    scopus 로고
    • Differential induction of peroxisomal populations in subcellular fractions of rat liver
    • Wilcke M., and Alexson S.E. Differential induction of peroxisomal populations in subcellular fractions of rat liver. Biochim. Biophys. Acta 1544 (2001) 358-369
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 358-369
    • Wilcke, M.1    Alexson, S.E.2
  • 205
    • 0028939995 scopus 로고
    • Novel peroxisomal populations in subcellular fractions from rat liver. Implications for peroxisome structure and biogenesis
    • Wilcke M., Hultenby K., and Alexson S.E.H. Novel peroxisomal populations in subcellular fractions from rat liver. Implications for peroxisome structure and biogenesis. J. Biol. Chem. 270 (1995) 6949-6958
    • (1995) J. Biol. Chem. , vol.270 , pp. 6949-6958
    • Wilcke, M.1    Hultenby, K.2    Alexson, S.E.H.3
  • 206
    • 22044444453 scopus 로고    scopus 로고
    • The control of peroxisome number and size during division and proliferation
    • Yan M., Rayapuram N., and Subramani S. The control of peroxisome number and size during division and proliferation. Curr. Opin. Cell Biol. 17 (2005) 376-383
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 376-383
    • Yan, M.1    Rayapuram, N.2    Subramani, S.3
  • 207
    • 41649109400 scopus 로고    scopus 로고
    • Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris
    • Yan M., Rachubinski D.A., Joshi S., Rachubinski R.A., and Subramani S. Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris. Mol. Biol. Cell. 19 (2008) 885-898
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 885-898
    • Yan, M.1    Rachubinski, D.A.2    Joshi, S.3    Rachubinski, R.A.4    Subramani, S.5
  • 208
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J., and Kozlov M.M. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7 (2006) 9-19
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 209
    • 0026082909 scopus 로고
    • Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae
    • Zinser E., Sperka-Gottlieb C.D., Fasch E.V., Kohlwein S.D., Paltauf F., and Daum G. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae. J. Bacteriol. 173 (1991) 2026-2034
    • (1991) J. Bacteriol. , vol.173 , pp. 2026-2034
    • Zinser, E.1    Sperka-Gottlieb, C.D.2    Fasch, E.V.3    Kohlwein, S.D.4    Paltauf, F.5    Daum, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.