메뉴 건너뛰기




Volumn 167, Issue 6, 2004, Pages 1099-1112

Quantitative mass spectrometry reveals a role for the GTPase Rho 1 p in actin organization on the peroxisome membrane

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MEMBRANE PROTEIN; PROTEIN PEX25P; PROTEIN RHO1P; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 19944426486     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200404119     Document Type: Article
Times cited : (133)

References (38)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and M. Mann. 2003. Mass spectrometry-based proteomics. Nature. 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 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
    • 0013788558 scopus 로고
    • Combined biochemical and morphological study of particulate fractions from rat liver. Analysis of preparations enriched in lysosomes or in particles containing urate oxidase, D-amino acid oxidase, and catalase
    • Baudhuin, P., H. Beaufay, and C. de Duve. 1965. Combined biochemical and morphological study of particulate fractions from rat liver. Analysis of preparations enriched in lysosomes or in particles containing urate oxidase, D-amino acid oxidase, and catalase. J. Cell Biol. 26:219-243.
    • (1965) J. Cell Biol. , vol.26 , pp. 219-243
    • Baudhuin, P.1    Beaufay, H.2    De Duve, C.3
  • 5
    • 0037632981 scopus 로고    scopus 로고
    • Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes
    • Birschmann, I., A.K. Stroobants, M. van den Berg, A. Schafer, K. Rosenkranz, W.H. Kunau, and H.F. Tabak. 2003. Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes. Mol. Biol. Cell. 14:2226-2236.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 2226-2236
    • Birschmann, I.1    Stroobants, A.K.2    Van Den Berg, M.3    Schafer, A.4    Rosenkranz, K.5    Kunau, W.H.6    Tabak, H.F.7
  • 8
    • 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
  • 9
    • 11244296966 scopus 로고
    • Exploring cells with a centrifuge
    • J. Lindsten, editor. World Scientific Publishing Co., London
    • de Duve, C. 1992. Exploring cells with a centrifuge. In Nobel Lectures in Physiology 1971-1980. J. Lindsten, editor. World Scientific Publishing Co., London. 152-172.
    • (1992) Nobel Lectures in Physiology 1971-1980 , pp. 152-172
    • De Duve, C.1
  • 10
    • 0345255690 scopus 로고    scopus 로고
    • Receptor internalization in yeast requires the Tor2-Rho1 signaling pathway
    • deHart, A.K., J.D. Schnell, D.A. Allen, J.Y. Tsai, and L. Hicke. 2003. Receptor internalization in yeast requires the Tor2-Rho1 signaling pathway. Mol. Biol. Cell. 14:4676-4684.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4676-4684
    • DeHart, A.K.1    Schnell, J.D.2    Allen, D.A.3    Tsai, J.Y.4    Hicke, L.5
  • 11
    • 0035886714 scopus 로고    scopus 로고
    • Rho1p and Cdc42p act after Ypt7p to regulate vacuole docking
    • Eitzen, G., N. Thorngren, and W. Wickner. 2001. Rho1p and Cdc42p act after Ypt7p to regulate vacuole docking. EMBO J. 20:5650-5656.
    • (2001) EMBO J. , vol.20 , pp. 5650-5656
    • Eitzen, G.1    Thorngren, N.2    Wickner, W.3
  • 12
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson, M.J., and C.A. Kaiser. 1996. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol. Biol. Cell. 7:1043-1058.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 13
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotopecoded affinity tags
    • Gygi, S.P., B. Rist, S.A. Gerber, F. Turecek, M.H. Gelb. and R. Aebersold. 1999. Quantitative analysis of complex protein mixtures using isotopecoded affinity tags. Nat. Biotechnol. 17:994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 14
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science. 279:509-514.
    • (1998) Science. , vol.279 , pp. 509-514
    • Hall, A.1
  • 15
    • 0026098352 scopus 로고
    • A novel protein kinase homolog essential for protein sorting to the yeast lysosome-like vacuole
    • Herman, P.K., J.H. Stack, J.A. DeModena, and S.D. Emr. 1991. A novel protein kinase homolog essential for protein sorting to the yeast lysosome-like vacuole. Cell. 64:425-437.
    • (1991) Cell , vol.64 , pp. 425-437
    • Herman, P.K.1    Stack, J.H.2    DeModena, J.A.3    Emr, S.D.4
  • 17
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner, D., M. van den Berg, P. Philippsen, H.F. Tabak, and E.H. Hettema. 2001. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155:979-990.
    • (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
  • 18
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R., and T.C. Südhof. 1999. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68:863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 19
    • 0027756102 scopus 로고
    • A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmo-sensitive mutant of Saccharomyces cerevisiae
    • Larsson, K., R. Ansell, P. Eriksson, and L. Adler. 1993. A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmo-sensitive mutant of Saccharomyces cerevisiae. Mol. Microbiol. 10:1101-1111.
    • (1993) Mol. Microbiol. , vol.10 , pp. 1101-1111
    • Larsson, K.1    Ansell, R.2    Eriksson, P.3    Adler, L.4
  • 20
    • 0031782969 scopus 로고    scopus 로고
    • Cell polarity and morphogenesis in budding yeast
    • Madden, K., and M. Snyder. 1998. Cell polarity and morphogenesis in budding yeast. Annu. Rev. Microbiol. 52:687-744.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 687-744
    • Madden, K.1    Snyder, M.2
  • 21
    • 0036437326 scopus 로고    scopus 로고
    • Membrane fusion in eukaryotic cells
    • Mayer, A. 2002. Membrane fusion in eukaryotic cells. Annu. Rev. Cell Dev. Biol. 18:289-314.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 289-314
    • Mayer, A.1
  • 22
    • 0032483384 scopus 로고    scopus 로고
    • Ran and nuclear transport
    • Moore, M.S. 1998. Ran and nuclear transport. J. Biol. Chem. 273:22857-22860.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22857-22860
    • Moore, M.S.1
  • 24
    • 0030048509 scopus 로고    scopus 로고
    • Covalent attachment of FAD to the yeast succinate dehydrogenase flavoprotein requires import into mitochondria, presequence removal, and folding
    • Robinson, K.M., and B.D. Lemire. 1996. Covalent attachment of FAD to the yeast succinate dehydrogenase flavoprotein requires import into mitochondria, presequence removal, and folding. J. Biol. Chem. 271:4055-4060.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4055-4060
    • Robinson, K.M.1    Lemire, B.D.2
  • 25
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of Pex11p and the novel Pex25p and Pex27p in peroxisome biogenesis
    • Rottensteiner, H., K. Stein, E. Sonnenhol, and R. Erdmann. 2003. Conserved function of Pex11p and the novel Pex25p and Pex27p in peroxisome biogenesis. Mol. Biol. Cell. 14:4316-4328.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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., J.C. Torres-Guzman, F.J. Vizeacoumar, J.J. Smith, M. Marelli, J.D. Aitchison, and R.A. Rachubinski. 2003. 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. 14:4089-4102.
    • (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
  • 30
    • 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
  • 32
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 33
    • 0023361695 scopus 로고
    • Proliferation of microbodies in Saccharomyces cerevisiae
    • Veenhuis, M., M. Mateblowski, W.H. Kunau, and W. Harder. 1987. Proliferation of microbodies in Saccharomyces cerevisiae. Yeast. 3:77-84.
    • (1987) Yeast , vol.3 , pp. 77-84
    • Veenhuis, M.1    Mateblowski, M.2    Kunau, W.H.3    Harder, W.4
  • 35
    • 0742288046 scopus 로고    scopus 로고
    • Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae
    • Vizeacoumar, F.J., J.C. Torres-Guzman, D. Bouard, J.D. Aitchison, and R.A. Rachubinski. 2003. Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae. Mol. Biol. Cell. 15:665-677.
    • (2003) Mol. Biol. Cell. , vol.15 , pp. 665-677
    • Vizeacoumar, F.J.1    Torres-Guzman, J.C.2    Bouard, D.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 36
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.