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Volumn 25, Issue 2, 2015, Pages 152-162

COPII coat composition is actively regulated by luminal cargo maturation

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; PROTEIN BINDING;

EID: 84921363168     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2014.11.039     Document Type: Article
Times cited : (57)

References (50)
  • 1
    • 77953642000 scopus 로고    scopus 로고
    • Protein sorting receptors in the early secretory pathway
    • J. Dancourt, and C. Barlowe Protein sorting receptors in the early secretory pathway Annu. Rev. Biochem. 79 2010 777 802
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 777-802
    • Dancourt, J.1    Barlowe, C.2
  • 2
    • 78651066551 scopus 로고    scopus 로고
    • COPII-mediated vesicle formation at a glance
    • D. Jensen, and R. Schekman COPII-mediated vesicle formation at a glance J. Cell Sci. 124 2011 1 4
    • (2011) J. Cell Sci. , vol.124 , pp. 1-4
    • Jensen, D.1    Schekman, R.2
  • 3
    • 84893329888 scopus 로고    scopus 로고
    • The back and forth of cargo exit from the endoplasmic reticulum
    • Y. Geva, and M. Schuldiner The back and forth of cargo exit from the endoplasmic reticulum Curr. Biol. 24 2014 R130 R136
    • (2014) Curr. Biol. , vol.24 , pp. R130-R136
    • Geva, Y.1    Schuldiner, M.2
  • 4
    • 70349842313 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors
    • A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Second Edition Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • M.A.J. Ferguson, T. Kinoshita, and G.W. Hart Glycosylphosphatidylinositol anchors A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Essentials of Glycobiology Second Edition 2009 Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • (2009) Essentials of Glycobiology
    • Ferguson, M.A.J.1    Kinoshita, T.2    Hart, G.W.3
  • 5
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • M. Muñiz, P. Morsomme, and H. Riezman 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
  • 6
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles
    • T.L. Doering, and R. Schekman GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles EMBO J. 15 1996 182 191
    • (1996) EMBO J. , vol.15 , pp. 182-191
    • Doering, T.L.1    Schekman, R.2
  • 9
    • 84862189303 scopus 로고    scopus 로고
    • GPI-anchor remodeling: Potential functions of GPI-anchors in intracellular trafficking and membrane dynamics
    • M. Fujita, and T. Kinoshita GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics Biochim. Biophys. Acta 1821 2012 1050 1058
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1050-1058
    • Fujita, M.1    Kinoshita, T.2
  • 11
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • M. Muñiz, C. Nuoffer, H.P. Hauri, and H. Riezman 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
  • 15
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • F. Schimmöller, B. Singer-Krüger, S. Schröder, U. Krüger, C. Barlowe, and H. Riezman The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi EMBO J. 14 1995 1329 1339
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmöller, F.1    Singer-Krüger, B.2    Schröder, S.3    Krüger, U.4    Barlowe, C.5    Riezman, H.6
  • 16
    • 0035900761 scopus 로고    scopus 로고
    • Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex
    • W.J. Belden, and C. Barlowe Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex J. Biol. Chem. 276 2001 43040 43048
    • (2001) J. Biol. Chem. , vol.276 , pp. 43040-43048
    • Belden, W.J.1    Barlowe, C.2
  • 20
    • 0039517273 scopus 로고    scopus 로고
    • Localization and recycling of gp27 (hp24gamma3): Complex formation with other p24 family members
    • J. Füllekrug, T. Suganuma, B.L. Tang, W. Hong, B. Storrie, and T. Nilsson Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members Mol. Biol. Cell 10 1999 1939 1955
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1939-1955
    • Füllekrug, J.1    Suganuma, T.2    Tang, B.L.3    Hong, W.4    Storrie, B.5    Nilsson, T.6
  • 21
    • 84891377648 scopus 로고    scopus 로고
    • Isoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteins
    • R. Hirata, C. Nihei, and A. Nakano Isoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteins J. Biol. Chem. 288 2013 37057 37070
    • (2013) J. Biol. Chem. , vol.288 , pp. 37057-37070
    • Hirata, R.1    Nihei, C.2    Nakano, A.3
  • 22
    • 0037112755 scopus 로고    scopus 로고
    • Cargo selection into COPII vesicles is driven by the Sec24p subunit
    • E. Miller, B. Antonny, S. Hamamoto, and R. Schekman Cargo selection into COPII vesicles is driven by the Sec24p subunit EMBO J. 21 2002 6105 6113
    • (2002) EMBO J. , vol.21 , pp. 6105-6113
    • Miller, E.1    Antonny, B.2    Hamamoto, S.3    Schekman, R.4
  • 23
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • E.A. Miller, T.H. Beilharz, P.N. Malkus, M.C. Lee, S. Hamamoto, L. Orci, and R. Schekman Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles Cell 114 2003 497 509
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 24
    • 0034722347 scopus 로고    scopus 로고
    • Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae
    • Y. Shimoni, T. Kurihara, M. Ravazzola, M. Amherdt, L. Orci, and R. Schekman Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae J. Cell Biol. 151 2000 973 984
    • (2000) J. Cell Biol. , vol.151 , pp. 973-984
    • Shimoni, Y.1    Kurihara, T.2    Ravazzola, M.3    Amherdt, M.4    Orci, L.5    Schekman, R.6
  • 25
    • 84880583267 scopus 로고    scopus 로고
    • Vesicle-mediated export from the ER: COPII coat function and regulation
    • J.G. D'Arcangelo, K.R. Stahmer, and E.A. Miller Vesicle-mediated export from the ER: COPII coat function and regulation Biochim. Biophys. Acta 1833 2013 2464 2472
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2464-2472
    • D'Arcangelo, J.G.1    Stahmer, K.R.2    Miller, E.A.3
  • 26
    • 70349838223 scopus 로고    scopus 로고
    • GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi
    • M. Fujita, Y. Maeda, M. Ra, Y. Yamaguchi, R. Taguchi, and T. Kinoshita GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi Cell 139 2009 352 365
    • (2009) Cell , vol.139 , pp. 352-365
    • Fujita, M.1    Maeda, Y.2    Ra, M.3    Yamaguchi, Y.4    Taguchi, R.5    Kinoshita, T.6
  • 28
    • 0034637525 scopus 로고    scopus 로고
    • YLL031c belongs to a novel family of membrane proteins involved in the transfer of ethanolaminephosphate onto the core structure of glycosylphosphatidylinositol anchors in yeast
    • I. Flury, A. Benachour, and A. Conzelmann YLL031c belongs to a novel family of membrane proteins involved in the transfer of ethanolaminephosphate onto the core structure of glycosylphosphatidylinositol anchors in yeast J. Biol. Chem. 275 2000 24458 24465
    • (2000) J. Biol. Chem. , vol.275 , pp. 24458-24465
    • Flury, I.1    Benachour, A.2    Conzelmann, A.3
  • 29
    • 84908653870 scopus 로고    scopus 로고
    • Cdc1 removes the ethanolamine phosphate of the first mannose of GPI anchors and thereby facilitates the integration of GPI proteins into the yeast cell wall
    • H.M. Vazquez, C. Vionnet, C. Roubaty, and A. Conzelmann Cdc1 removes the ethanolamine phosphate of the first mannose of GPI anchors and thereby facilitates the integration of GPI proteins into the yeast cell wall Mol. Biol. Cell 25 2014 3375 3388
    • (2014) Mol. Biol. Cell , vol.25 , pp. 3375-3388
    • Vazquez, H.M.1    Vionnet, C.2    Roubaty, C.3    Conzelmann, A.4
  • 30
    • 0035423555 scopus 로고    scopus 로고
    • ER export: Public transportation by the COPII coach
    • B. Antonny, and R. Schekman ER export: public transportation by the COPII coach Curr. Opin. Cell Biol. 13 2001 438 443
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 438-443
    • Antonny, B.1    Schekman, R.2
  • 31
    • 40749160804 scopus 로고    scopus 로고
    • Lipid remodeling of GPI-anchored proteins and its function
    • M. Fujita, and Y. Jigami Lipid remodeling of GPI-anchored proteins and its function Biochim. Biophys. Acta 1780 2008 410 420
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 410-420
    • Fujita, M.1    Jigami, Y.2
  • 32
    • 84902436526 scopus 로고    scopus 로고
    • The α-helical region in p24γ2 subunit of p24 protein cargo receptor is pivotal for the recognition and transport of glycosylphosphatidylinositol-anchored proteins
    • R. Theiler, M. Fujita, M. Nagae, Y. Yamaguchi, Y. Maeda, and T. Kinoshita The α-helical region in p24γ2 subunit of p24 protein cargo receptor is pivotal for the recognition and transport of glycosylphosphatidylinositol-anchored proteins J. Biol. Chem. 289 2014 16835 16843
    • (2014) J. Biol. Chem. , vol.289 , pp. 16835-16843
    • Theiler, R.1    Fujita, M.2    Nagae, M.3    Yamaguchi, Y.4    Maeda, Y.5    Kinoshita, T.6
  • 33
    • 77956016935 scopus 로고    scopus 로고
    • Synthetic glycosylphosphatidylinositol as tools for glycoparasitology research
    • N. Azzouz, F. Kamena, and P.H. Seeberger Synthetic glycosylphosphatidylinositol as tools for glycoparasitology research OMICS 14 2010 445 454
    • (2010) OMICS , vol.14 , pp. 445-454
    • Azzouz, N.1    Kamena, F.2    Seeberger, P.H.3
  • 34
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • M.J. Kuehn, J.M. Herrmann, and R. Schekman COPII-cargo interactions direct protein sorting into ER-derived transport vesicles Nature 391 1998 187 190
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 35
    • 35549004893 scopus 로고    scopus 로고
    • Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31
    • X. Bi, J.D. Mancias, and J. Goldberg Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31 Dev. Cell 13 2007 635 645
    • (2007) Dev. Cell , vol.13 , pp. 635-645
    • Bi, X.1    Mancias, J.D.2    Goldberg, J.3
  • 36
    • 84858323525 scopus 로고    scopus 로고
    • ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p
    • A. Copic, C.F. Latham, M.A. Horlbeck, J.G. D'Arcangelo, and E.A. Miller ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p Science 335 2012 1359 1362
    • (2012) Science , vol.335 , pp. 1359-1362
    • Copic, A.1    Latham, C.F.2    Horlbeck, M.A.3    D'Arcangelo, J.G.4    Miller, E.A.5
  • 37
    • 15544367075 scopus 로고    scopus 로고
    • Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis
    • K. Sato, and A. Nakano Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis Nat. Struct. Mol. Biol. 12 2005 167 174
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 167-174
    • Sato, K.1    Nakano, A.2
  • 38
    • 70350763840 scopus 로고    scopus 로고
    • Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane
    • K.V. Tabata, K. Sato, T. Ide, T. Nishizaka, A. Nakano, and H. Noji Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane EMBO J. 28 2009 3279 3289
    • (2009) EMBO J. , vol.28 , pp. 3279-3289
    • Tabata, K.V.1    Sato, K.2    Ide, T.3    Nishizaka, T.4    Nakano, A.5    Noji, H.6
  • 39
    • 40849088168 scopus 로고    scopus 로고
    • The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus
    • A. Aguilera-Romero, J. Kaminska, A. Spang, H. Riezman, and M. Muñiz The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus J. Cell Biol. 180 2008 713 720
    • (2008) J. Cell Biol. , vol.180 , pp. 713-720
    • Aguilera-Romero, A.1    Kaminska, J.2    Spang, A.3    Riezman, H.4    Muñiz, M.5
  • 41
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • A. Bielli, C.J. Haney, G. Gabreski, S.C. Watkins, S.I. Bannykh, and M. Aridor Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission J. Cell Biol. 171 2005 919 924
    • (2005) J. Cell Biol. , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 42
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • M.C. Lee, L. Orci, S. Hamamoto, E. Futai, M. Ravazzola, and R. Schekman 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
  • 43
    • 0033591254 scopus 로고    scopus 로고
    • Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity
    • A. Benachour, G. Sipos, I. Flury, F. Reggiori, E. Canivenc-Gansel, C. Vionnet, A. Conzelmann, and M. Benghezal Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity J. Biol. Chem. 274 1999 15251 15261
    • (1999) J. Biol. Chem. , vol.274 , pp. 15251-15261
    • Benachour, A.1    Sipos, G.2    Flury, I.3    Reggiori, F.4    Canivenc-Gansel, E.5    Vionnet, C.6    Conzelmann, A.7    Benghezal, M.8
  • 46
    • 0035736439 scopus 로고    scopus 로고
    • CDNA cloning, genomic organization and expression of the novel human metallophosphoesterase gene MPPE1 on chromosome 18p11.2
    • J.T. Vuoristo, and L. Ala-Kokko cDNA cloning, genomic organization and expression of the novel human metallophosphoesterase gene MPPE1 on chromosome 18p11.2 Cytogenet. Cell Genet. 95 2001 60 63
    • (2001) Cytogenet. Cell Genet. , vol.95 , pp. 60-63
    • Vuoristo, J.T.1    Ala-Kokko, L.2
  • 47
    • 8544278140 scopus 로고    scopus 로고
    • Functional dependence on calcineurin by variants of the Saccharomyces cerevisiae vacuolar Ca2+/H+ exchanger Vcx1p
    • J.K. Pittman, N.H. Cheng, T. Shigaki, M. Kunta, and K.D. Hirschi Functional dependence on calcineurin by variants of the Saccharomyces cerevisiae vacuolar Ca2+/H+ exchanger Vcx1p Mol. Microbiol. 54 2004 1104 1116
    • (2004) Mol. Microbiol. , vol.54 , pp. 1104-1116
    • Pittman, J.K.1    Cheng, N.H.2    Shigaki, T.3    Kunta, M.4    Hirschi, K.D.5
  • 48
    • 31944447156 scopus 로고    scopus 로고
    • Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins
    • M. Fujita, T. Yoko-O, and Y. Jigami Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins Mol. Biol. Cell 17 2006 834 850
    • (2006) Mol. Biol. Cell , vol.17 , pp. 834-850
    • Fujita, M.1    Yoko-O, T.2    Jigami, Y.3
  • 49
    • 80053353907 scopus 로고    scopus 로고
    • Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic
    • S. Chen, H. Cai, S.K. Park, S. Menon, C.L. Jackson, and S. Ferro-Novick Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic Mol. Biol. Cell 22 2011 3634 3644
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3634-3644
    • Chen, S.1    Cai, H.2    Park, S.K.3    Menon, S.4    Jackson, C.L.5    Ferro-Novick, S.6
  • 50
    • 0033789168 scopus 로고    scopus 로고
    • Analysis of ceramides present in glycosylphosphatidylinositol anchored proteins of Saccharomyces cerevisiae
    • I. Guillas, M. Pfefferli, and A. Conzelmann Analysis of ceramides present in glycosylphosphatidylinositol anchored proteins of Saccharomyces cerevisiae Methods Enzymol. 312 2000 506 515
    • (2000) Methods Enzymol. , vol.312 , pp. 506-515
    • Guillas, I.1    Pfefferli, M.2    Conzelmann, A.3


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