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Volumn 106, Issue 50, 2009, Pages 21121-21125

Golgi protein FAPP2 tubulates membranes

Author keywords

Membrane tubulation; PH domain; Phosphatidylinositol 4 phosphate; Small angle x ray scattering (SAXS); Trans Golgi network

Indexed keywords

ADAPTOR PROTEIN; FOUR PHOSPHATE ADAPTOR PROTEIN 2; PHOSPHATIDYLINOSITIDE; UNCLASSIFIED DRUG;

EID: 75849125878     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911789106     Document Type: Article
Times cited : (53)

References (32)
  • 1
    • 41549120213 scopus 로고    scopus 로고
    • Regulation of membrane trafficking in polarized epithelial cells
    • Fölsch H (2008) Regulation of membrane trafficking in polarized epithelial cells. Curr Opin Cell Biol 20:208-213.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 208-213
    • Fölsch, H.1
  • 2
    • 12344260000 scopus 로고    scopus 로고
    • Polarized sorting in epithelial cells: Raft clustering and the biogenesis of the apical membrane
    • Schuck S, Simons K (2004) Polarized sorting in epithelial cells: Raft clustering and the biogenesis of the apical membrane. J Cell Sci 117:5955-5964.
    • (2004) J Cell Sci , vol.117 , pp. 5955-5964
    • Schuck, S.1    Simons, K.2
  • 4
    • 2342556630 scopus 로고    scopus 로고
    • FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and Ptd Ins(4)P
    • Godi A, et al. (2004) FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and Ptd Ins(4)P. Nat Cell Biol 6:393-404.
    • (2004) Nat Cell Biol , vol.6 , pp. 393-404
    • Godi, A.1
  • 5
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Vieira OV, Verkade P, Manninen A, Simons K (2005) FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J Cell Biol 170:521-526.
    • (2005) J Cell Biol , vol.170 , pp. 521-526
    • Vieira, O.V.1    Verkade, P.2    Manninen, A.3    Simons, K.4
  • 6
    • 73449097531 scopus 로고    scopus 로고
    • FAPP2 is required for aquaporin-2 apical sorting at trans-Golgi network in polarized MDCK cells
    • 10.1152/ajpcell.00098
    • Yui N, et al. (2009) FAPP2 is required for aquaporin-2 apical sorting at trans-Golgi network in polarized MDCK cells. Am J Physiol Cell Physiol, 10.1152/ajpcell.00098.2009.
    • (2009) Am J Physiol Cell Physiol
    • Yui, N.1
  • 7
    • 34548498611 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
    • D'Angelo G, et al. (2007) Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449:62-67.
    • (2007) Nature , vol.449 , pp. 62-67
    • D'Angelo, G.1
  • 8
    • 35348991132 scopus 로고    scopus 로고
    • Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis
    • Halter D, et al. (2007) Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis. J Cell Biol 179:101-115.
    • (2007) J Cell Biol , vol.179 , pp. 101-115
    • Halter, D.1
  • 9
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A, Uyhazi K, Frost A, De Camilli P (2006) GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441:528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 10
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain- containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, et al. (2000) Identification of pleckstrin-homology-domain- containing proteins with novel phosphoinositide-binding specificities. Biochem J 351:19-31.
    • (2000) Biochem J , vol.351 , pp. 19-31
    • Dowler, S.1
  • 11
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon HT, Gallop JL (2005) Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438:590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 12
  • 13
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J, Kozlov MM (2006) How proteins produce cellular membrane curvature. Nat Rev Mol Cell Biol 7:9 -19.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 14
    • 1442317538 scopus 로고    scopus 로고
    • BARdomains as sensors ofmembranecurvature: The amphiphysin BAR structure
    • Peter BJ, et al. (2004)BARdomains as sensors ofmembranecurvature: The amphiphysin BAR structure. Science 303:495-499.
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1
  • 15
    • 33750037303 scopus 로고    scopus 로고
    • Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations
    • Blood PD, Voth GA (2006) Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations. Proc Natl Acad Sci USA 103:15068-15072.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15068-15072
    • Blood, P.D.1    Voth, G.A.2
  • 16
    • 34548483180 scopus 로고    scopus 로고
    • Structural and membrane binding analysis of the Phox homology domain of Bem1p: Basis of phosphatidylinositol 4-phosphate specificity
    • Stahelin RV, Karathanassis D, Murray D, Williams RL, Cho W (2007) Structural and membrane binding analysis of the Phox homology domain of Bem1p: Basis of phosphatidylinositol 4-phosphate specificity. J Biol Chem 282:25737-25747.
    • (2007) J Biol Chem , vol.282 , pp. 25737-25747
    • Stahelin, R.V.1    Karathanassis, D.2    Murray, D.3    Williams, R.L.4    Cho, W.5
  • 17
    • 0347504836 scopus 로고    scopus 로고
    • Membrane trafficking: Coat control by curvature
    • Lippincott-Schwartz J, Liu W(2003) Membrane trafficking: Coat control by curvature. Nature 426:507-508.
    • (2003) Nature , vol.426 , pp. 507-508
    • Lippincott-Schwartz, J.1    Liu, W.2
  • 18
    • 0031457805 scopus 로고    scopus 로고
    • Post-Golgi biosynthetic trafficking
    • Keller P, Simons K (1997) Post-Golgi biosynthetic trafficking. J Cell Sci 110:3001-3009.
    • (1997) J Cell Sci , vol.110 , pp. 3001-3009
    • Keller, P.1    Simons, K.2
  • 19
    • 50949133967 scopus 로고    scopus 로고
    • Arf family GTP loading is activated by, and generates, positive membrane curvature
    • Lundmark R, Doherty GJ, Vallis Y, Peter BJ, McMahon HT (2008) Arf family GTP loading is activated by, and generates, positive membrane curvature. Biochem J 414:189-194.
    • (2008) Biochem J , vol.414 , pp. 189-194
    • Lundmark, R.1    Doherty, G.J.2    Vallis, Y.3    Peter, B.J.4    McMahon, H.T.5
  • 20
    • 50149083446 scopus 로고    scopus 로고
    • Membrane curvature induced by Arf1-GTP is essential for vesicle formation
    • Beck R, et al. (2008) Membrane curvature induced by Arf1-GTP is essential for vesicle formation. Proc Natl Acad Sci USA 105:11731-11736.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11731-11736
    • Beck, R.1
  • 21
    • 55549125212 scopus 로고    scopus 로고
    • Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding
    • Krauss M, et al. (2008) Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding. J Biol Chem 283:27717-27723.
    • (2008) J Biol Chem , vol.283 , pp. 27717-27723
    • Krauss, M.1
  • 23
    • 23044510465 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide
    • Tamboli IY, et al. (2005) Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide. J Biol Chem 280:28110-28117.
    • (2005) J Biol Chem , vol.280 , pp. 28110-28117
    • Tamboli, I.Y.1
  • 25
    • 28444461398 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae
    • Bankaitis VA, et al. (2005) Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae. Adv Enzyme Regul 45:155-170.
    • (2005) Adv Enzyme Regul , vol.45 , pp. 155-170
    • Bankaitis, V.A.1
  • 26
    • 58149190012 scopus 로고    scopus 로고
    • Glycolipid transfer proteins and membrane interaction
    • Mattjus P (2009) Glycolipid transfer proteins and membrane interaction. Biochim Biophys Acta 1788:267-272.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 267-272
    • Mattjus, P.1
  • 27
    • 0020114103 scopus 로고
    • X-ray diffraction and scattering on disordered systems using synchrotron radiation
    • Koch MHJ, Bordas J (1983) X-ray diffraction and scattering on disordered systems using synchrotron radiation. Nucl Instrum Methods Physics Res 208:461-469.
    • (1983) Nucl Instrum Methods Physics Res , vol.208 , pp. 461-469
    • Koch, M.H.J.1    Bordas, J.2
  • 28
    • 34248347847 scopus 로고    scopus 로고
    • Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg
    • Roessle MW,et al. (2007) Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg. J Appl Crystallogr 40:s190-s194.
    • (2007) J Appl Crystallogr , vol.40
    • Roessle, M.W.1
  • 29
    • 51949084084 scopus 로고    scopus 로고
    • Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33
    • Round AR, et al. (2008) Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33. J Appl Crystallogr 41:913-917.
    • (2008) J Appl Crystallogr , vol.41 , pp. 913-917
    • Round, A.R.1
  • 31
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76:2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 32
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89:1237-1250.
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.