메뉴 건너뛰기




Volumn 209, Issue 1, 2015, Pages 97-110

Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2 regulates endocytic recycling

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; INTEGRIN; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PLECKSTRIN; SAC2 PROTEIN; TRANSFERRIN; UNCLASSIFIED DRUG; INOSITOL-POLYPHOSPHATE 5-PHOSPHATASE; PHOSPHATASE; PHOSPHATIDYLINOSITOL 4-PHOSPHATE; POLYPHOSPHOINOSITIDE; TRANSFERRIN RECEPTOR;

EID: 84928253123     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201408027     Document Type: Article
Times cited : (48)

References (61)
  • 1
    • 77955203926 scopus 로고    scopus 로고
    • Quantifying colocalization by correlation: the Pearson correlation coefficient is superior to the Mander's overlap coefficient
    • Adler, J., and I. Parmryd. 2010. Quantifying colocalization by correlation: the Pearson correlation coefficient is superior to the Mander's overlap coefficient. Cytometry A. 77:733-742. http://dx.doi.org/10.1002/cyto.a.20896
    • (2010) Cytometry A , vol.77 , pp. 733-742
    • Adler, J.1    Parmryd, I.2
  • 2
    • 0037738555 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1Bmediated neurite outgrowth
    • Albertinazzi, C., L. Za, S. Paris, and I. de Curtis. 2003. ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1Bmediated neurite outgrowth. Mol. Biol. Cell. 14:1295-1307. http://dx.doi.org/10.1091/mbc. E02-07-0406
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1295-1307
    • Albertinazzi, C.1    Za, L.2    Paris, S.3    de Curtis, I.4
  • 4
    • 84880962133 scopus 로고    scopus 로고
    • Phosphoinositides: tiny lipids with giant impact on cell regulation
    • Balla, T. 2013. Phosphoinositides: tiny lipids with giant impact on cell regulation. Physiol. Rev. 93:1019-1137. http://dx.doi.org/10.1152/physrev.00028.2012
    • (2013) Physiol. Rev. , vol.93 , pp. 1019-1137
    • Balla, T.1
  • 5
    • 34447133038 scopus 로고    scopus 로고
    • Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J
    • Chow, C.Y., Y. Zhang, J.J. Dowling, N. Jin, M. Adamska, K. Shiga, K. Szigeti, M.E. Shy, J. Li, X. Zhang, et al. 2007. Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J. Nature. 448:68-72. http://dx.doi.org/10.1038/nature05876
    • (2007) Nature , vol.448 , pp. 68-72
    • Chow, C.Y.1    Zhang, Y.2    Dowling, J.J.3    Jin, N.4    Adamska, M.5    Shiga, K.6    Szigeti, K.7    Shy, M.E.8    Li, J.9    Zhang, X.10
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763. http://dx.doi.org/10.1107/S0907444994003112
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , Issue.4 , pp. 760-763
  • 9
    • 84884183110 scopus 로고    scopus 로고
    • Cell biology in neuroscience: mechanisms of cell migration in the nervous system
    • Cooper, J.A. 2013. Cell biology in neuroscience: mechanisms of cell migration in the nervous system. J. Cell Biol. 202:725-734. http://dx.doi.org/10.1083/jcb.201305021
    • (2013) J. Cell Biol. , vol.202 , pp. 725-734
    • Cooper, J.A.1
  • 11
    • 2942718545 scopus 로고    scopus 로고
    • PI-loting membrane traffic
    • De Matteis, M.A., and A. Godi. 2004. PI-loting membrane traffic. Nat. Cell Biol. 6:487-492. http://dx.doi.org/10.1038/ncb0604-487
    • (2004) Nat. Cell Biol. , vol.6 , pp. 487-492
    • De Matteis, M.A.1    Godi, A.2
  • 12
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G., and P. De Camilli. 2006. Phosphoinositides in cell regulation and membrane dynamics. Nature. 443:651-657. http://dx.doi.org/10.1038/nature05185
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 13
    • 84907099490 scopus 로고    scopus 로고
    • The Legionella longbeachae Icm/Dot substrate SidC selectively binds phosphatidylinositol 4-phosphate with nanomolar affinity and promotes pathogen vacuole-endoplasmic reticulum interactions
    • Dolinsky, S., I. Haneburger, A. Cichy, M. Hannemann, A. Itzen, and H. Hilbi. 2014. The Legionella longbeachae Icm/Dot substrate SidC selectively binds phosphatidylinositol 4-phosphate with nanomolar affinity and promotes pathogen vacuole-endoplasmic reticulum interactions. Infect. Immun. 82:4021-4033. http://dx.doi.org/10.1128/IAI.01685-14
    • (2014) Infect. Immun. , vol.82 , pp. 4021-4033
    • Dolinsky, S.1    Haneburger, I.2    Cichy, A.3    Hannemann, M.4    Itzen, A.5    Hilbi, H.6
  • 14
    • 33644499479 scopus 로고    scopus 로고
    • The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover
    • Duex, J.E., F. Tang, and L.S. Weisman. 2006. The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover. J. Cell Biol. 172:693-704. http://dx.doi.org/10.1083/jcb.200512105
    • (2006) J. Cell Biol. , vol.172 , pp. 693-704
    • Duex, J.E.1    Tang, F.2    Weisman, L.S.3
  • 15
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and K. Cowtan. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132. http://dx.doi.org/10.1107/S0907444904019158
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 17
    • 75149129096 scopus 로고    scopus 로고
    • Moving forward: polarised trafficking in cell migration
    • Fletcher, S.J., and J.Z. Rappoport. 2010. Moving forward: polarised trafficking in cell migration. Trends Cell Biol. 20:71-78. http://dx.doi.org/10.1016/j.tcb.2009.11.006
    • (2010) Trends Cell Biol. , vol.20 , pp. 71-78
    • Fletcher, S.J.1    Rappoport, J.Z.2
  • 19
    • 0033532062 scopus 로고    scopus 로고
    • SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
    • Guo, S., L.E. Stolz, S.M. Lemrow, and J.D. York. 1999. SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases. J. Biol. Chem. 274:12990-12995. http://dx.doi.org/10.1074/jbc.274.19.12990
    • (1999) J. Biol. Chem. , vol.274 , pp. 12990-12995
    • Guo, S.1    Stolz, L.E.2    Lemrow, S.M.3    York, J.D.4
  • 20
    • 79956320991 scopus 로고    scopus 로고
    • Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain
    • He, J., J.L. Scott, A. Heroux, S. Roy, M. Lenoir, M. Overduin, R.V. Stahelin, and T.G. Kutateladze. 2011. Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain. J. Biol. Chem. 286:18650-18657. http://dx.doi.org/10.1074/jbc. M111.233015
    • (2011) J. Biol. Chem. , vol.286 , pp. 18650-18657
    • He, J.1    Scott, J.L.2    Heroux, A.3    Roy, S.4    Lenoir, M.5    Overduin, M.6    Stahelin, R.V.7    Kutateladze, T.G.8
  • 21
    • 74249095519 scopus 로고    scopus 로고
    • CRISPR/Cas, the immune system of bacteria and archaea
    • Horvath, P., and R. Barrangou. 2010. CRISPR/Cas, the immune system of bacteria and archaea. Science. 327:167-170. http://dx.doi.org/10.1126/science.1179555
    • (2010) Science , vol.327 , pp. 167-170
    • Horvath, P.1    Barrangou, R.2
  • 22
    • 84939979550 scopus 로고    scopus 로고
    • The structure of phosphoinositide phosphatases:Insights into substrate specificity and catalysis
    • Hsu, F., and Y. Mao. 2014. The structure of phosphoinositide phosphatases:Insights into substrate specificity and catalysis. Biochim. Biophys. Acta. http://dx.doi.org/10.1016/j.bbalip.2014.09.015
    • (2014) Biochim. Biophys. Acta
    • Hsu, F.1    Mao, Y.2
  • 23
    • 33748466150 scopus 로고    scopus 로고
    • Endocytic recycling pathways:emerging regulators of cell migration
    • Jones, M.C., P.T. Caswell, and J.C. Norman. 2006. Endocytic recycling pathways:emerging regulators of cell migration. Curr. Opin. Cell Biol. 18:549-557. http://dx.doi.org/10.1016/j.ceb.2006.08.003
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 549-557
    • Jones, M.C.1    Caswell, P.T.2    Norman, J.C.3
  • 24
    • 34548660798 scopus 로고    scopus 로고
    • Mover is a novel vertebrate-specific presynaptic protein with differential distribution at subsets of CNS synapses
    • Kremer, T., C. Kempf, N. Wittenmayer, R. Nawrotzki, T. Kuner, J. Kirsch, and T. Dresbach. 2007. Mover is a novel vertebrate-specific presynaptic protein with differential distribution at subsets of CNS synapses. FEBS Lett. 581:4727-4733. http://dx.doi.org/10.1016/j.febslet.2007.08.070
    • (2007) FEBS Lett. , vol.581 , pp. 4727-4733
    • Kremer, T.1    Kempf, C.2    Wittenmayer, N.3    Nawrotzki, R.4    Kuner, T.5    Kirsch, J.6    Dresbach, T.7
  • 25
    • 0036298197 scopus 로고    scopus 로고
    • Synaptotagminlike protein 5: a novel Rab27A effector with C-terminal tandem C2 domains
    • Kuroda, T.S., M. Fukuda, H. Ariga, and K. Mikoshiba. 2002. Synaptotagminlike protein 5: a novel Rab27A effector with C-terminal tandem C2 domains. Biochem. Biophys. Res. Commun. 293:899-906. http://dx.doi.org/10.1016/S0006-291X(02)00320-0
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 899-906
    • Kuroda, T.S.1    Fukuda, M.2    Ariga, H.3    Mikoshiba, K.4
  • 26
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M.A., and J. Schlessinger. 2010. Cell signaling by receptor tyrosine kinases. Cell. 141:1117-1134. http://dx.doi.org/10.1016/j.cell.2010.06.011
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 27
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and-independent components
    • Levine, T.P., and S. Munro. 2002. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and-independent components. Curr. Biol. 12:695-704. http://dx.doi.org/10.1016/S0960-9822(02)00779-0
    • (2002) Curr. Biol. , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 28
    • 84860677862 scopus 로고    scopus 로고
    • The recycling endosome and its role in neurological disorders
    • Li, X., and M. DiFiglia. 2012. The recycling endosome and its role in neurological disorders. Prog. Neurobiol. 97:127-141. http://dx.doi.org/10.1016/j.pneurobio.2011.10.002
    • (2012) Prog. Neurobiol. , vol.97 , pp. 127-141
    • Li, X.1    DiFiglia, M.2
  • 29
    • 77950682093 scopus 로고    scopus 로고
    • Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease
    • Li, X., A. Valencia, E. Sapp, N. Masso, J. Alexander, P. Reeves, K.B. Kegel, N. Aronin, and M. Difiglia. 2010. Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease. J. Neurosci. 30:4552-4561. http://dx.doi.org/10.1523/JNEUROSCI.5865-09.2010
    • (2010) J. Neurosci. , vol.30 , pp. 4552-4561
    • Li, X.1    Valencia, A.2    Sapp, E.3    Masso, N.4    Alexander, J.5    Reeves, P.6    Kegel, K.B.7    Aronin, N.8    Difiglia, M.9
  • 31
    • 77951978964 scopus 로고    scopus 로고
    • Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function
    • Manford, A., T. Xia, A.K. Saxena, C. Stefan, F. Hu, S.D. Emr, and Y. Mao. 2010. Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function. EMBO J. 29:1489-1498. http://dx.doi.org/10.1038/emboj.2010.57
    • (2010) EMBO J. , vol.29 , pp. 1489-1498
    • Manford, A.1    Xia, T.2    Saxena, A.K.3    Stefan, C.4    Hu, F.5    Emr, S.D.6    Mao, Y.7
  • 32
    • 67650373163 scopus 로고    scopus 로고
    • A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism
    • Mao, Y., D.M. Balkin, R. Zoncu, K.S. Erdmann, L. Tomasini, F. Hu, M.M. Jin, M.E. Hodsdon, and P. De Camilli. 2009. A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism. EMBO J. 28:1831-1842. http://dx.doi.org/10.1038/emboj.2009.155
    • (2009) EMBO J. , vol.28 , pp. 1831-1842
    • Mao, Y.1    Balkin, D.M.2    Zoncu, R.3    Erdmann, K.S.4    Tomasini, L.5    Hu, F.6    Jin, M.M.7    Hodsdon, M.E.8    De Camilli, P.9
  • 34
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon, H.T., and E. Boucrot. 2011. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 12:517-533. http://dx.doi.org/10.1038/nrm3151
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 36
    • 0035933722 scopus 로고    scopus 로고
    • Identification and characterization of a sac domain-containing phosphoinositide 5-phosphatase
    • Minagawa, T., T. Ijuin, Y. Mochizuki, and T. Takenawa. 2001. Identification and characterization of a sac domain-containing phosphoinositide 5-phosphatase. J. Biol. Chem. 276:22011-22015. http://dx.doi.org/10.1074/jbc. M101579200
    • (2001) J. Biol. Chem. , vol.276 , pp. 22011-22015
    • Minagawa, T.1    Ijuin, T.2    Mochizuki, Y.3    Takenawa, T.4
  • 37
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., A.A. Vagin, and E.J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53:240-255. http://dx.doi.org/10.1107/S0907444996012255
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 39
    • 0034602319 scopus 로고    scopus 로고
    • Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity
    • Nemoto, Y., B.G. Kearns, M.R. Wenk, H. Chen, K. Mori, J.G. Alb Jr., P. De Camilli, and V.A. Bankaitis. 2000. Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity. J. Biol. Chem. 275:34293-34305. http://dx.doi.org/10.1074/jbc. M003923200
    • (2000) J. Biol. Chem. , vol.275 , pp. 34293-34305
    • Nemoto, Y.1    Kearns, B.G.2    Wenk, M.R.3    Chen, H.4    Mori, K.5    Alb, J.G.6    De Camilli, P.7    Bankaitis, V.A.8
  • 40
    • 0029000258 scopus 로고
    • The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase
    • Norris, F.A., V. Auethavekiat, and P.W. Majerus. 1995. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270:16128-16133. http://dx.doi.org/10.1074/jbc.270.27.16128
    • (1995) J. Biol. Chem. , vol.270 , pp. 16128-16133
    • Norris, F.A.1    Auethavekiat, V.2    Majerus, P.W.3
  • 41
    • 0034194152 scopus 로고    scopus 로고
    • Phosphoinositide signaling and the regulation of membrane trafficking in yeast
    • Odorizzi, G., M. Babst, and S.D. Emr. 2000. Phosphoinositide signaling and the regulation of membrane trafficking in yeast. Trends Biochem. Sci. 25:229-235. http://dx.doi.org/10.1016/S0968-0004(00)01543-7
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 229-235
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326. http://dx.doi.org/10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs
    • Pape, T., and T.R. Schneider. 2004. HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J. Appl. Crystallogr. 37:843-844. http://dx.doi.org/10.1107/S0021889804018047
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 44
    • 0036701581 scopus 로고    scopus 로고
    • Insights from yeast endosomes
    • Pelham, H.R. 2002. Insights from yeast endosomes. Curr. Opin. Cell Biol. 14:454-462. http://dx.doi.org/10.1016/S0955-0674(02)00352-6
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 454-462
    • Pelham, H.R.1
  • 45
    • 79960717910 scopus 로고    scopus 로고
    • Endocytosis and signaling
    • Platta, H.W., and H. Stenmark. 2011. Endocytosis and signaling. Curr. Opin. Cell Biol. 23:393-403. http://dx.doi.org/10.1016/j.ceb.2011.03.008
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 393-403
    • Platta, H.W.1    Stenmark, H.2
  • 47
    • 0037350449 scopus 로고    scopus 로고
    • Real-time analysis of clathrin-mediated endocytosis during cell migration
    • Rappoport, J.Z., and S.M. Simon. 2003. Real-time analysis of clathrin-mediated endocytosis during cell migration. J. Cell Sci. 116:847-855. http://dx.doi.org/10.1242/jcs.00289
    • (2003) J. Cell Sci. , vol.116 , pp. 847-855
    • Rappoport, J.Z.1    Simon, S.M.2
  • 48
    • 0346729925 scopus 로고    scopus 로고
    • Vacuole size control: regulation of PtdIns(3,5)P2 levels by the vacuole-associated Vac14-Fig4 complex, a PtdIns(3,5)P2-specific phosphatase
    • Rudge, S.A., D.M. Anderson, and S.D. Emr. 2004. Vacuole size control: regulation of PtdIns(3,5)P2 levels by the vacuole-associated Vac14-Fig4 complex, a PtdIns(3,5)P2-specific phosphatase. Mol. Biol. Cell. 15:24-36. http://dx.doi.org/10.1091/mbc. E03-05-0297
    • (2004) Mol. Biol. Cell , vol.15 , pp. 24-36
    • Rudge, S.A.1    Anderson, D.M.2    Emr, S.D.3
  • 49
    • 67649650263 scopus 로고    scopus 로고
    • Roles of endosomal trafficking in neurite outgrowth and guidance
    • Sann, S., Z. Wang, H. Brown, and Y. Jin. 2009. Roles of endosomal trafficking in neurite outgrowth and guidance. Trends Cell Biol. 19:317-324. http://dx.doi.org/10.1016/j.tcb.2009.05.001
    • (2009) Trends Cell Biol. , vol.19 , pp. 317-324
    • Sann, S.1    Wang, Z.2    Brown, H.3    Jin, Y.4
  • 50
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman, M.N. 2004. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165:111-122. http://dx.doi.org/10.1083/jcb.200312034
    • (2004) J. Cell Biol. , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 51
    • 34547796509 scopus 로고    scopus 로고
    • Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval
    • Seaman, M.N. 2007. Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval. J. Cell Sci. 120:2378-2389. http://dx.doi.org/10.1242/jcs.009654
    • (2007) J. Cell Sci. , vol.120 , pp. 2378-2389
    • Seaman, M.N.1
  • 56
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Vieira, O.V., P. Verkade, A. Manninen, and K. Simons. 2005. FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J. Cell Biol. 170:521-526. http://dx.doi.org/10.1083/jcb.200503078
    • (2005) J. Cell Biol. , vol.170 , pp. 521-526
    • Vieira, O.V.1    Verkade, P.2    Manninen, A.3    Simons, K.4
  • 57
    • 0037240484 scopus 로고    scopus 로고
    • Visualization of TGN to endosome trafficking through fluorescently labeled MPR and AP-1 in living cells
    • Waguri, S., F. Dewitte, R. Le Borgne, Y. Rouillé, Y. Uchiyama, J.F. Dubremetz, and B. Hoflack. 2003. Visualization of TGN to endosome trafficking through fluorescently labeled MPR and AP-1 in living cells. Mol. Biol. Cell. 14:142-155. http://dx.doi.org/10.1091/mbc. E02-06-0338
    • (2003) Mol. Biol. Cell , vol.14 , pp. 142-155
    • Waguri, S.1    Dewitte, F.2    Le Borgne, R.3    Rouillé, Y.4    Uchiyama, Y.5    Dubremetz, J.F.6    Hoflack, B.7
  • 58
    • 34248226275 scopus 로고    scopus 로고
    • αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration
    • White, D.P., P.T. Caswell, and J.C. Norman. 2007. αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration. J. Cell Biol. 177:515-525. http://dx.doi.org/10.1083/jcb.200609004
    • (2007) J. Cell Biol. , vol.177 , pp. 515-525
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 59
    • 0027269974 scopus 로고
    • SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast
    • Whitters, E.A., A.E. Cleves, T.P. McGee, H.B. Skinner, and V.A. Bankaitis. 1993. SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast. J. Cell Biol. 122:79-94. http://dx.doi.org/10.1083/jcb.122.1.79
    • (1993) J. Cell Biol. , vol.122 , pp. 79-94
    • Whitters, E.A.1    Cleves, A.E.2    McGee, T.P.3    Skinner, H.B.4    Bankaitis, V.A.5
  • 60
    • 73349084646 scopus 로고    scopus 로고
    • Inpp5f is a polyphosphoinositide phosphatase that regulates cardiac hypertrophic responsiveness
    • Zhu, W., C.M. Trivedi, D. Zhou, L. Yuan, M.M. Lu, and J.A. Epstein. 2009. Inpp5f is a polyphosphoinositide phosphatase that regulates cardiac hypertrophic responsiveness. Circ. Res. 105:1240-1247. http://dx.doi.org/10.1161/CIRCRESAHA.109.208785
    • (2009) Circ. Res. , vol.105 , pp. 1240-1247
    • Zhu, W.1    Trivedi, C.M.2    Zhou, D.3    Yuan, L.4    Lu, M.M.5    Epstein, J.A.6
  • 61
    • 62549151303 scopus 로고    scopus 로고
    • A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes
    • Zoncu, R., R.M. Perera, D.M. Balkin, M. Pirruccello, D. Toomre, and P. De Camilli. 2009. A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Cell. 136:1110-1121. http://dx.doi.org/10.1016/j.cell.2009.01.032
    • (2009) Cell , vol.136 , pp. 1110-1121
    • Zoncu, R.1    Perera, R.M.2    Balkin, D.M.3    Pirruccello, M.4    Toomre, D.5    De Camilli, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.