메뉴 건너뛰기




Volumn 21, Issue 9, 2011, Pages 515-525

Membrane-trafficking sorting hubs: Cooperation between PI4P and small GTPases at the trans-Golgi network

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE;

EID: 80052186347     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2011.05.005     Document Type: Review
Times cited : (93)

References (121)
  • 1
    • 78751656754 scopus 로고    scopus 로고
    • Role of Rab GTPases in membrane traffic and cell physiology
    • Hutagalung A.H., Novick P.J. Role of Rab GTPases in membrane traffic and cell physiology. Physiol. Rev. 2011, 91:119-149.
    • (2011) Physiol. Rev. , vol.91 , pp. 119-149
    • Hutagalung, A.H.1    Novick, P.J.2
  • 2
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia R., Munro S. Organelle identity and the signposts for membrane traffic. Nature 2005, 438:597-604.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 3
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G., De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature 2006, 443:651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 4
    • 0032877340 scopus 로고    scopus 로고
    • Regulation of early-endosome dynamics by phosphatidylinositol 3-phosphate binding proteins
    • Clague M.J., et al. Regulation of early-endosome dynamics by phosphatidylinositol 3-phosphate binding proteins. Biochem. Soc. Trans. 1999, 27:662-666.
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 662-666
    • Clague, M.J.1
  • 5
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu P.V., et al. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 1993, 260:88-91.
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1
  • 6
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci C., et al. The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 1992, 70:715-728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1
  • 7
    • 0028786852 scopus 로고
    • Evidence for phosphatidylinositol 3-kinase as a regulator of endocytosis via activation of Rab5
    • Li G., et al. Evidence for phosphatidylinositol 3-kinase as a regulator of endocytosis via activation of Rab5. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:10207-10211.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10207-10211
    • Li, G.1
  • 8
    • 20444410032 scopus 로고    scopus 로고
    • Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the clathrin-coated pit
    • Sato M., et al. Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the clathrin-coated pit. Nat. Cell Biol. 2005, 7:559-569.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 559-569
    • Sato, M.1
  • 9
    • 56149118851 scopus 로고    scopus 로고
    • Coordinated regulation of AP2 uncoating from clathrin-coated vesicles by rab5 and hRME-6
    • Semerdjieva S., et al. Coordinated regulation of AP2 uncoating from clathrin-coated vesicles by rab5 and hRME-6. J. Cell Biol. 2008, 183:499-511.
    • (2008) J. Cell Biol. , vol.183 , pp. 499-511
    • Semerdjieva, S.1
  • 10
    • 0033174034 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-OH kinases are Rab5 effectors
    • Christoforidis S., et al. Phosphatidylinositol-3-OH kinases are Rab5 effectors. Nat. Cell Biol. 1999, 1:249-252.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 249-252
    • Christoforidis, S.1
  • 11
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
    • Simonsen A., et al. EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 1998, 394:494-498.
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1
  • 12
    • 0035930332 scopus 로고    scopus 로고
    • Multivalent endosome targeting by homodimeric EEA1
    • Dumas J.J., et al. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell 2001, 8:947-958.
    • (2001) Mol. Cell , vol.8 , pp. 947-958
    • Dumas, J.J.1
  • 13
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann D.J., et al. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 2003, 162:413-423.
    • (2003) J. Cell Biol. , vol.162 , pp. 413-423
    • Katzmann, D.J.1
  • 14
    • 77950460749 scopus 로고    scopus 로고
    • Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells
    • Kinchen J.M., Ravichandran K.S. Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells. Nature 2010, 464:778-782.
    • (2010) Nature , vol.464 , pp. 778-782
    • Kinchen, J.M.1    Ravichandran, K.S.2
  • 15
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev D., et al. Identification of the switch in early-to-late endosome transition. Cell 2010, 141:497-508.
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1
  • 16
    • 77957231342 scopus 로고    scopus 로고
    • The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7
    • Nordmann M., et al. The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7. Curr. Biol. 2010, 20:1654-1659.
    • (2010) Curr. Biol. , vol.20 , pp. 1654-1659
    • Nordmann, M.1
  • 17
    • 33751253774 scopus 로고    scopus 로고
    • Sara endosomes and the maintenance of Dpp signaling levels across mitosis
    • Bokel C., et al. Sara endosomes and the maintenance of Dpp signaling levels across mitosis. Science 2006, 314:1135-1139.
    • (2006) Science , vol.314 , pp. 1135-1139
    • Bokel, C.1
  • 18
    • 34248231196 scopus 로고    scopus 로고
    • Endofin acts as a Smad anchor for receptor activation in BMP signaling
    • Shi W., et al. Endofin acts as a Smad anchor for receptor activation in BMP signaling. J. Cell Sci. 2007, 120:1216-1224.
    • (2007) J. Cell Sci. , vol.120 , pp. 1216-1224
    • Shi, W.1
  • 19
    • 67349204759 scopus 로고    scopus 로고
    • Directional Delta and Notch trafficking in Sara endosomes during asymmetric cell division
    • Coumailleau F., et al. Directional Delta and Notch trafficking in Sara endosomes during asymmetric cell division. Nature 2009, 458:1051-1055.
    • (2009) Nature , vol.458 , pp. 1051-1055
    • Coumailleau, F.1
  • 20
    • 61849156850 scopus 로고    scopus 로고
    • Intercellular transfer to signalling endosomes regulates an ex vivo bone marrow niche
    • Gillette J.M., et al. Intercellular transfer to signalling endosomes regulates an ex vivo bone marrow niche. Nat. Cell Biol. 2009, 11:303-311.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 303-311
    • Gillette, J.M.1
  • 21
    • 0026730464 scopus 로고
    • The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway
    • van der Sluijs P., et al. The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway. Cell 1992, 70:729-740.
    • (1992) Cell , vol.70 , pp. 729-740
    • van der Sluijs, P.1
  • 22
    • 66349083804 scopus 로고    scopus 로고
    • Cargo-mediated regulation of a rapid Rab4-dependent recycling pathway
    • Yudowski G.A., et al. Cargo-mediated regulation of a rapid Rab4-dependent recycling pathway. Mol. Biol. Cell 2009, 20:2774-2784.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2774-2784
    • Yudowski, G.A.1
  • 23
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich O., et al. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 1996, 135:913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1
  • 24
    • 0035914343 scopus 로고    scopus 로고
    • Identification and characterization of a family of Rab11-interacting proteins
    • Hales C.M., et al. Identification and characterization of a family of Rab11-interacting proteins. J. Biol. Chem. 2001, 276:39067-39075.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39067-39075
    • Hales, C.M.1
  • 25
    • 0027765507 scopus 로고
    • Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion
    • Hay J.C., Martin T.F. Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion. Nature 1993, 366:572-575.
    • (1993) Nature , vol.366 , pp. 572-575
    • Hay, J.C.1    Martin, T.F.2
  • 26
    • 0028953311 scopus 로고
    • ATP-dependent inositide phosphorylation required for Ca(2+)-activated secretion
    • Hay J.C., et al. ATP-dependent inositide phosphorylation required for Ca(2+)-activated secretion. Nature 1995, 374:173-177.
    • (1995) Nature , vol.374 , pp. 173-177
    • Hay, J.C.1
  • 27
    • 0029966103 scopus 로고    scopus 로고
    • Chromaffin granule-associated phosphatidylinositol 4-kinase activity is required for stimulated secretion
    • Wiedemann C., et al. Chromaffin granule-associated phosphatidylinositol 4-kinase activity is required for stimulated secretion. EMBO J. 1996, 15:2094-2101.
    • (1996) EMBO J. , vol.15 , pp. 2094-2101
    • Wiedemann, C.1
  • 28
    • 0032146218 scopus 로고    scopus 로고
    • An essential role for a small synaptic vesicle-associated phosphatidylinositol 4-kinase in neurotransmitter release
    • Wiedemann C., et al. An essential role for a small synaptic vesicle-associated phosphatidylinositol 4-kinase in neurotransmitter release. J. Neurosci. 1998, 18:5594-5602.
    • (1998) J. Neurosci. , vol.18 , pp. 5594-5602
    • Wiedemann, C.1
  • 29
    • 0033607537 scopus 로고    scopus 로고
    • Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae
    • Hama H., et al. Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 1999, 274:34294-34300.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34294-34300
    • Hama, H.1
  • 30
    • 0033258472 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi
    • Walch-Solimena C., Novick P. The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi. Nat. Cell Biol. 1999, 1:523-525.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 523-525
    • Walch-Solimena, C.1    Novick, P.2
  • 31
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis V.A., et al. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 1990, 347:561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1
  • 32
    • 0033840656 scopus 로고    scopus 로고
    • Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics
    • Audhya A., et al. Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics. Mol. Biol. Cell 2000, 11:2673-2689.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2673-2689
    • Audhya, A.1
  • 33
    • 0033194151 scopus 로고    scopus 로고
    • ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex
    • Godi A., et al. ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex. Nat. Cell Biol. 1999, 1:280-287.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 280-287
    • Godi, A.1
  • 34
    • 0037455579 scopus 로고    scopus 로고
    • EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking
    • Mills I.G., et al. EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking. J. Cell Biol. 2003, 160:213-222.
    • (2003) J. Cell Biol. , vol.160 , pp. 213-222
    • Mills, I.G.1
  • 35
    • 0042591490 scopus 로고    scopus 로고
    • Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi
    • Wang Y.J., et al. Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. Cell 2003, 114:299-310.
    • (2003) Cell , vol.114 , pp. 299-310
    • Wang, Y.J.1
  • 36
    • 15444363818 scopus 로고    scopus 로고
    • Distinct Golgi populations of phosphatidylinositol 4-phosphate regulated by phosphatidylinositol 4-kinases
    • Weixel K.M., et al. Distinct Golgi populations of phosphatidylinositol 4-phosphate regulated by phosphatidylinositol 4-kinases. J. Biol. Chem. 2005, 280:10501-10508.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10501-10508
    • Weixel, K.M.1
  • 37
    • 70349835304 scopus 로고    scopus 로고
    • GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding
    • Dippold H.C., et al. GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding. Cell 2009, 139:337-351.
    • (2009) Cell , vol.139 , pp. 337-351
    • Dippold, H.C.1
  • 38
    • 0036320668 scopus 로고    scopus 로고
    • Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae
    • Bonangelino C.J., et al. Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol. Biol. Cell 2002, 13:2486-2501.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2486-2501
    • Bonangelino, C.J.1
  • 39
    • 41649090365 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases requires a Vps74p oligomer
    • Schmitz K.R., et al. Golgi localization of glycosyltransferases requires a Vps74p oligomer. Dev. Cell 2008, 14:523-534.
    • (2008) Dev. Cell , vol.14 , pp. 523-534
    • Schmitz, K.R.1
  • 40
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu L., et al. Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 2008, 321:404-407.
    • (2008) Science , vol.321 , pp. 404-407
    • Tu, L.1
  • 41
    • 76149142505 scopus 로고    scopus 로고
    • PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking
    • Wood C.S., et al. PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking. J. Cell Biol. 2009, 187:967-975.
    • (2009) J. Cell Biol. , vol.187 , pp. 967-975
    • Wood, C.S.1
  • 42
    • 0036701880 scopus 로고    scopus 로고
    • ARF1 regulatory factors and COPI vesicle formation
    • Spang A. ARF1 regulatory factors and COPI vesicle formation. Curr. Opin. Cell Biol. 2002, 14:423-427.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 423-427
    • Spang, A.1
  • 43
    • 0037046145 scopus 로고    scopus 로고
    • Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3
    • Austin C., et al. Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3. Biochemistry 2002, 41:4669-4677.
    • (2002) Biochemistry , vol.41 , pp. 4669-4677
    • Austin, C.1
  • 44
    • 34347382638 scopus 로고    scopus 로고
    • PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal
    • Wang J., et al. PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal. Mol. Biol. Cell 2007, 18:2646-2655.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2646-2655
    • Wang, J.1
  • 45
    • 0034599528 scopus 로고    scopus 로고
    • GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex
    • Dell'Angelica E.C., et al. GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J. Cell Biol. 2000, 149:81-94.
    • (2000) J. Cell Biol. , vol.149 , pp. 81-94
    • Dell'Angelica, E.C.1
  • 46
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: adaptors on the move
    • Bonifacino J.S. The GGA proteins: adaptors on the move. Nat. Rev. Mol. Cell Biol. 2004, 5:23-32.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 47
    • 77952396703 scopus 로고    scopus 로고
    • Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling
    • Szentpetery Z., et al. Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:8225-8230.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 8225-8230
    • Szentpetery, Z.1
  • 48
    • 0037328750 scopus 로고    scopus 로고
    • EpsinR: an ENTH domain-containing protein that interacts with AP-1
    • Hirst J., et al. EpsinR: an ENTH domain-containing protein that interacts with AP-1. Mol. Biol. Cell 2003, 14:625-641.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 625-641
    • Hirst, J.1
  • 49
    • 67949092932 scopus 로고    scopus 로고
    • AP-3-dependent trafficking and disease: the first decade
    • Dell'Angelica E.C. AP-3-dependent trafficking and disease: the first decade. Curr. Opin. Cell Biol. 2009, 21:552-559.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 552-559
    • Dell'Angelica, E.C.1
  • 50
    • 44949264001 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-kinase type II alpha contains an AP-3-sorting motif and a kinase domain that are both required for endosome traffic
    • Craige B., et al. Phosphatidylinositol-4-kinase type II alpha contains an AP-3-sorting motif and a kinase domain that are both required for endosome traffic. Mol. Biol. Cell 2008, 19:1415-1426.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1415-1426
    • Craige, B.1
  • 51
    • 59449092912 scopus 로고    scopus 로고
    • Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal cells
    • Salazar G., et al. Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal cells. J. Biol. Chem. 2009, 284:1790-1802.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1790-1802
    • Salazar, G.1
  • 52
    • 12844258045 scopus 로고    scopus 로고
    • Synthetic genetic array analysis of the PtdIns 4-kinase Pik1p identifies components in a Golgi-specific Ypt31/rab-GTPase signaling pathway
    • Sciorra V.A., et al. Synthetic genetic array analysis of the PtdIns 4-kinase Pik1p identifies components in a Golgi-specific Ypt31/rab-GTPase signaling pathway. Mol. Biol. Cell 2005, 16:776-793.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 776-793
    • Sciorra, V.A.1
  • 53
    • 77953022901 scopus 로고    scopus 로고
    • Interaction between Sec7p and Pik1p: the first clue for the regulation of a coincidence detection signal
    • Gloor Y., et al. Interaction between Sec7p and Pik1p: the first clue for the regulation of a coincidence detection signal. Eur. J. Cell Biol. 2010, 89:575-583.
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 575-583
    • Gloor, Y.1
  • 54
    • 47649118467 scopus 로고    scopus 로고
    • The clathrin adaptor Gga2p is a phosphatidylinositol 4-phosphate effector at the Golgi exit
    • Demmel L., et al. The clathrin adaptor Gga2p is a phosphatidylinositol 4-phosphate effector at the Golgi exit. Mol. Biol. Cell 2008, 19:1991-2002.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1991-2002
    • Demmel, L.1
  • 55
    • 0038032921 scopus 로고    scopus 로고
    • The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a yeast TGN-to-endosome pathway distinct from the GGA protein-dependent pathway
    • Ha S.A., et al. The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a yeast TGN-to-endosome pathway distinct from the GGA protein-dependent pathway. Mol. Biol. Cell 2003, 14:1319-1333.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1319-1333
    • Ha, S.A.1
  • 56
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles C.R., et al. The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 1997, 91:109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1
  • 57
    • 33749011468 scopus 로고    scopus 로고
    • Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast
    • Wang C.W., et al. Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast. J. Cell Biol. 2006, 174:973-983.
    • (2006) J. Cell Biol. , vol.174 , pp. 973-983
    • Wang, C.W.1
  • 58
    • 73949113376 scopus 로고    scopus 로고
    • The exomer coat complex transports Fus1p to the plasma membrane via a novel plasma membrane sorting signal in yeast
    • Barfield R.M., et al. The exomer coat complex transports Fus1p to the plasma membrane via a novel plasma membrane sorting signal in yeast. Mol. Biol. Cell 2009, 20:4985-4996.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4985-4996
    • Barfield, R.M.1
  • 59
    • 33644854880 scopus 로고    scopus 로고
    • Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi
    • Trautwein M., et al. Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi. EMBO J. 2006, 25:943-954.
    • (2006) EMBO J. , vol.25 , pp. 943-954
    • Trautwein, M.1
  • 60
    • 2342556630 scopus 로고    scopus 로고
    • FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P
    • Godi A., et al. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat. Cell Biol. 2004, 6:393-404.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 393-404
    • Godi, A.1
  • 61
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Vieira O.V., et al. FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J. Cell Biol. 2005, 170:521-526.
    • (2005) J. Cell Biol. , vol.170 , pp. 521-526
    • Vieira, O.V.1
  • 62
    • 77950370938 scopus 로고    scopus 로고
    • Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains
    • Lenoir M., et al. Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains. EMBO Rep. 2010, 11:279-284.
    • (2010) EMBO Rep. , vol.11 , pp. 279-284
    • Lenoir, M.1
  • 63
    • 79151470948 scopus 로고    scopus 로고
    • Coordination of Golgi functions by phosphatidylinositol 4-kinases
    • Graham T.R., Burd C.G. Coordination of Golgi functions by phosphatidylinositol 4-kinases. Trends Cell Biol. 2011, 21:113-121.
    • (2011) Trends Cell Biol. , vol.21 , pp. 113-121
    • Graham, T.R.1    Burd, C.G.2
  • 64
    • 7444259627 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex
    • de Graaf P., et al. Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex. Mol. Biol. Cell 2004, 15:2038-2047.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2038-2047
    • de Graaf, P.1
  • 65
    • 33645316071 scopus 로고    scopus 로고
    • A role for the RabA4b effector protein PI-4Kbeta1 in polarized expansion of root hair cells in Arabidopsis thaliana
    • Preuss M.L., et al. A role for the RabA4b effector protein PI-4Kbeta1 in polarized expansion of root hair cells in Arabidopsis thaliana. J. Cell Biol. 2006, 172:991-998.
    • (2006) J. Cell Biol. , vol.172 , pp. 991-998
    • Preuss, M.L.1
  • 66
    • 74049162362 scopus 로고    scopus 로고
    • Dual roles for the Drosophila PI 4-kinase four wheel drive in localizing Rab11 during cytokinesis
    • Polevoy G., et al. Dual roles for the Drosophila PI 4-kinase four wheel drive in localizing Rab11 during cytokinesis. J. Cell Biol. 2009, 187:847-858.
    • (2009) J. Cell Biol. , vol.187 , pp. 847-858
    • Polevoy, G.1
  • 67
    • 77954368281 scopus 로고    scopus 로고
    • The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes
    • Dumaresq-Doiron K., et al. The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes. J. Cell Sci. 2010, 123:2273-2280.
    • (2010) J. Cell Sci. , vol.123 , pp. 2273-2280
    • Dumaresq-Doiron, K.1
  • 68
    • 0030930514 scopus 로고    scopus 로고
    • Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles
    • Walch-Solimena C., et al. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 1997, 137:1495-1509.
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-1509
    • Walch-Solimena, C.1
  • 69
    • 0037054540 scopus 로고    scopus 로고
    • Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast
    • Ortiz D., et al. Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J. Cell Biol. 2002, 157:1005-1015.
    • (2002) J. Cell Biol. , vol.157 , pp. 1005-1015
    • Ortiz, D.1
  • 70
    • 77952943084 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate controls both membrane recruitment and a regulatory switch of the Rab GEF Sec2p
    • Mizuno-Yamasaki E., et al. Phosphatidylinositol 4-phosphate controls both membrane recruitment and a regulatory switch of the Rab GEF Sec2p. Dev. Cell 2010, 18:828-840.
    • (2010) Dev. Cell , vol.18 , pp. 828-840
    • Mizuno-Yamasaki, E.1
  • 71
    • 33744739840 scopus 로고    scopus 로고
    • The rab exchange factor Sec2p reversibly associates with the exocyst
    • Medkova M., et al. The rab exchange factor Sec2p reversibly associates with the exocyst. Mol. Biol. Cell 2006, 17:2757-2769.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2757-2769
    • Medkova, M.1
  • 72
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • Pruyne D.W., et al. Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J. Cell Biol. 1998, 143:1931-1945.
    • (1998) J. Cell Biol. , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1
  • 73
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • Schott D., et al. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol. 1999, 147:791-808.
    • (1999) J. Cell Biol. , vol.147 , pp. 791-808
    • Schott, D.1
  • 74
    • 0037033787 scopus 로고    scopus 로고
    • Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length
    • Schott D.H., et al. Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length. J. Cell Biol. 2002, 156:35-39.
    • (2002) J. Cell Biol. , vol.156 , pp. 35-39
    • Schott, D.H.1
  • 75
    • 8444223155 scopus 로고    scopus 로고
    • Mechanisms of polarized growth and organelle segregation in yeast
    • Pruyne D., et al. Mechanisms of polarized growth and organelle segregation in yeast. Annu. Rev. Cell Dev. Biol. 2004, 20:559-591.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 559-591
    • Pruyne, D.1
  • 76
    • 78651445373 scopus 로고    scopus 로고
    • PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast
    • Santiago-Tirado F.H., et al. PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast. Dev. Cell 2011, 20:47-59.
    • (2011) Dev. Cell , vol.20 , pp. 47-59
    • Santiago-Tirado, F.H.1
  • 77
    • 77955056034 scopus 로고    scopus 로고
    • Manipulation of host membrane machinery by bacterial pathogens
    • Cossart P., Roy C.R. Manipulation of host membrane machinery by bacterial pathogens. Curr. Opin. Cell Biol. 2010, 22:547-554.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 547-554
    • Cossart, P.1    Roy, C.R.2
  • 78
    • 0017662282 scopus 로고
    • Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory disease
    • McDade J.E., et al. Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory disease. N. Engl. J. Med. 1977, 297:1197-1203.
    • (1977) N. Engl. J. Med. , vol.297 , pp. 1197-1203
    • McDade, J.E.1
  • 79
    • 33646915714 scopus 로고    scopus 로고
    • Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole
    • Weber S.S., et al. Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole. PLoS Pathog. 2006, 2:e46.
    • (2006) PLoS Pathog. , vol.2
    • Weber, S.S.1
  • 80
    • 64149084796 scopus 로고    scopus 로고
    • Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila
    • Brombacher E., et al. Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila. J. Biol. Chem. 2009, 284:4846-4856.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4846-4856
    • Brombacher, E.1
  • 81
    • 55749101951 scopus 로고    scopus 로고
    • The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole
    • Ragaz C., et al. The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole. Cell Microbiol. 2008, 10:2416-2433.
    • (2008) Cell Microbiol. , vol.10 , pp. 2416-2433
    • Ragaz, C.1
  • 82
    • 58149183673 scopus 로고    scopus 로고
    • Proteome analysis of Legionella vacuoles purified by magnetic immunoseparation reveals secretory and endosomal GTPases
    • Urwyler S., et al. Proteome analysis of Legionella vacuoles purified by magnetic immunoseparation reveals secretory and endosomal GTPases. Traffic 2009, 10:76-87.
    • (2009) Traffic , vol.10 , pp. 76-87
    • Urwyler, S.1
  • 83
    • 0141669008 scopus 로고    scopus 로고
    • Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner
    • Rzomp K.A., et al. Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner. Infect. Immun. 2003, 71:5855-5870.
    • (2003) Infect. Immun. , vol.71 , pp. 5855-5870
    • Rzomp, K.A.1
  • 84
    • 77951231154 scopus 로고    scopus 로고
    • Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion
    • Moorhead A.M., et al. Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion. Infect. Immun. 2010, 78:1990-2007.
    • (2010) Infect. Immun. , vol.78 , pp. 1990-2007
    • Moorhead, A.M.1
  • 85
    • 78149451596 scopus 로고    scopus 로고
    • Phosphoinositides are essential coactivators for p21-activated kinase 1
    • Strochlic T.I., et al. Phosphoinositides are essential coactivators for p21-activated kinase 1. Mol. Cell 2010, 40:493-500.
    • (2010) Mol. Cell , vol.40 , pp. 493-500
    • Strochlic, T.I.1
  • 86
    • 29144458344 scopus 로고    scopus 로고
    • Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus
    • Strahl T., et al. Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus. J. Cell Biol. 2005, 171:967-979.
    • (2005) J. Cell Biol. , vol.171 , pp. 967-979
    • Strahl, T.1
  • 87
    • 84960994832 scopus 로고
    • Enzyme secretion and the incorporation of P32 into phospholipides of pancreas slices
    • Hokin M.R., Hokin L.E. Enzyme secretion and the incorporation of P32 into phospholipides of pancreas slices. J. Biol. Chem. 1953, 203:967-977.
    • (1953) J. Biol. Chem. , vol.203 , pp. 967-977
    • Hokin, M.R.1    Hokin, L.E.2
  • 88
    • 0343168409 scopus 로고
    • Phosphoinositides and protein secretion in pancreas slices
    • Hokin L.E., Hokin M.R. Phosphoinositides and protein secretion in pancreas slices. J. Biol. Chem. 1958, 233:805-810.
    • (1958) J. Biol. Chem. , vol.233 , pp. 805-810
    • Hokin, L.E.1    Hokin, M.R.2
  • 89
    • 0016613531 scopus 로고
    • Inositol phospholipids and cell surface receptor function
    • Michell R.H. Inositol phospholipids and cell surface receptor function. Biochim. Biophys. Acta 1975, 415:81-147.
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 81-147
    • Michell, R.H.1
  • 90
    • 0017353659 scopus 로고
    • Acetylcholine increases the breakdown of triphosphoinositide of rabbit iris muscle prelabelled with [32P] phosphate
    • Abdel-Latif A.A., et al. Acetylcholine increases the breakdown of triphosphoinositide of rabbit iris muscle prelabelled with [32P] phosphate. Biochem. J. 1977, 162:61-73.
    • (1977) Biochem. J. , vol.162 , pp. 61-73
    • Abdel-Latif, A.A.1
  • 91
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge M.J., Irvine R.F. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature 1984, 312:315-321.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 92
    • 0025216568 scopus 로고
    • Human platelets form 3-phosphorylated phosphoinositides in response to alpha-thrombin, U46619, or GTP gamma S
    • Kucera G.L., Rittenhouse S.E. Human platelets form 3-phosphorylated phosphoinositides in response to alpha-thrombin, U46619, or GTP gamma S. J. Biol. Chem. 1990, 265:5345-5348.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5345-5348
    • Kucera, G.L.1    Rittenhouse, S.E.2
  • 93
    • 0026654026 scopus 로고
    • Platelet-derived growth factor stimulates synthesis of PtdIns(3,4,5)P3 by activating a PtdIns(4,5)P2 3-OH kinase
    • Hawkins P.T., et al. Platelet-derived growth factor stimulates synthesis of PtdIns(3,4,5)P3 by activating a PtdIns(4,5)P2 3-OH kinase. Nature 1992, 358:157-159.
    • (1992) Nature , vol.358 , pp. 157-159
    • Hawkins, P.T.1
  • 94
    • 0141787150 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3
    • Hilpela P., et al. Regulation of the actin cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3. Curr. Top. Microbiol. Immunol. 2004, 282:117-163.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.282 , pp. 117-163
    • Hilpela, P.1
  • 95
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan J.E., et al. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 1994, 371:168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1
  • 96
    • 0030939005 scopus 로고    scopus 로고
    • Specific role for the PH domain of dynamin-1 in the regulation of rapid endocytosis in adrenal chromaffin cells
    • Artalejo C.R., et al. Specific role for the PH domain of dynamin-1 in the regulation of rapid endocytosis in adrenal chromaffin cells. EMBO J. 1997, 16:1565-1574.
    • (1997) EMBO J. , vol.16 , pp. 1565-1574
    • Artalejo, C.R.1
  • 97
    • 0032493134 scopus 로고    scopus 로고
    • Inhibition of mSOS-activity by binding of phosphatidylinositol 4,5-P2 to the mSOS pleckstrin homology domain
    • Jefferson A.B., et al. Inhibition of mSOS-activity by binding of phosphatidylinositol 4,5-P2 to the mSOS pleckstrin homology domain. Oncogene 1998, 16:2303-2310.
    • (1998) Oncogene , vol.16 , pp. 2303-2310
    • Jefferson, A.B.1
  • 98
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi R., et al. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J. Cell Biol. 2000, 150:1299-1310.
    • (2000) J. Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1
  • 99
    • 0028270099 scopus 로고
    • Travelling in style: the cell biology of pollen
    • Bedinger P.A., et al. Travelling in style: the cell biology of pollen. Trends Cell Biol. 1994, 4:132-138.
    • (1994) Trends Cell Biol. , vol.4 , pp. 132-138
    • Bedinger, P.A.1
  • 100
    • 0344417107 scopus 로고    scopus 로고
    • Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth
    • Kost B., et al. Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth. J. Cell Biol. 1999, 145:317-330.
    • (1999) J. Cell Biol. , vol.145 , pp. 317-330
    • Kost, B.1
  • 101
    • 20044394532 scopus 로고    scopus 로고
    • Phosphoinositides and phosphatidic acid regulate pollen tube growth and reorientation through modulation of [Ca2+]c and membrane secretion
    • Monteiro D., et al. Phosphoinositides and phosphatidic acid regulate pollen tube growth and reorientation through modulation of [Ca2+]c and membrane secretion. J. Exp. Bot. 2005, 56:1665-1674.
    • (2005) J. Exp. Bot. , vol.56 , pp. 1665-1674
    • Monteiro, D.1
  • 102
    • 33947518847 scopus 로고    scopus 로고
    • Pollen tube tip growth depends on plasma membrane polarization mediated by tobacco PLC3 activity and endocytic membrane recycling
    • Helling D., et al. Pollen tube tip growth depends on plasma membrane polarization mediated by tobacco PLC3 activity and endocytic membrane recycling. Plant Cell 2006, 18:3519-3534.
    • (2006) Plant Cell , vol.18 , pp. 3519-3534
    • Helling, D.1
  • 103
    • 53749095272 scopus 로고    scopus 로고
    • The Arabidopsis phosphatidylinositol 3-kinase is important for pollen development
    • Lee Y., et al. The Arabidopsis phosphatidylinositol 3-kinase is important for pollen development. Plant Physiol. 2008, 147:1886-1897.
    • (2008) Plant Physiol. , vol.147 , pp. 1886-1897
    • Lee, Y.1
  • 104
    • 0030669546 scopus 로고    scopus 로고
    • Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis
    • Dove S.K., et al. Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis. Nature 1997, 390:187-192.
    • (1997) Nature , vol.390 , pp. 187-192
    • Dove, S.K.1
  • 105
    • 71049136485 scopus 로고    scopus 로고
    • Arabidopsis FAB1/PIKfyve proteins are essential for development of viable pollen
    • Whitley P., et al. Arabidopsis FAB1/PIKfyve proteins are essential for development of viable pollen. Plant Physiol. 2009, 151:1812-1822.
    • (2009) Plant Physiol. , vol.151 , pp. 1812-1822
    • Whitley, P.1
  • 106
    • 79551706977 scopus 로고    scopus 로고
    • Loss-of-function and gain-of-function mutations in FAB1A/B impair endomembrane homeostasis, conferring pleiotropic developmental abnormalities in arabidopsis
    • Hirano T., et al. Loss-of-function and gain-of-function mutations in FAB1A/B impair endomembrane homeostasis, conferring pleiotropic developmental abnormalities in arabidopsis. Plant Physiol. 2011, 155:797-807.
    • (2011) Plant Physiol. , vol.155 , pp. 797-807
    • Hirano, T.1
  • 107
    • 56349113288 scopus 로고    scopus 로고
    • Phosphoinositides in plants: novel functions in membrane trafficking
    • Thole J.M., Nielsen E. Phosphoinositides in plants: novel functions in membrane trafficking. Curr. Opin. Plant Biol. 2008, 11:620-631.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 620-631
    • Thole, J.M.1    Nielsen, E.2
  • 108
    • 58349120191 scopus 로고    scopus 로고
    • Imaging phosphatidylinositol 4-phosphate dynamics in living plant cells
    • Vermeer J.E., et al. Imaging phosphatidylinositol 4-phosphate dynamics in living plant cells. Plant J. 2009, 57:356-372.
    • (2009) Plant J. , vol.57 , pp. 356-372
    • Vermeer, J.E.1
  • 109
    • 79751495582 scopus 로고    scopus 로고
    • Electron Tomography of RabA4b- and PI-4Kbeta1-Labeled Trans Golgi Network Compartments in Arabidopsis
    • Kang B.H., et al. Electron Tomography of RabA4b- and PI-4Kbeta1-Labeled Trans Golgi Network Compartments in Arabidopsis. Traffic 2011, 12:313-329.
    • (2011) Traffic , vol.12 , pp. 313-329
    • Kang, B.H.1
  • 110
    • 48249135589 scopus 로고    scopus 로고
    • Root hair defective4 encodes a phosphatidylinositol-4-phosphate phosphatase required for proper root hair development in Arabidopsis thaliana
    • Thole J.M., et al. Root hair defective4 encodes a phosphatidylinositol-4-phosphate phosphatase required for proper root hair development in Arabidopsis thaliana. Plant Cell 2008, 20:381-395.
    • (2008) Plant Cell , vol.20 , pp. 381-395
    • Thole, J.M.1
  • 111
    • 20044391625 scopus 로고    scopus 로고
    • A Sec14p-nodulin domain phosphatidylinositol transfer protein polarizes membrane growth of Arabidopsis thaliana root hairs
    • Vincent P., et al. A Sec14p-nodulin domain phosphatidylinositol transfer protein polarizes membrane growth of Arabidopsis thaliana root hairs. J. Cell Biol. 2005, 168:801-812.
    • (2005) J. Cell Biol. , vol.168 , pp. 801-812
    • Vincent, P.1
  • 112
    • 10344240413 scopus 로고    scopus 로고
    • The Arabidopsis COW1 gene encodes a phosphatidylinositol transfer protein essential for root hair tip growth
    • Bohme K., et al. The Arabidopsis COW1 gene encodes a phosphatidylinositol transfer protein essential for root hair tip growth. Plant J. 2004, 40:686-698.
    • (2004) Plant J. , vol.40 , pp. 686-698
    • Bohme, K.1
  • 113
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol-binding protein recognizes a determinant specific to Golgi membranes
    • Levine T.P., Munro S. The pleckstrin homology domain of oxysterol-binding protein recognizes a determinant specific to Golgi membranes. Curr. Biol. 1998, 8:729-739.
    • (1998) Curr. Biol. , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2
  • 114
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • Levine T.P., Munro S. Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol. Biol. Cell 2001, 12:1633-1644.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 115
    • 0036544518 scopus 로고    scopus 로고
    • Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex
    • Li X., et al. Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. J. Cell Biol. 2002, 157:63-77.
    • (2002) J. Cell Biol. , vol.157 , pp. 63-77
    • Li, X.1
  • 116
    • 2342430611 scopus 로고    scopus 로고
    • The p21-activated protein kinase-related kinase Cla4 is a coincidence detector of signaling by Cdc42 and phosphatidylinositol 4-phosphate
    • Wild A.C., et al. The p21-activated protein kinase-related kinase Cla4 is a coincidence detector of signaling by Cdc42 and phosphatidylinositol 4-phosphate. J. Biol. Chem. 2004, 279:17101-17110.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17101-17110
    • Wild, A.C.1
  • 117
    • 33747402357 scopus 로고    scopus 로고
    • PI4P-signaling pathway for the synthesis of a nascent membrane structure in selective autophagy
    • Yamashita S., et al. PI4P-signaling pathway for the synthesis of a nascent membrane structure in selective autophagy. J. Cell Biol. 2006, 173:709-717.
    • (2006) J. Cell Biol. , vol.173 , pp. 709-717
    • Yamashita, S.1
  • 118
    • 34548483180 scopus 로고    scopus 로고
    • Structural and membrane binding analysis of the Phox homology domain of Bem1p: basis of phosphatidylinositol 4-phosphate specificity
    • Stahelin R.V., et al. Structural and membrane binding analysis of the Phox homology domain of Bem1p: basis of phosphatidylinositol 4-phosphate specificity. J. Biol. Chem. 2007, 282:25737-25747.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25737-25747
    • Stahelin, R.V.1
  • 119
    • 73349131126 scopus 로고    scopus 로고
    • Regulation of a Golgi flippase by phosphoinositides and an ArfGEF
    • Natarajan P., et al. Regulation of a Golgi flippase by phosphoinositides and an ArfGEF. Nat. Cell Biol. 2009, 11:1421-1426.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1421-1426
    • Natarajan, P.1
  • 120
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S., et al. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 2000, 351:19-31.
    • (2000) Biochem. J. , vol.351 , pp. 19-31
    • Dowler, S.1
  • 121
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components
    • Levine T.P., Munro S. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components. Curr. Biol. 2002, 12:695-704.
    • (2002) Curr. Biol. , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.