메뉴 건너뛰기




Volumn 37, Issue 2, 2012, Pages 141-154

Arf1 and arf3 are required for the integrity of recycling endosomes and the recycling pathway

Author keywords

ARF; Endosome; Golgi; Recycling; Small GTPase

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; ARF3 PROTEIN, HUMAN; RAB PROTEIN; RAB11 PROTEIN; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 84874041428     PISSN: 03867196     EISSN: 13473700     Source Type: Journal    
DOI: 10.1247/csf.12015     Document Type: Article
Times cited : (52)

References (50)
  • 1
    • 33745183370 scopus 로고    scopus 로고
    • A Phosphatidylinositol-3-Kinase-Dependent Signal Transition Regulates ARF1 and ARF6 during Fcγ Receptor-Mediated Phagocytosis
    • Beemiller, P., Hoppe, A.D., and Swanson, J.A. 2006. A Phosphatidylinositol-3-Kinase-Dependent Signal Transition Regulates ARF1 and ARF6 during Fcγ Receptor-Mediated Phagocytosis. PLoS Biol., 4: e162.
    • (2006) PLoS Biol , vol.4 , pp. e162
    • Beemiller, P.1    Hoppe, A.D.2    Swanson, J.A.3
  • 2
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown, H.A., Gutowski, S., Moomaw, C.R., Slaughter, C., and Sternweis, P.C. 1993. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell, 75: 1137–1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 5
    • 68949091932 scopus 로고    scopus 로고
    • Phosphatidic acid regulation of phosphatidylinositol 4-phosphate 5-kinases
    • Cockcroft, S. 2009. Phosphatidic acid regulation of phosphatidylinositol 4-phosphate 5-kinases. Biochim. Biophys. Acta, 1791: 905–912.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 905-912
    • Cockcroft, S.1
  • 6
    • 34250313651 scopus 로고    scopus 로고
    • Active Arf6 Recruits ARNO/Cytohesin GEFs to the PM by Binding Their PH Domains
    • Cohen, L.A., Honda, A., Varnai, P., Brown, F.D., Balla, T., and Donaldson, J.G. 2007. Active Arf6 Recruits ARNO/Cytohesin GEFs to the PM by Binding Their PH Domains. Mol. Biol. Cell, 18: 2244–2253.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2244-2253
    • Cohen, L.A.1    Honda, A.2    Varnai, P.3    Brown, F.D.4    Balla, T.5    Donaldson, J.G.6
  • 7
  • 8
    • 0026321613 scopus 로고
    • Effects of brefeldin A on the endocytic route. Redistribution of mannose 6-phosphate/insulin-like growth factor II receptors to the cell surface
    • Damke, H., Klumperman, J., von Figura, K., and Braulke, T. 1991. Effects of brefeldin A on the endocytic route. Redistribution of mannose 6-phosphate/insulin-like growth factor II receptors to the cell surface. J. Biol. Chem., 266: 24829–24833.
    • (1991) J. Biol. Chem , vol.266 , pp. 24829-24833
    • Damke, H.1    Klumperman, J.2    von Figura, K.3    Braulke, T.4
  • 9
    • 68949164754 scopus 로고    scopus 로고
    • Phospholipase D in endocytosis and endosomal recycling pathways
    • Donaldson, J.G. 2009. Phospholipase D in endocytosis and endosomal recycling pathways. Biochim. Biophys. Acta, 1791: 845–849.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 845-849
    • Donaldson, J.G.1
  • 10
    • 0032563568 scopus 로고    scopus 로고
    • An Endocytosed TGN38 Chimeric Protein Is Delivered to the TGN after Trafficking through the Endocytic Recycling Compartment in CHO Cells
    • Ghosh, R.N., Mallet, W.G., Soe, T.T., McGraw, T.E., and Maxfield, F.R. 1998. An Endocytosed TGN38 Chimeric Protein Is Delivered to the TGN after Trafficking through the Endocytic Recycling Compartment in CHO Cells. J. Cell Biol., 142: 923–936.
    • (1998) J. Cell Biol , vol.142 , pp. 923-936
    • Ghosh, R.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 11
    • 38149068433 scopus 로고    scopus 로고
    • The Small G Proteins of the Arf Family and Their Regulators
    • Gillingham, A.K. and Munro, S. 2007. The Small G Proteins of the Arf Family and Their Regulators. Ann. Rev. Cell Dev. Biol., 23: 579–611.
    • (2007) Ann. Rev. Cell Dev. Biol , vol.23 , pp. 579-611
    • Gillingham, A.K.1    Munro, S.2
  • 12
    • 0029807379 scopus 로고    scopus 로고
    • Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1–ARF6)
    • Hosaka, M., Toda, K., Takatsu, H., Torii, S., Murakami, K., and Nakayama, K. 1996. Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1–ARF6). J. Biochem. (Tokyo), 120: 813–819.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 813-819
    • Hosaka, M.1    Toda, K.2    Takatsu, H.3    Torii, S.4    Murakami, K.5    Nakayama, K.6
  • 13
    • 33746175744 scopus 로고    scopus 로고
    • AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors
    • Ishizaki, R., Shin, H.W., Iguchi-Ariga, S.M., Ariga, H., and Nakayama, K. 2006. AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors. Genes Cells, 11: 949–959.
    • (2006) Genes Cells , vol.11 , pp. 949-959
    • Ishizaki, R.1    Shin, H.W.2    Iguchi-Ariga, S.M.3    Ariga, H.4    Nakayama, K.5
  • 14
    • 48749130156 scopus 로고    scopus 로고
    • Redun-dant Roles of BIG2 and BIG1, Guanine-Nucleotide Exchange Factors for ADP-Ribosylation Factors in Membrane Traffic between the trans-Golgi Network and Endosomes
    • Ishizaki, R., Shin, H.-W., Mitsuhashi, H., and Nakayama, K. 2008. Redun-dant Roles of BIG2 and BIG1, Guanine-Nucleotide Exchange Factors for ADP-Ribosylation Factors in Membrane Traffic between the trans-Golgi Network and Endosomes. Mol. Biol. Cell, 19: 2650–2660.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2650-2660
    • Ishizaki, R.1    Shin, H.-W.2    Mitsuhashi, H.3    Nakayama, K.4
  • 15
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors
    • Jackson, C.L. and Casanova, J.E. 2000. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol., 10: 60–67.
    • (2000) Trends Cell Biol , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 16
    • 0033166062 scopus 로고    scopus 로고
    • ADP ribosyla-tion factor 1 mutants identify a phospholipase D effector region and reveal that phospholipase D participates in lysosomal secretion but is not sufficient for recruitment of coatomer I
    • (Pt 1)
    • Jones, D.H., Bax, B., Fensome, A., and Cockcroft, S. 1999. ADP ribosyla-tion factor 1 mutants identify a phospholipase D effector region and reveal that phospholipase D participates in lysosomal secretion but is not sufficient for recruitment of coatomer I. Biochem. J., 341(Pt 1): 185–192.
    • (1999) Biochem. J , vol.341 , pp. 185-192
    • Jones, D.H.1    Bax, B.2    Fensome, A.3    Cockcroft, S.4
  • 17
    • 30044435325 scopus 로고    scopus 로고
    • An Effector Domain Mutant of Arf6 Implicates Phospholipase D in Endosomal Membrane Recycling
    • Jovanovic, O.A., Brown, F.D., and Donaldson, J.G. 2006. An Effector Domain Mutant of Arf6 Implicates Phospholipase D in Endosomal Membrane Recycling. Mol. Biol. Cell, 17: 327–335.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 327-335
    • Jovanovic, O.A.1    Brown, F.D.2    Donaldson, J.G.3
  • 18
    • 33644526287 scopus 로고    scopus 로고
    • Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins
    • Kahn, R.A., Cherfils, J., Elias, M., Lovering, R.C., Munro, S., and Schurmann, A. 2006. Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins. J. Cell Biol., 172: 645– 650.
    • (2006) J. Cell Biol , vol.172 , pp. 645-650
    • Kahn, R.A.1    Cherfils, J.2    Elias, M.3    Lovering, R.C.4    Munro, S.5    Schurmann, A.6
  • 19
    • 0031974495 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel human trans-Golgi network glyco-protein, TGN51, that contains multiple tyrosine-containing motifs
    • Kain, R., Angata, K., Kerjaschki, D., and Fukuda, M. 1998. Molecular cloning and expression of a novel human trans-Golgi network glyco-protein, TGN51, that contains multiple tyrosine-containing motifs. J. Biol. Chem., 273: 981–988.
    • (1998) J. Biol. Chem , vol.273 , pp. 981-988
    • Kain, R.1    Angata, K.2    Kerjaschki, D.3    Fukuda, M.4
  • 20
    • 0036017789 scopus 로고    scopus 로고
    • GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat
    • Kawamoto, K., Yoshida, Y., Tamaki, H., Torii, S., Shinotsuka, C., Yamashina, S., and Nakayama, K. 2002. GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Traffic, 3: 483–495.
    • (2002) Traffic , vol.3 , pp. 483-495
    • Kawamoto, K.1    Yoshida, Y.2    Tamaki, H.3    Torii, S.4    Shinotsuka, C.5    Yamashina, S.6    Nakayama, K.7
  • 21
    • 37749001768 scopus 로고    scopus 로고
    • ARF1 is directly involved in dynamin-independent endocytosis
    • Kumari, S. and Mayor, S. 2008. ARF1 is directly involved in dynamin-independent endocytosis. Nat. Cell Biol., 10: 30–41.
    • (2008) Nat. Cell Biol , vol.10 , pp. 30-41
    • Kumari, S.1    Mayor, S.2
  • 22
    • 0027727324 scopus 로고
    • An electron microscopic study of TGN38/41 dynamics
    • Ladinsky, M.S. and Howell, K.E. 1993. An electron microscopic study of TGN38/41 dynamics. J. Cell Sci. Suppl., 17: 41–47.
    • (1993) J. Cell Sci. Suppl , vol.17 , pp. 41-47
    • Ladinsky, M.S.1    Howell, K.E.2
  • 23
    • 33745007067 scopus 로고    scopus 로고
    • The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis
    • Lee, C.S., Kim, I.S., Park, J.B., Lee, M.N., Lee, H.Y., Suh, P.G., and Ryu, S.H. 2006. The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis. Nat. Cell Biol., 8: 477–484.
    • (2006) Nat. Cell Biol , vol.8 , pp. 477-484
    • Lee, C.S.1    Kim, I.S.2    Park, J.B.3    Lee, M.N.4    Lee, H.Y.5    Suh, P.G.6    Ryu, S.H.7
  • 24
    • 0025940101 scopus 로고
    • Brefeldin A’s effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., Yuan, L., Tipper, C., Amherdt, M., Orci, L., and Klausner, R.D. 1991. Brefeldin A’s effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell, 67: 601–616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6
  • 25
    • 84861846404 scopus 로고    scopus 로고
    • Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis
    • Makyio, H., Ohgi, M., Takei, T., Takahashi, S., Takatsu, H., Katoh, Y., Hanai, A., Ueda, T., Kanaho, Y., Xie, Y., et al. 2012. Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis. EMBO J., 31: 2590–2603.
    • (2012) EMBO J , vol.31 , pp. 2590-2603
    • Makyio, H.1    Ohgi, M.2    Takei, T.3    Takahashi, S.4    Takatsu, H.5    Katoh, Y.6    Hanai, A.7    Ueda, T.8    Kanaho, Y.9    Xie, Y.10
  • 26
    • 0033606772 scopus 로고    scopus 로고
    • Chimeric forms of furin and TGN38 are transported with the plasma membrane in the trans-Golgi network via distinct endosomal pathways
    • Mallet, W.G. and Maxfield, F.R. 1999. Chimeric forms of furin and TGN38 are transported with the plasma membrane in the trans-Golgi network via distinct endosomal pathways. J. Cell Biol., 146: 345–359.
    • (1999) J. Cell Biol , vol.146 , pp. 345-359
    • Mallet, W.G.1    Maxfield, F.R.2
  • 27
    • 79953172625 scopus 로고    scopus 로고
    • Arfaptins Are Localized to the trans-Golgi by Interaction with Arl1, but Not Arfs
    • Man, Z., Kondo, Y., Koga, H., Umino, H., Nakayama, K., and Shin, H.-W. 2011. Arfaptins Are Localized to the trans-Golgi by Interaction with Arl1, but Not Arfs. J. Biol. Chem., 286: 11569–11578.
    • (2011) J. Biol. Chem , vol.286 , pp. 11569-11578
    • Man, Z.1    Kondo, Y.2    Koga, H.3    Umino, H.4    Nakayama, K.5    Shin, H.-W.6
  • 28
    • 77952950015 scopus 로고    scopus 로고
    • Arf3 is activated uniquely at the trans-Golgi network by brefeldin A-inhibited guanine nucleotide exchange factors
    • Manolea, F., Chun, J., Chen, D.W., Clarke, I., Summerfeldt, N., Dacks, J.B., and Melancon, P. 2010. Arf3 is activated uniquely at the trans-Golgi network by brefeldin A-inhibited guanine nucleotide exchange factors. Mol. Biol. Cell, 21: 1836–1849.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1836-1849
    • Manolea, F.1    Chun, J.2    Chen, D.W.3    Clarke, I.4    Summerfeldt, N.5    Dacks, J.B.6    Melancon, P.7
  • 30
    • 67449104522 scopus 로고    scopus 로고
    • Differential Effects of Depletion of ARL1 and ARFRP1 on Membrane Trafficking between the trans-Golgi Network and Endosomes
    • Nishimoto-Morita, K., Shin, H.-W., Mitsuhashi, H., Kitamura, M., Zhang, Q., Johannes, L., and Nakayama, K. 2009. Differential Effects of Depletion of ARL1 and ARFRP1 on Membrane Trafficking between the trans-Golgi Network and Endosomes. J. Biol. Chem., 284: 10583– 10592.
    • (2009) J. Biol. Chem , vol.284 , pp. 10583-10592
    • Nishimoto-Morita, K.1    Shin, H.-W.2    Mitsuhashi, H.3    Kitamura, M.4    Zhang, Q.5    Johannes, L.6    Nakayama, K.7
  • 31
    • 31944435161 scopus 로고    scopus 로고
    • Phospholipase D2 Is Required for Efficient Endocytic Recycling of Transferrin Receptors
    • Padron, D., Tall, R.D., and Roth, M.G. 2006. Phospholipase D2 Is Required for Efficient Endocytic Recycling of Transferrin Receptors. Mol. Biol. Cell, 17: 598–606.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 598-606
    • Padron, D.1    Tall, R.D.2    Roth, M.G.3
  • 32
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN
    • Reaves, B., Horn, M., and Banting, G. 1993. TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell, 4: 93–105.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 33
    • 2542466750 scopus 로고    scopus 로고
    • Role of Cytoplasmic Domain Serines in Intracellular Trafficking of Furin
    • Schapiro, F.B., Soe, T.T., Mallet, W.G., and Maxfield, F.R. 2004. Role of Cytoplasmic Domain Serines in Intracellular Trafficking of Furin. Mol. Biol. Cell, 15: 2884–2894.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2884-2894
    • Schapiro, F.B.1    Soe, T.T.2    Mallet, W.G.3    Maxfield, F.R.4
  • 34
    • 33644555815 scopus 로고    scopus 로고
    • Association of brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2) with recycling endosomes during transferrin uptake
    • Shen, X., Xu, K.-F., Fan, Q., Pacheco-Rodriguez, G., Moss, J., and Vaughan, M. 2006. Association of brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2) with recycling endosomes during transferrin uptake. Proc. Natl. Acad. Sci., 103: 2635–2640.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 2635-2640
    • Shen, X.1    Xu, K.-F.2    Fan, Q.3    Pacheco-Rodriguez, G.4    Moss, J.5    Vaughan, M.6
  • 35
    • 0030817913 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p
    • Shin, H.W., Shinotsuka, C., Torii, S., Murakami, K., and Nakayama, K. 1997. Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J. Biochem. (Tokyo), 122: 525–530.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 525-530
    • Shin, H.W.1    Shinotsuka, C.2    Torii, S.3    Murakami, K.4    Nakayama, K.5
  • 36
    • 9444274139 scopus 로고    scopus 로고
    • BIG2, a Guanine Nucleotide Exchange Factor for ADP-Ribosylation Factors: Its Localization to Recycling Endosomes and Implication in the Endosome Integrity
    • Shin, H.-W., Morinaga, N., Noda, M., and Nakayama, K. 2004. BIG2, a Guanine Nucleotide Exchange Factor for ADP-Ribosylation Factors: Its Localization to Recycling Endosomes and Implication in the Endosome Integrity. Mol. Biol. Cell, 15: 5283–5294.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5283-5294
    • Shin, H.-W.1    Morinaga, N.2    Noda, M.3    Nakayama, K.4
  • 37
    • 14944365406 scopus 로고    scopus 로고
    • Guanine Nucleotide-Exchange Factors for Arf GTPases: Their Diverse Functions in Membrane Traffic
    • Shin, H.-W. and Nakayama, K. 2004. Guanine Nucleotide-Exchange Factors for Arf GTPases: Their Diverse Functions in Membrane Traffic. J. Biochem. (Tokyo), 136: 761–767.
    • (2004) J. Biochem. (Tokyo) , vol.136 , pp. 761-767
    • Shin, H.-W.1    Nakayama, K.2
  • 38
    • 26244468567 scopus 로고    scopus 로고
    • Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking
    • Shin, H.-W., Kobayashi, H., Kitamura, M., Waguri, S., Suganuma, T., Uchiyama, Y., and Nakayama, K. 2005. Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking. J. Cell Sci., 118: 4039–4048.
    • (2005) J. Cell Sci , vol.118 , pp. 4039-4048
    • Shin, H.-W.1    Kobayashi, H.2    Kitamura, M.3    Waguri, S.4    Suganuma, T.5    Uchiyama, Y.6    Nakayama, K.7
  • 39
    • 0037155210 scopus 로고    scopus 로고
    • Mechanism of ADP ribosylation factor-stimulated phosphatidylinositol 4,5-bisphosphate synthesis in HL60 cells
    • Skippen, A., Jones, D.H., Morgan, C.P., Li, M., and Cockcroft, S. 2002. Mechanism of ADP ribosylation factor-stimulated phosphatidylinositol 4,5-bisphosphate synthesis in HL60 cells. J. Biol. Chem., 277: 5823–5831.
    • (2002) J. Biol. Chem , vol.277 , pp. 5823-5831
    • Skippen, A.1    Jones, D.H.2    Morgan, C.P.3    Li, M.4    Cockcroft, S.5
  • 40
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen, B., De Renzis, S., Nielsen, E., Rietdorf, J., and Zerial, M. 2000. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J. Cell Biol., 149: 901–914.
    • (2000) J. Cell Biol , vol.149 , pp. 901-914
    • Sonnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 42
    • 0028875689 scopus 로고
    • Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain
    • Takahashi, S., Nakagawa, T., Banno, T., Watanabe, T., Murakami, K., and Nakayama, K. 1995. Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain. J. Biol. Chem., 270: 28397–28401.
    • (1995) J. Biol. Chem , vol.270 , pp. 28397-28401
    • Takahashi, S.1    Nakagawa, T.2    Banno, T.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 43
    • 80052264931 scopus 로고    scopus 로고
    • Distinct roles of Rab11 and Arf6 in the regulation of Rab11-FIP3/arfophilin-1 localization in mitotic cells
    • Takahashi, S., Takei, T., Koga, H., Takatsu, H., Shin, H.-W., and Nakayama, K. 2011. Distinct roles of Rab11 and Arf6 in the regulation of Rab11-FIP3/arfophilin-1 localization in mitotic cells. Genes Cells, 16: 938–950.
    • (2011) Genes Cells , vol.16 , pp. 938-950
    • Takahashi, S.1    Takei, T.2    Koga, H.3    Takatsu, H.4    Shin, H.-W.5    Nakayama, K.6
  • 45
    • 0037101770 scopus 로고    scopus 로고
    • GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors
    • Takatsu, H., Yoshino, K., Toda, K., and Nakayama, K. 2002. GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. Biochem. J., 365: 369–378.
    • (2002) Biochem. J , vol.365 , pp. 369-378
    • Takatsu, H.1    Yoshino, K.2    Toda, K.3    Nakayama, K.4
  • 46
    • 0037078319 scopus 로고    scopus 로고
    • Calcium-regulated exocytosis of dense-core vesicles requires the activation of ADP-ribosylation factor (ARF)6 by ARF nucleotide binding site opener at the plasma membrane
    • Vitale, N., Chasserot-Golaz, S., Bailly, Y., Morinaga, N., Frohman, M.A., and Bader, M.F. 2002. Calcium-regulated exocytosis of dense-core vesicles requires the activation of ADP-ribosylation factor (ARF)6 by ARF nucleotide binding site opener at the plasma membrane. J. Cell Biol., 159: 79–89.
    • (2002) J. Cell Biol , vol.159 , pp. 79-89
    • Vitale, N.1    Chasserot-Golaz, S.2    Bailly, Y.3    Morinaga, N.4    Frohman, M.A.5    Bader, M.F.6
  • 47
    • 26244448510 scopus 로고    scopus 로고
    • Isoform-selective Effects of the Depletion of ADP-Ribosylation Factors 1–5 on Membrane Traffic
    • Volpicelli-Daley, L.A., Li, Y., Zhang, C.J., and Kahn, R.A. 2005. Isoform-selective Effects of the Depletion of ADP-Ribosylation Factors 1–5 on Membrane Traffic. Mol. Biol. Cell, 16: 4495–4508.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4495-4508
    • Volpicelli-Daley, L.A.1    Li, Y.2    Zhang, C.J.3    Kahn, R.A.4
  • 48
    • 0026713586 scopus 로고
    • The morphology but not the function of endosomes and lysosomes is altered by brefeldin A
    • Wood, S.A. and Brown, W.J. 1992. The morphology but not the function of endosomes and lysosomes is altered by brefeldin A. J. Cell Biol., 119: 273–285.
    • (1992) J. Cell Biol , vol.119 , pp. 273-285
    • Wood, S.A.1    Brown, W.J.2
  • 49
    • 77955114037 scopus 로고    scopus 로고
    • Functional cross-talk between Rab14 and Rab4 through a dual effector, RUFY1/Rabip4
    • Yamamoto, H., Koga, H., Katoh, Y., Takahashi, S., Nakayama, K., and Shin, H.W. 2010. Functional cross-talk between Rab14 and Rab4 through a dual effector, RUFY1/Rabip4. Mol. Biol. Cell, 21: 2746–2755.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2746-2755
    • Yamamoto, H.1    Koga, H.2    Katoh, Y.3    Takahashi, S.4    Nakayama, K.5    Shin, H.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.