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Volumn 17, Issue 8, 2007, Pages 711-716

The Arl4 Family of Small G Proteins Can Recruit the Cytohesin Arf6 Exchange Factors to the Plasma Membrane

Author keywords

CELLBIO; SIGNALING

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ARL4A PROTEIN, HUMAN; COMPLEMENTARY DNA; CYTOHESIN 2; CYTOHESIN-2; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HYBRID PROTEIN; ISOPROTEIN; UNCLASSIFIED DRUG;

EID: 34147139995     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2007.03.007     Document Type: Article
Times cited : (109)

References (37)
  • 3
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • Renault L., Guibert B., and Cherfils J. Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426 (2003) 525-530
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 4
    • 0031982629 scopus 로고    scopus 로고
    • ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6
    • Frank S., Upender S., Hansen S.H., and Casanova J.E. ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6. J. Biol. Chem. 273 (1998) 23-27
    • (1998) J. Biol. Chem. , vol.273 , pp. 23-27
    • Frank, S.1    Upender, S.2    Hansen, S.H.3    Casanova, J.E.4
  • 5
    • 0034693264 scopus 로고    scopus 로고
    • Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs
    • Klarlund J.K., Tsiaras W., Holik J.J., Chawla A., and Czech M.P. Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs. J. Biol. Chem. 275 (2000) 32816-32821
    • (2000) J. Biol. Chem. , vol.275 , pp. 32816-32821
    • Klarlund, J.K.1    Tsiaras, W.2    Holik, J.J.3    Chawla, A.4    Czech, M.P.5
  • 6
    • 6344229320 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains
    • Cronin T.C., DiNitto J.P., Czech M.P., and Lambright D.G. Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains. EMBO J. 23 (2004) 3711-3720
    • (2004) EMBO J. , vol.23 , pp. 3711-3720
    • Cronin, T.C.1    DiNitto, J.P.2    Czech, M.P.3    Lambright, D.G.4
  • 7
    • 0032499031 scopus 로고    scopus 로고
    • Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
    • Venkateswarlu K., Oatey P.B., Tavare J.M., and Cullen P.J. Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase. Curr. Biol. 8 (1998) 463-466
    • (1998) Curr. Biol. , vol.8 , pp. 463-466
    • Venkateswarlu, K.1    Oatey, P.B.2    Tavare, J.M.3    Cullen, P.J.4
  • 8
    • 0032805160 scopus 로고    scopus 로고
    • EGF- and NGF-stimulated translocation of cytohesin-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohesin-1 PH domain
    • Venkateswarlu K., Gunn-Moore F., Tavare J.M., and Cullen P.J. EGF- and NGF-stimulated translocation of cytohesin-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohesin-1 PH domain. J. Cell Sci. 112 (1999) 1957-1965
    • (1999) J. Cell Sci. , vol.112 , pp. 1957-1965
    • Venkateswarlu, K.1    Gunn-Moore, F.2    Tavare, J.M.3    Cullen, P.J.4
  • 9
    • 0034735952 scopus 로고    scopus 로고
    • Membrane targeting: What a difference a G makes
    • Cullen P.J., and Chardin P. Membrane targeting: What a difference a G makes. Curr. Biol. 10 (2000) R876-R878
    • (2000) Curr. Biol. , vol.10
    • Cullen, P.J.1    Chardin, P.2
  • 11
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for 'front-back' communication
    • Pasqualato S., Renault L., and Cherfils J. Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep. 3 (2002) 1035-1041
    • (2002) EMBO Rep. , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 12
    • 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. Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins. J. Cell Biol. 172 (2006) 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
  • 14
    • 10044297008 scopus 로고    scopus 로고
    • Functional genomic analysis of the ADP-ribosylation factor family of GTPases: Phylogeny among diverse eukaryotes and function in C. elegans
    • Li Y., Kelly W.G., Logsdon Jr. J.M., Schurko A.M., Harfe B.D., Hill-Harfe K.L., and Kahn R.A. Functional genomic analysis of the ADP-ribosylation factor family of GTPases: Phylogeny among diverse eukaryotes and function in C. elegans. FASEB J. 18 (2004) 1834-1850
    • (2004) FASEB J. , vol.18 , pp. 1834-1850
    • Li, Y.1    Kelly, W.G.2    Logsdon Jr., J.M.3    Schurko, A.M.4    Harfe, B.D.5    Hill-Harfe, K.L.6    Kahn, R.A.7
  • 15
    • 0032818978 scopus 로고    scopus 로고
    • ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup of the ARF family characterization by rapid nucleotide exchange and a nuclear localization signal
    • Jacobs S., Schilf C., Fliegert F., Koling S., Weber Y., Schurmann A., and Joost H.G. ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup of the ARF family characterization by rapid nucleotide exchange and a nuclear localization signal. FEBS Lett. 456 (1999) 384-388
    • (1999) FEBS Lett. , vol.456 , pp. 384-388
    • Jacobs, S.1    Schilf, C.2    Fliegert, F.3    Koling, S.4    Weber, Y.5    Schurmann, A.6    Joost, H.G.7
  • 16
    • 0028221481 scopus 로고
    • Cloning of two novel ADP-ribosylation factor-like proteins and characterization of their differential expression in 3T3-L1 cells
    • Schurmann A., Breiner M., Becker W., Huppertz C., Kainulainen H., Kentrup H., and Joost H.G. Cloning of two novel ADP-ribosylation factor-like proteins and characterization of their differential expression in 3T3-L1 cells. J. Biol. Chem. 269 (1994) 15683-15688
    • (1994) J. Biol. Chem. , vol.269 , pp. 15683-15688
    • Schurmann, A.1    Breiner, M.2    Becker, W.3    Huppertz, C.4    Kainulainen, H.5    Kentrup, H.6    Joost, H.G.7
  • 18
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher C., and Balch W.E. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J. Biol. Chem. 269 (1994) 1437-1448
    • (1994) J. Biol. Chem. , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 20
    • 0034602992 scopus 로고    scopus 로고
    • Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors
    • Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K., Kirby M., Moss J., and Vaughan M. Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors. J. Biol. Chem. 275 (2000) 3221-3230
    • (2000) J. Biol. Chem. , vol.275 , pp. 3221-3230
    • Ogasawara, M.1    Kim, S.C.2    Adamik, R.3    Togawa, A.4    Ferrans, V.J.5    Takeda, K.6    Kirby, M.7    Moss, J.8    Vaughan, M.9
  • 21
    • 27844469655 scopus 로고    scopus 로고
    • Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners
    • Varnai P., Bondeva T., Tamas P., Toth B., Buday L., Hunyady L., and Balla T. Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners. J. Cell Sci. 118 (2005) 4879-4888
    • (2005) J. Cell Sci. , vol.118 , pp. 4879-4888
    • Varnai, P.1    Bondeva, T.2    Tamas, P.3    Toth, B.4    Buday, L.5    Hunyady, L.6    Balla, T.7
  • 23
    • 13544249968 scopus 로고    scopus 로고
    • In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis
    • Dormann D., Weijer G., Dowler S., and Weijer C.J. In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis. J. Cell Sci. 117 (2004) 6497-6509
    • (2004) J. Cell Sci. , vol.117 , pp. 6497-6509
    • Dormann, D.1    Weijer, G.2    Dowler, S.3    Weijer, C.J.4
  • 24
    • 25844454807 scopus 로고    scopus 로고
    • Coincidence detection in phosphoinositide signaling
    • Carlton J.G., and Cullen P.J. Coincidence detection in phosphoinositide signaling. Trends Cell Biol. 15 (2005) 540-547
    • (2005) Trends Cell Biol. , vol.15 , pp. 540-547
    • Carlton, J.G.1    Cullen, P.J.2
  • 25
    • 2442663143 scopus 로고    scopus 로고
    • Membrane trafficking: Dual-key strategy
    • Itoh T., and De Camilli P. Membrane trafficking: Dual-key strategy. Nature 429 (2004) 141-143
    • (2004) Nature , vol.429 , pp. 141-143
    • Itoh, T.1    De Camilli, P.2
  • 26
    • 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 Munro S. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-Kinase-dependent and -independent components. Curr. Biol. 12 (2002) 695-704
    • (2002) Curr. Biol. , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 27
    • 0034141642 scopus 로고    scopus 로고
    • Signalling via ADP-ribosylation factor 6 lies downstream of phosphatidylinositide 3-kinase
    • Venkateswarlu K., and Cullen P.J. Signalling via ADP-ribosylation factor 6 lies downstream of phosphatidylinositide 3-kinase. Biochem. J. 345 (2000) 719-724
    • (2000) Biochem. J. , vol.345 , pp. 719-724
    • Venkateswarlu, K.1    Cullen, P.J.2
  • 28
    • 0039818755 scopus 로고    scopus 로고
    • A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1
    • Beraud-Dufour S., Robineau S., Chardin P., Paris S., Chabre M., Cherfils J., and Antonny B. A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1. EMBO J. 17 (1998) 3651-3659
    • (1998) EMBO J. , vol.17 , pp. 3651-3659
    • Beraud-Dufour, S.1    Robineau, S.2    Chardin, P.3    Paris, S.4    Chabre, M.5    Cherfils, J.6    Antonny, B.7
  • 29
    • 0030816319 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway
    • Radhakrishna H., and Donaldson J.G. ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway. J. Cell Biol. 139 (1997) 49-61
    • (1997) J. Cell Biol. , vol.139 , pp. 49-61
    • Radhakrishna, H.1    Donaldson, J.G.2
  • 30
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Schorey C., Li G., Colombo M.I., and Stahl P.D. A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267 (1995) 1175-1178
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Schorey, C.1    Li, G.2    Colombo, M.I.3    Stahl, P.D.4
  • 31
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund J.K., Guilherme A., Holik J.J., Virbasius J.V., Chawla A., and Czech M.P. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275 (1997) 1927-1930
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 32
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech M.P. Dynamics of phosphoinositides in membrane retrieval and insertion. Annu. Rev. Physiol. 65 (2003) 791-815
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 33
    • 0036484062 scopus 로고    scopus 로고
    • Drosophila's insulin/PI3-kinase pathway coordinates cellular metabolism with nutritional conditions
    • Britton J.S., Lockwood W.K., Li L., Cohen S.M., and Edgar B.A. Drosophila's insulin/PI3-kinase pathway coordinates cellular metabolism with nutritional conditions. Dev. Cell 2 (2002) 239-249
    • (2002) Dev. Cell , vol.2 , pp. 239-249
    • Britton, J.S.1    Lockwood, W.K.2    Li, L.3    Cohen, S.M.4    Edgar, B.A.5
  • 34
    • 0032532269 scopus 로고    scopus 로고
    • The mouse ADP-ribosylation factor-like 4 gene: Two separate promoters direct specific transcription in tissues and testicular germ cell
    • Jacobs S., Schurmann A., Becker W., Bockers T.M., Copeland N.G., Jenkins N.A., and Joost H.G. The mouse ADP-ribosylation factor-like 4 gene: Two separate promoters direct specific transcription in tissues and testicular germ cell. Biochem. J. 335 (1998) 259-265
    • (1998) Biochem. J. , vol.335 , pp. 259-265
    • Jacobs, S.1    Schurmann, A.2    Becker, W.3    Bockers, T.M.4    Copeland, N.G.5    Jenkins, N.A.6    Joost, H.G.7
  • 35
    • 0242266897 scopus 로고    scopus 로고
    • Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus
    • Panic B., Perisic O., Veprintsev D.B., Williams R.L., and Munro S. Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol. Cell 12 (2003) 863-874
    • (2003) Mol. Cell , vol.12 , pp. 863-874
    • Panic, B.1    Perisic, O.2    Veprintsev, D.B.3    Williams, R.L.4    Munro, S.5
  • 36
    • 2442498522 scopus 로고    scopus 로고
    • ADP-ribosylation factor (ARF)-like 7 (ARL7) is induced by cholesterol loading and participates in apolipoprotein AI-dependent cholesterol export
    • Engel T., Lueken A., Bode G., Hobohm U., Lorkowski S., Schlueter B., Rust S., Cullen P., Pech M., Assmann G., et al. ADP-ribosylation factor (ARF)-like 7 (ARL7) is induced by cholesterol loading and participates in apolipoprotein AI-dependent cholesterol export. FEBS Lett. 566 (2004) 241-246
    • (2004) FEBS Lett. , vol.566 , pp. 241-246
    • Engel, T.1    Lueken, A.2    Bode, G.3    Hobohm, U.4    Lorkowski, S.5    Schlueter, B.6    Rust, S.7    Cullen, P.8    Pech, M.9    Assmann, G.10
  • 37
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes
    • Levine T.P., and Munro S. The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes. Curr. Biol. 8 (1998) 729-739
    • (1998) Curr. Biol. , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2


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