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Volumn 14, Issue 4, 2003, Pages 1295-1307

ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1B-mediated neurite outgrowth

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; RAC1 PROTEIN; RAC3 PROTEIN; UNCLASSIFIED DRUG;

EID: 0037738555     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-07-0406     Document Type: Article
Times cited : (91)

References (43)
  • 1
    • 0022380281 scopus 로고
    • Responses of cultured neural retinal cells to substratum-bound laminin and other extracellular matrix molecules
    • Adler, R., Jerdan, J., and A.T. Hewitt. (1985). Responses of cultured neural retinal cells to substratum-bound laminin and other extracellular matrix molecules. Dev. Biol 112, 100-114.
    • (1985) Dev. Biol. , vol.112 , pp. 100-114
    • Adler, R.1    Jerdan, J.2    Hewitt, A.T.3
  • 2
    • 0031852652 scopus 로고    scopus 로고
    • Overexpression of a neural-specific Rho family GTPase, cRac1B, selectively induces enhanced neuritogenesis and neurite branching in primary neurons
    • Albertinazzi, C., Gilardelli, D., Paris, S., Longhi, R., and de Curtis, I. (1998). Overexpression of a neural-specific Rho family GTPase, cRac1B, selectively induces enhanced neuritogenesis and neurite branching in primary neurons. J. Cell Biol. 142, 815-825.
    • (1998) J. Cell Biol. , vol.142 , pp. 815-825
    • Albertinazzi, C.1    Gilardelli, D.2    Paris, S.3    Longhi, R.4    De Curtis, I.5
  • 3
    • 0033531955 scopus 로고    scopus 로고
    • Characterization of Rac and Cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases
    • Bernard, V., Pohl, B.P., and Bokoch, G.M. (1999). Characterization of Rac and Cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J. Biol. Chem. 274, 13198-13204.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13198-13204
    • Bernard, V.1    Pohl, B.P.2    Bokoch, G.M.3
  • 4
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 5
    • 0029048041 scopus 로고
    • Preferential addition of newly synthesized membrane protein at axonal growth cones
    • Craig, A.M., Wyborski, R.J., and Banker, G. (1995). Preferential addition of newly synthesized membrane protein at axonal growth cones. Nature 375, 592-594.
    • (1995) Nature , vol.375 , pp. 592-594
    • Craig, A.M.1    Wyborski, R.J.2    Banker, G.3
  • 6
    • 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. (1995). A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267, 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
  • 7
    • 0035040153 scopus 로고    scopus 로고
    • Cell migration: GAPs between membrane traffic and the cytoskeleton
    • de Curtis, I. (2001). Cell migration: GAPs between membrane traffic and the cytoskeleton. EMBO Rep. 2, 277-281.
    • (2001) EMBO Rep. , vol.2 , pp. 277-281
    • De Curtis, I.1
  • 9
    • 0033232780 scopus 로고    scopus 로고
    • Membrane recycling in the neuronal growth cone revealed by FM1-43 labeling
    • Diefenbach, T.J., Guthrie, P.B., Stier, H., Billups, B., and Kater, S.B. (1999). Membrane recycling in the neuronal growth cone revealed by FM1-43 labeling. J. Neuroscience 19, 9436-9444.
    • (1999) J. Neuroscience , vol.19 , pp. 9436-9444
    • Diefenbach, T.J.1    Guthrie, P.B.2    Stier, H.3    Billups, B.4    Kater, S.B.5
  • 10
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson, J.G., and Jackson, C.L. (2000). Regulators and effectors of the ARF GTPases. Curr. Opin. Cell Biol. 12, 475-482.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 11
    • 0023881180 scopus 로고
    • Structure of LEP100, a glycoprotein that shuttles between lysosomes and the plasma membrane, deduced from the nucleotide sequence of the encoding cDNA
    • Fambrough, D.M., Takeyasu, K., Lippincott-Schwarz, J., and Siegel, N.R. (1988). Structure of LEP100, a glycoprotein that shuttles between lysosomes and the plasma membrane, deduced from the nucleotide sequence of the encoding cDNA. J. Cell Biol. 106, 61-67.
    • (1988) J. Cell Biol. , vol.106 , pp. 61-67
    • Fambrough, D.M.1    Takeyasu, K.2    Lippincott-Schwarz, J.3    Siegel, N.R.4
  • 12
    • 0033538485 scopus 로고    scopus 로고
    • Distribution of ARF6 between membrane and cytosol is regulated by its GTPase cycle
    • Gaschet, J., and Hsu, V.W. (1999). Distribution of ARF6 between membrane and cytosol is regulated by its GTPase cycle. J. Biol. Chem. 274, 20040-20045.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20040-20045
    • Gaschet, J.1    Hsu, V.W.2
  • 13
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg, J. (1999). Structural and functional analysis of the ARF1ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96, 893-902.
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 14
    • 0030824832 scopus 로고    scopus 로고
    • Characterization of Rac3, a novel member of the Rho family
    • Haataja, L., Groffen, J., and Heisterkamp, N. (1997). Characterization of Rac3, a novel member of the Rho family. J. Biol. Chem. 272, 20384-20388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20384-20388
    • Haataja, L.1    Groffen, J.2    Heisterkamp, N.3
  • 16
    • 0017643426 scopus 로고
    • RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination
    • Lehrach, H., Diamond, D., Wozney, J.M., and Boedtker, H. (1977). RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry 16, 4743-4751.
    • (1977) Biochemistry , vol.16 , pp. 4743-4751
    • Lehrach, H.1    Diamond, D.2    Wozney, J.M.3    Boedtker, H.4
  • 17
    • 0031041168 scopus 로고    scopus 로고
    • Comparative activity of ADPribosylation factor family members in the early steps of coated vesicle formation on rat liver Golgi membranes
    • Liang, J.O., and Kornfeld, S. (1997). Comparative activity of ADPribosylation factor family members in the early steps of coated vesicle formation on rat liver Golgi membranes. J. Biol. Chem. 272, 4141-4148.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4141-4148
    • Liang, J.O.1    Kornfeld, S.2
  • 18
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • Luo, L. (2000). Rho GTPases in neuronal morphogenesis. Nat. Rev. Neurosci. 1, 173-180.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 173-180
    • Luo, L.1
  • 19
    • 0030844902 scopus 로고    scopus 로고
    • Differential expression of distinct members of the Rho family of GTP-binding proteins during neuronal development: Identification of Rac1B, a new neural-specific member of the family
    • Malosio, M.L., Gilardelli, D., Paris, S., Albertinazzi, C., and de Curtis, I. (1997). Differential expression of distinct members of the Rho family of GTP-binding proteins during neuronal development: identification of Rac1B, a new neural-specific member of the family. J. Neurosci. 17, 6717-6728.
    • (1997) J. Neurosci. , vol.17 , pp. 6717-6728
    • Malosio, M.L.1    Gilardelli, D.2    Paris, S.3    Albertinazzi, C.4    De Curtis, I.5
  • 20
    • 0033573126 scopus 로고    scopus 로고
    • Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein β
    • Mandiyan, V., Andreev, J., Schlessinger, J., and Hubbard, S.R. (1999). Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein β. EMBO J. 18, 6890-6898.
    • (1999) EMBO J. , vol.18 , pp. 6890-6898
    • Mandiyan, V.1    Andreev, J.2    Schlessinger, J.3    Hubbard, S.R.4
  • 21
  • 22
    • 0035173058 scopus 로고    scopus 로고
    • An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization
    • Mazaki, Y., et al. (2001). An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization. Mol. Biol. Cell 12, 645-662.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 645-662
    • Mazaki, Y.1
  • 23
    • 0035694169 scopus 로고    scopus 로고
    • Molecular mechanisms regulating the subcellular localization of p95APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface
    • Matafora, V., Paris, S., Dariozzi, S., and de Curtis, I. (2001). Molecular mechanisms regulating the subcellular localization of p95APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface. J Cell Sci. 114, 4509-4520.
    • (2001) J. Cell Sci. , vol.114 , pp. 4509-4520
    • Matafora, V.1    Paris, S.2    Dariozzi, S.3    De Curtis, I.4
  • 24
    • 0036231071 scopus 로고    scopus 로고
    • Analysis of the subcellular distribution of avian p95-APP2, an ARF-GAP orthologous to mammalian paxillin kinase linker
    • Paris, S., Za, L., Sporchia, B., and de Curtis, I. (2002). Analysis of the subcellular distribution of avian p95-APP2, an ARF-GAP orthologous to mammalian paxillin kinase linker. Int. J. Biochem. Cell Biol. 34, 826-837.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 826-837
    • Paris, S.1    Za, L.2    Sporchia, B.3    De Curtis, I.4
  • 25
    • 0028951905 scopus 로고
    • Overexpression of wildtype and mutant ARF1 and ARF6: Distinct perturbations of nonoverlapping membrane compartments
    • Peters, P.J., Hsu, V.W., Ooi, C.E., Finazzi, D., Teal, S.B., Oorschot, V., Donaldson, J.G., and Klausner, R.D. (1995). Overexpression of wildtype and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J. Cell Biol. 128, 1003-1017.
    • (1995) J. Cell Biol. , vol.128 , pp. 1003-1017
    • Peters, P.J.1    Hsu, V.W.2    Ooi, C.E.3    Finazzi, D.4    Teal, S.B.5    Oorschot, V.6    Donaldson, J.G.7    Klausner, R.D.8
  • 26
    • 0033508898 scopus 로고    scopus 로고
    • Dynamics of tubulovesicular recycling endosomes in hippocampal neurons
    • Prekeris, R., Foletti, D.L., and Scheller, R.H. (1999). Dynamics of tubulovesicular recycling endosomes in hippocampal neurons. J. Neurosci. 19, 10324-10337.
    • (1999) J. Neurosci. , vol.19 , pp. 10324-10337
    • Prekeris, R.1    Foletti, D.L.2    Scheller, R.H.3
  • 27
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radhakrishna, H., Al-Awar, O., Khachikian, Z., and Donaldson, J.G. (1999). ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell Sci. 112, 855-866.
    • (1999) J. Cell Sci. , vol.112 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 28
    • 0029795963 scopus 로고    scopus 로고
    • Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase
    • Radhakrishna, H., Klausner, R.D., and Donaldson, J.G. (1996). Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J. Cell Biol. 134, 935-947.
    • (1996) J. Cell Biol. , vol.134 , pp. 935-947
    • Radhakrishna, H.1    Klausner, R.D.2    Donaldson, J.G.3
  • 30
    • 0032568657 scopus 로고    scopus 로고
    • Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes
    • Ren, M., Xu, G., Zeng, J., De Lemos-Chiarandini, C., Adesnik, M., and Sabatini, D.D. (1998). Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes. Proc. Natl. Acad. Sci. USA 95, 6187-6192.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6187-6192
    • Ren, M.1    Xu, G.2    Zeng, J.3    De Lemos-Chiarandini, C.4    Adesnik, M.5    Sabatini, D.D.6
  • 31
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesion and actin stress fibers in response to growth factors
    • Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein Rho regulates the assembly of focal adhesion and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 32
    • 0033574602 scopus 로고    scopus 로고
    • Snapshots of ARF1: Implications for mechanisms of activation and inactivation
    • Roth, M.G. (1999). Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell Vol. 97, 149-152.
    • (1999) Cell , vol.97 , pp. 149-152
    • Roth, M.G.1
  • 34
    • 0035845640 scopus 로고    scopus 로고
    • Arfophilin is a common target of both class II and class III ADP-ribosylation factors
    • Shin, O.H., Couvillon, A.D., and Exton, J.H. (2001). Arfophilin is a common target of both class II and class III ADP-ribosylation factors. Biochemistry 40, 10846-10852.
    • (2001) Biochemistry , vol.40 , pp. 10846-10852
    • Shin, O.H.1    Couvillon, A.D.2    Exton, J.H.3
  • 36
    • 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
  • 37
    • 0034604293 scopus 로고    scopus 로고
    • Role of coatomer and phospholipids in GTPase-activating protein-dependent hydrolysis of GTP by ADP-ribosylation factor-1
    • Szafer, E., Pick, E., Rotman, M., Zuck, S., Huber, I., and Cassel, D. (2000). Role of coatomer and phospholipids in GTPase-activating protein-dependent hydrolysis of GTP by ADP-ribosylation factor-1. J. Biol. Chem. 275, 23615-23619.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23615-23619
    • Szafer, E.1    Pick, E.2    Rotman, M.3    Zuck, S.4    Huber, I.5    Cassel, D.6
  • 38
    • 0028863477 scopus 로고
    • Making the connection: Cytoskeletal rearrangements during growth cone guidance
    • Tanaka, E., and Sabry, J. (1995). Making the connection: cytoskeletal rearrangements during growth cone guidance. Cell 83, 171-176.
    • (1995) Cell , vol.83 , pp. 171-176
    • Tanaka, E.1    Sabry, J.2
  • 41
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • 1996
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M., and Parton, R.G. (1996). (1996). Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135, 913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 42
    • 0034607876 scopus 로고    scopus 로고
    • GIT proteins, a novel family of phosphatidylinositol 3,4,5-trisphosphate-stimulated GTPase-activating proteins for ARF6
    • Vitale, N., Patton, W.A., Moss, J., Vaughan, M., Lefkowitz, R.J., and Premont, R.T. (2000). GIT proteins, a novel family of phosphatidylinositol 3,4,5-trisphosphate-stimulated GTPase-activating proteins for ARF6. J. Biol. Chem. 275, 13901-13906.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13901-13906
    • Vitale, N.1    Patton, W.A.2    Moss, J.3    Vaughan, M.4    Lefkowitz, R.J.5    Premont, R.T.6
  • 43
    • 0028275353 scopus 로고
    • Isolation of recombinant ADP-ribosylation factor 6, a 20-kDa guanine nucleotidebinding protein, in an activated GTP-bound state
    • Welsh, C.F., Moss, J., and Vaughan, M. (1994). Isolation of recombinant ADP-ribosylation factor 6, a 20-kDa guanine nucleotidebinding protein, in an activated GTP-bound state. J. Biol. Chem. 269, 15583-15587.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15583-15587
    • Welsh, C.F.1    Moss, J.2    Vaughan, M.3


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