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Volumn 17, Issue 8, 2007, Pages 722-727

Regulation of Arf6 and ACAP1 Signaling by the PTB-Domain-Containing Adaptor Protein GULP

Author keywords

CELLBIO; SIGNALING

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; ADP-RIBOSYLATION FACTOR 6; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34047269093     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2007.03.014     Document Type: Article
Times cited : (22)

References (25)
  • 2
    • 23844548266 scopus 로고    scopus 로고
    • Localization and function of Arf family GTPases
    • Donaldson J.G., and Honda A. Localization and function of Arf family GTPases. Biochem. Soc. Trans. 33 (2005) 639-642
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 639-642
    • Donaldson, J.G.1    Honda, A.2
  • 5
    • 0346725004 scopus 로고    scopus 로고
    • Arf GAPs: Multifunctional proteins that regulate membrane traffic and actin remodelling
    • Randazzo P.A., and Hirsch D.S. Arf GAPs: Multifunctional proteins that regulate membrane traffic and actin remodelling. Cell. Signal. 16 (2004) 401-413
    • (2004) Cell. Signal. , vol.16 , pp. 401-413
    • Randazzo, P.A.1    Hirsch, D.S.2
  • 6
    • 27644528406 scopus 로고    scopus 로고
    • Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration
    • Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., and Hsu V.W. Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration. Dev. Cell 9 (2005) 663-673
    • (2005) Dev. Cell , vol.9 , pp. 663-673
    • Li, J.1    Ballif, B.A.2    Powelka, A.M.3    Dai, J.4    Gygi, S.P.5    Hsu, V.W.6
  • 7
    • 33646757519 scopus 로고    scopus 로고
    • Arf GAPs and membrane traffic
    • Nie Z., and Randazzo P.A. Arf GAPs and membrane traffic. J. Cell Sci. 119 (2006) 1203-1211
    • (2006) J. Cell Sci. , vol.119 , pp. 1203-1211
    • Nie, Z.1    Randazzo, P.A.2
  • 8
    • 0032511234 scopus 로고    scopus 로고
    • Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans
    • Liu Q.A., and Hengartner M.O. Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans. Cell 93 (1998) 961-972
    • (1998) Cell , vol.93 , pp. 961-972
    • Liu, Q.A.1    Hengartner, M.O.2
  • 9
    • 0033581828 scopus 로고    scopus 로고
    • Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6
    • Liu Q.A., and Hengartner M.O. Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6. Curr. Biol. 9 (1999) 1347-1350
    • (1999) Curr. Biol. , vol.9 , pp. 1347-1350
    • Liu, Q.A.1    Hengartner, M.O.2
  • 10
    • 0002037649 scopus 로고    scopus 로고
    • The human homologue of Caenorhabditis elegans CED-6 specifically promotes phagocytosis of apoptotic cells
    • Smits E., Van Criekinge W., Plaetinck G., and Bogaert T. The human homologue of Caenorhabditis elegans CED-6 specifically promotes phagocytosis of apoptotic cells. Curr. Biol. 9 (1999) 1351-1354
    • (1999) Curr. Biol. , vol.9 , pp. 1351-1354
    • Smits, E.1    Van Criekinge, W.2    Plaetinck, G.3    Bogaert, T.4
  • 11
    • 33744947548 scopus 로고    scopus 로고
    • Essential role of the apoptotic cell engulfment genes draper and ced-6 in programmed axon pruning during Drosophila metamorphosis
    • Awasaki T., Tatsumi R., Takahashi K., Arai K., Nakanishi Y., Ueda R., and Ito K. Essential role of the apoptotic cell engulfment genes draper and ced-6 in programmed axon pruning during Drosophila metamorphosis. Neuron 50 (2006) 855-867
    • (2006) Neuron , vol.50 , pp. 855-867
    • Awasaki, T.1    Tatsumi, R.2    Takahashi, K.3    Arai, K.4    Nakanishi, Y.5    Ueda, R.6    Ito, K.7
  • 13
    • 0001360346 scopus 로고    scopus 로고
    • Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells
    • Su H.P., Brugnera E., Van Criekinge W., Smits E., Hengartner M., Bogaert T., and Ravichandran K.S. Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells. J. Biol. Chem. 275 (2000) 9542-9549
    • (2000) J. Biol. Chem. , vol.275 , pp. 9542-9549
    • Su, H.P.1    Brugnera, E.2    Van Criekinge, W.3    Smits, E.4    Hengartner, M.5    Bogaert, T.6    Ravichandran, K.S.7
  • 14
    • 33744952845 scopus 로고    scopus 로고
    • The lipoprotein receptor-related protein-1 (LRP) adapter protein GULP mediates trafficking of the LRP ligand prosaposin, leading to sphingolipid and free cholesterol accumulation in late endosomes and impaired efflux
    • Kiss R.S., Ma Z., Nakada-Tsukui K., Brugnera E., Vassiliou G., McBride H.M., Ravichandran K.S., and Marcel Y.L. The lipoprotein receptor-related protein-1 (LRP) adapter protein GULP mediates trafficking of the LRP ligand prosaposin, leading to sphingolipid and free cholesterol accumulation in late endosomes and impaired efflux. J. Biol. Chem. 281 (2006) 12081-12092
    • (2006) J. Biol. Chem. , vol.281 , pp. 12081-12092
    • Kiss, R.S.1    Ma, Z.2    Nakada-Tsukui, K.3    Brugnera, E.4    Vassiliou, G.5    McBride, H.M.6    Ravichandran, K.S.7    Marcel, Y.L.8
  • 15
    • 0242330147 scopus 로고    scopus 로고
    • Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection
    • Traub L.M. Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection. J. Cell Biol. 163 (2003) 203-208
    • (2003) J. Cell Biol. , vol.163 , pp. 203-208
    • Traub, L.M.1
  • 18
    • 0037023693 scopus 로고    scopus 로고
    • Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)
    • Su H.P., Nakada-Tsukui K., Tosello-Trampont A.C., Li Y., Bu G., Henson P.M., and Ravichandran K.S. Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP). J. Biol. Chem. 277 (2002) 11772-11779
    • (2002) J. Biol. Chem. , vol.277 , pp. 11772-11779
    • Su, H.P.1    Nakada-Tsukui, K.2    Tosello-Trampont, A.C.3    Li, Y.4    Bu, G.5    Henson, P.M.6    Ravichandran, K.S.7
  • 19
    • 0033560032 scopus 로고    scopus 로고
    • EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization
    • Franco M., Peters P.J., Boretto J., van Donselaar E., Neri A., D'Souza-Schorey C., and Chavrier P. EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. EMBO J. 18 (1999) 1480-1491
    • (1999) EMBO J. , vol.18 , pp. 1480-1491
    • Franco, M.1    Peters, P.J.2    Boretto, J.3    van Donselaar, E.4    Neri, A.5    D'Souza-Schorey, C.6    Chavrier, P.7
  • 20
    • 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
  • 21
    • 0037073704 scopus 로고    scopus 로고
    • AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton
    • Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J., and Randazzo P.A. AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton. J. Biol. Chem. 277 (2002) 48965-48975
    • (2002) J. Biol. Chem. , vol.277 , pp. 48965-48975
    • Nie, Z.1    Stanley, K.T.2    Stauffer, S.3    Jacques, K.M.4    Hirsch, D.S.5    Takei, J.6    Randazzo, P.A.7
  • 22
    • 0033573126 scopus 로고    scopus 로고
    • Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta
    • Mandiyan V., Andreev J., Schlessinger J., and Hubbard S.R. Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta. EMBO J. 18 (1999) 6890-6898
    • (1999) EMBO J. , vol.18 , pp. 6890-6898
    • Mandiyan, V.1    Andreev, J.2    Schlessinger, J.3    Hubbard, S.R.4
  • 23
    • 0141481046 scopus 로고    scopus 로고
    • Munc18 interacting proteins: ADP-ribosylation factor-dependent coat proteins that regulate the traffic of beta-Alzheimer's precursor protein
    • Hill K., Li Y., Bennett M., McKay M., Zhu X., Shern J., Torre E., Lah J.J., Levey A.I., and Kahn R.A. Munc18 interacting proteins: ADP-ribosylation factor-dependent coat proteins that regulate the traffic of beta-Alzheimer's precursor protein. J. Biol. Chem. 278 (2003) 36032-36040
    • (2003) J. Biol. Chem. , vol.278 , pp. 36032-36040
    • Hill, K.1    Li, Y.2    Bennett, M.3    McKay, M.4    Zhu, X.5    Shern, J.6    Torre, E.7    Lah, J.J.8    Levey, A.I.9    Kahn, R.A.10
  • 24
    • 10344234238 scopus 로고    scopus 로고
    • PTB or not to be: Promiscuous, tolerant and Bizarro domains come of age
    • Farooq A., and Zhou M.M. PTB or not to be: Promiscuous, tolerant and Bizarro domains come of age. IUBMB Life 56 (2004) 547-557
    • (2004) IUBMB Life , vol.56 , pp. 547-557
    • Farooq, A.1    Zhou, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.