N Vitale

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. ncbi request reprint The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing
    R T Premont
    Departments of Medicine and Biochemistry, Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 275:22373-80. 2000
  2. ncbi request reprint Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1
    N Vitale
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 272:25077-82. 1997
  3. ncbi request reprint Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)
    N Vitale
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 273:2553-60. 1998
  4. pmc Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus
    N Vitale
    Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 95:8613-8. 1998
  5. ncbi request reprint Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)
    N Vitale
    Pulmonary Critical Care Medicine Branch and the Pathology Section, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 275:21331-9. 2000
  6. pmc Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1
    N Vitale
    Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Mol Cell Biol 20:7342-52. 2000
  7. ncbi request reprint Characterization of a GTPase-activating protein that stimulates GTP hydrolysis by both ADP-ribosylation factor (ARF) and ARF-like proteins. Comparison to the ARD1 gap domain
    M Ding
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 271:24005-9. 1996
  8. pmc ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain
    N Vitale
    Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 93:1941-4. 1996
  9. ncbi request reprint Guanine nucleotide exchange on ADP-ribosylation factors catalyzed by cytohesin-1 and its Sec7 domain
    G Pacheco-Rodriguez
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 273:26543-8. 1998
  10. pmc beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein
    R T Premont
    Departments of Medicine Cardiology and Biochemistry, Howard Hughes Medical Institute, Box 3821, Duke University Medical Center, Durham, NC 27710, USA
    Proc Natl Acad Sci U S A 95:14082-7. 1998

Collaborators

Detail Information

Publications15

  1. ncbi request reprint The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing
    R T Premont
    Departments of Medicine and Biochemistry, Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 275:22373-80. 2000
    ..Although GIT2 shares many properties with GIT1, it also exhibits both structural and functional diversity due to tissue-specific alternative splicing...
  2. ncbi request reprint Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1
    N Vitale
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 272:25077-82. 1997
    ..It is suggested that, like the amino-terminal segment of ARF, the equivalent region in ARD1, located between the GTPase-activating protein and ARF domains, may act as a GDP dissociation inhibitor...
  3. ncbi request reprint Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)
    N Vitale
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 273:2553-60. 1998
    ..The GAP domain of ARD1 thus is similar to ARF GAPs but differs from other GAPs in its covalent association with the GTP-binding domain...
  4. pmc Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus
    N Vitale
    Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 95:8613-8. 1998
    ..These observations suggest that the ARF-related protein ARD1 may play a role in the formation or function of lysosomes and in protein trafficking between Golgi and lysosomes...
  5. ncbi request reprint Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)
    N Vitale
    Pulmonary Critical Care Medicine Branch and the Pathology Section, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 275:21331-9. 2000
    ..It was concluded that cytohesin-1 is likely to be involved in ARD1 activation, consistent with a role for ARD1 in the regulation of vesicular trafficking...
  6. pmc Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1
    N Vitale
    Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Mol Cell Biol 20:7342-52. 2000
    ..These results suggest that ARD1 is a multidomain protein with ARF and GAP regions, which contain Golgi and lysosomal localization signals, respectively, that could function in vesicular trafficking...
  7. ncbi request reprint Characterization of a GTPase-activating protein that stimulates GTP hydrolysis by both ADP-ribosylation factor (ARF) and ARF-like proteins. Comparison to the ARD1 gap domain
    M Ding
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 271:24005-9. 1996
    ..The non-ARF1 domain of ARD1 enhanced the GTPase activity of the ARF domain, but not that of the ARF proteins and Delta13ARF1, i.e. it lacks the relatively broad substrate specificity exhibited by ARF GAP...
  8. pmc ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain
    N Vitale
    Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 93:1941-4. 1996
    ..Thus, like the alpha subunits of heterotrimeric G proteins, ARD1 appears to consist of two domains that interact to regulate the biological activity of the protein...
  9. ncbi request reprint Guanine nucleotide exchange on ADP-ribosylation factors catalyzed by cytohesin-1 and its Sec7 domain
    G Pacheco-Rodriguez
    Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 273:26543-8. 1998
    ..Data obtained with mutant ARF constructs are all consistent with the conclusion that the ARF N terminus is an important determinant of cytohesin-1 specificity...
  10. pmc beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein
    R T Premont
    Departments of Medicine Cardiology and Biochemistry, Howard Hughes Medical Institute, Box 3821, Duke University Medical Center, Durham, NC 27710, USA
    Proc Natl Acad Sci U S A 95:14082-7. 1998
    ..Moreover, they provide a mechanism for integration of receptor activation and endocytosis through regulation of ARF protein activation by GRK-mediated recruitment of the GIT1 ARF GAP to the plasma membrane...
  11. ncbi request reprint GIT proteins, A novel family of phosphatidylinositol 3,4, 5-trisphosphate-stimulated GTPase-activating proteins for ARF6
    N Vitale
    INSERM U 338, Centre de Neurochimie, 5 rue Blaise Pascal, 67084 Strasbourg Cedex, France
    J Biol Chem 275:13901-6. 2000
    ....
  12. ncbi request reprint Regulation of exocytosis in chromaffin cells by phosducin-like protein, a protein interacting with G protein betagamma subunits
    M Gensse
    Institut National de la Sante et de la Recherche Medicale, U 338 Biologie de la Communication Cellulaire, Strasbourg, France
    FEBS Lett 480:184-8. 2000
    ..Thus, PhLPs may participate directly in the regulation of calcium-evoked exocytosis...
  13. pmc Phospholipase D1: a key factor for the exocytotic machinery in neuroendocrine cells
    N Vitale
    , 5 rue Blaise Pascal, 67084 Strasbourg, France
    EMBO J 20:2424-34. 2001
    ..These results provide the first direct evidence that PLD1 is an important component of the exocytotic machinery in neuroendocrine cells...
  14. ncbi request reprint beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis
    A Claing
    Howard Hughes Medical Institute and Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 276:42509-13. 2001
    ....
  15. pmc A role for phospholipase D1 in neurotransmitter release
    Y Humeau
    Centre National de la Recherche Scientifique, Unité Propre de Recherche 2356, Neurotransmission et Secretion Neuroendocrine, 5 rue Blaise Pascal, IFR37, 67084 Strasbourg, France
    Proc Natl Acad Sci U S A 98:15300-5. 2001
    ..Our results provide evidence that PLD1 plays a major role in neurotransmission, most likely by controlling the fusogenic status of presynaptic release sites...