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Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex

Nature volume 364, pages 818–821 (1993)Cite this article

Abstract

THE formation of constitutive transport vesicles involves the association of non-clathrin coat proteins to transport organelles1,2. Here we report that IgE receptors and protein kinase C (PKC) regulate the GTP-dependent binding of the two coat proteins ADP-ribosylation factor (ARF) and β-COP3–5 to Golgi membranes in rat basophilic leukaemia cells. Activation of IgE receptors and PKC prevented the ARF and β-COP dissociation from Golgi membranes that occurs in permeabilized cells in the absence of GTP and potentiated the association-promoting effects of GTP and the G protein activator fluoroluminate. In contrast, PKC downregulation and PKC inhibition abolished the activity of GTP and fluoroluminate in promoting ARF binding to the Golgi complex. Studies of ARF binding to isolated Golgi membranes gave similar results. These findings suggest that coat assembly on Golgi membranes, and thus possibly constitutive secretory traffic, is modulated by membrane receptors and second messengers.

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Authors and Affiliations

  1. Unit of Physiopathology of Secretion, Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, Santa Maria Imbaro (Chieti), 66030, Italy

    Maria Antonietta De Matteis & Giovanna Santini

  2. Laboratory of Molecular Neurobiology, Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, Santa Maria Imbaro (Chieti), 66030, Italy

    Giuseppe Di Tullio & Alberto Luini

  3. Laboratory of Biological Chemistry, Division of Cancer Treatment, National Cancer Institute, NIH, Bethesda, Maryland, 20892, USA

    Richard A. Kahn

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  1. Maria Antonietta De Matteis
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  2. Giovanna Santini
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  3. Richard A. Kahn
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  4. Giuseppe Di Tullio
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  5. Alberto Luini
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De Matteis, M., Santini, G., Kahn, R. et al. Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex. Nature 364, 818–821 (1993). https://doi.org/10.1038/364818a0

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