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

Maria Antonietta De Matteis, Giovanna Santini, Richard A. Kahn, Giuseppe Di Tullio, Alberto Luini

Research output: Contribution to journalArticle

Abstract

THE formation of constitutive transport vesicles involves the association of non-clathrin coat proteins to transport organelles 1,2. 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 fluoroaluminate. 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.

Original languageEnglish
Pages (from-to)818-821
Number of pages4
JournalNature
Volume364
Issue number6440
Publication statusPublished - Aug 26 1993

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex'. Together they form a unique fingerprint.

  • Cite this

    De Matteis, M. A., Santini, G., Kahn, R. A., Di Tullio, G., & Luini, A. (1993). Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex. Nature, 364(6440), 818-821.