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J. Biol. Chem., Vol. 275, Issue 25, 19050-19059, June 23, 2000
From the The small GTP-binding protein ADP-ribosylation
factor 1 (ARF1) is an essential component of the molecular machinery
that catalyzes the formation of membrane-bound transport intermediates.
By using an in vitro assay that reproduces recruitment of
cytosolic proteins onto purified, high salt-washed Golgi membranes, we
have analyzed the role of cAMP-dependent protein kinase A
(PKA) on ARF1 incorporation. Addition to this assay of either pure
catalytic subunits of PKA (C-PKA) or cAMP increased ARF1 binding. By
contrast, ARF1 association was inhibited following C-PKA inactivation
with either PKA inhibitory peptide or RII
Effect of Protein Kinase A Activity on the Association of
ADP-ribosylation Factor 1 to Golgi Membranes*
,,
Department of Cell Biology,
University of Seville, 41012 Seville, the § Department of
Ciencias Fisiológicas II, Campus de Bellvitge, University of
Barcelona, 08907-Hospitalet, Barcelona, Spain and
** Biozentrum of the University of Basel,
Klingelbergstrasse 70, CH-4056, Switzerland
as well as after cytosol
depletion of C-PKA. C-PKA also stimulated recruitment and activation of
a recombinant form of human ARF1 in the absence of additional cytosolic
components. The binding step could be dissociated from the activation
reaction and found to be independent of guanine nucleotides and
saturable. This step was stimulated by C-PKA in an
ATP-dependent manner. Dephosphorylated Golgi membranes
exhibited a decreased ability to recruit ARF1, and this effect was
reverted by addition of C-PKA. Following an increase in the
intracellular level of cAMP, ARF proteins redistributed from cytosol to
the perinuclear Golgi region of intact cells. Collectively, the results
show that PKA exerts a key regulatory role in the recruitment of ARF1
onto Golgi membranes. In contrast, PKA modulators did not affect
recruitment of 
-COP onto Golgi membranes containing prebound
ARF1.
*
This work was supported in part by Grant 97/1170 from Fondo
de Investigaciones Sanitarias (Spain).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell
Biology, Faculty of Biology, University of Seville, Avd. Reina Mercedes s/n, 41012-Seville, Spain. Tel.: 34-954557044; Fax: 34-954610261; E-mail: avelasco@cica.es.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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