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Activated ADP-ribosylation Factor Assembles Distinct Pools of Actin on Golgi Membranes
Journal article   Open access   Peer reviewed

Activated ADP-ribosylation Factor Assembles Distinct Pools of Actin on Golgi Membranes

Raymond V. Fucini, Araceli Navarrete, Catherine Vadakkan, Lynne Lacomis, Hediye Erdjument-Bromage, Paul Tempst and Mark Stamnes
The Journal of biological chemistry, Vol.275(25), pp.18824-18829
06/23/2000
DOI: 10.1074/jbc.M000024200
PMID: 10777475
url
https://doi.org/10.1074/jbc.M000024200View
Published (Version of record) Open Access

Abstract

The small GTP-binding protein ADP-ribosylation factor (ARF) has been shown to regulate the interaction of actin and actin-binding proteins with the Golgi apparatus. Here we report that ARF activation stimulates the assembly of distinct pools of actin on Golgi membranes. One pool of actin cofractionates with coatomer (COPI)- coated vesicles and is sensitive to salt extraction and the plus end actin-binding toxin cytochalasin D. A second ARF-dependent actin pool remains on the Golgi membranes following vesicle extraction and is insensitive to cytochalasin D. Isolation of the salt-extractable ARF-dependent actin from the Golgi reveals that it is bound to a distinct repertoire of actin-binding proteins. The two abundant actin-binding proteins of the ARF-dependent actin complex are identified as spectrin and drebrin. We show that drebrin is a specific component of the cytochalasin D-sensitive, ARF-dependent actin pool on the Golgi. Finally, we show that depolymerization of this actin pool with cytochalasin D increases the extent of the salt-dependent release of COPI-coated vesicles from the Golgi following cell-free budding reactions. Together these data suggest that regulation of the actin-based cytoskeleton may play an important role during ARF-mediated transport vesicle assembly or release on the Golgi.

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