Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes

Ji-long Chen; Lynne Lacomis; Hediye Erdjument-Bromage; Paul Tempst; Mark Stamnes

doi:10.1016/j.febslet.2004.04.061

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Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes

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Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes

Ji-long Chen, Lynne Lacomis, Hediye Erdjument-Bromage, Paul Tempst and Mark Stamnes

FEBS letters, Vol.566(1), pp.281-286

2004

DOI: 10.1016/j.febslet.2004.04.061

PMID: 15147909

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Abstract

The actin cytoskeleton has been implicated in protein trafficking at the Golgi apparatus and in Golgi orientation and morphology. Actin dynamics at the Golgi are regulated in part by recruiting Cdc42 or Rac to the membrane through a binding interaction with the coatomer-coated (COPI)-vesicle coat protein, coatomer. This leads to actin polymerization through the effector, N-WASP and the Arp2/3 complex. Here, we have used reconstitution of vesicle budding to test whether Arp2/3 is recruited to membranes during the formation of COPI vesicles. Our results revealed that ARF1 activation leads to greatly increased Arp3 levels on the membranes. Coatomer-bound Cdc42 and pre-existing F-actin are important for Arp2/3 binding. ARF1-dependent Arp2/3 recruitment and actin polymerization can be reconstituted on liposomal membranes, indicating that no membrane proteins are necessary. These results show that activated ARF1 can stimulate Arp2/3 recruitment to Golgi membranes through coatomer, Cdc42 or Rac, and N-WASP.

ADP-ribosylation factor

Arp2/3

Cdc42

Coatomer

Cytoskeleton

Golgi apparatus

Details

Title: Subtitle: Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes
Creators: Ji-long Chen - University of Iowa
Lynne Lacomis - Memorial Sloan Kettering Cancer Center
Hediye Erdjument-Bromage - Memorial Sloan Kettering Cancer Center
Paul Tempst - Memorial Sloan Kettering Cancer Center
Mark Stamnes - Roy J. and Lucille A. Carver College of Medicine
Resource Type: Journal article
Publication Details: FEBS letters, Vol.566(1), pp.281-286
Publisher: Elsevier B.V
DOI: 10.1016/j.febslet.2004.04.061
PMID: 15147909
ISSN: 0014-5793
eISSN: 1873-3468
Language: English
Date published: 2004
Academic Unit: Molecular Physiology and Biophysics; Internal Medicine
Record Identifier: 9984297602702771

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