Premium
Cytosol‐derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer‐dependent actin polymerization on Golgi membranes
Author(s) -
Chen Ji-long,
Lacomis Lynne,
Erdjument-Bromage Hediye,
Tempst Paul,
Stamnes Mark
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.061
Subject(s) - copi , microbiology and biotechnology , golgi apparatus , actin remodeling , actin binding protein , actin remodeling of neurons , actin cytoskeleton , wiskott–aldrich syndrome protein , actin , biology , mdia1 , secretory pathway , cytoskeleton , biochemistry , endoplasmic reticulum , cell
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.