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. 1992 Apr 3;69(1):129-38.
doi: 10.1016/0092-8674(92)90124-u.

Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators

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Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators

M S Robinson et al. Cell. .

Abstract

Brefeldin A (BFA) causes a rapid redistribution of coat proteins (e.g., gamma-adaptin) associated with the clathrin-coated vesicles that bud from the trans-Golgi network (TGN), while the clathrin-coated vesicles that bud from the plasma membrane are unaffected. gamma-Adaptin redistributes with the same kinetics as beta-COP, a coat protein associated with the non-clathrin-coated vesicles that bud from the Golgi complex. Upon removal of BFA, however, gamma-adaptin recovers its perinuclear distribution more rapidly. Redistribution of both proteins can be prevented by pretreating cells with AlF4-. Recruitment of adaptors from the cytosol onto the TGN membrane has been reconstituted in a permeabilized cell system and is increased by addition of GTP gamma S and blocked by addition of BFA. These results suggest a role for G proteins in the control of the clathrin-coated vesicle cycle at the TGN and further extend the similarities between clathrin-coated vesicles and non-clathrin-coated vesicles.

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