A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack

L Orci, BS Glick, JE Rothman - Cell, 1986 - cell.com
L Orci, BS Glick, JE Rothman
Cell, 1986cell.com
Isolated Golgi membranes incubated in the presence of ATP and a cytosolic protein fraction
form a population of coated buds or vesicles from the Golgi cisternae. The coats do not have
the characteristic hexagonal-pentagonal basketwork of clathrin, and do not react with anti-
clathrin polyclonal antibody. The conditions that produce these apparently
nonclathrincoated buds also reconstitute protein transport between compartments of the
Golgi stack. The membrane of the buds contains the glycoprotein in transit through these …
Summary
Isolated Golgi membranes incubated in the presence of ATP and a cytosolic protein fraction form a population of coated buds or vesicles from the Golgi cisternae. The coats do not have the characteristic hexagonal-pentagonal basketwork of clathrin, and do not react with anti-clathrin polyclonal antibody. The conditions that produce these apparently nonclathrincoated buds also reconstitute protein transport between compartments of the Golgi stack. The membrane of the buds contains the glycoprotein in transit through these Golgi stacks (VSV-encoded G protein). This suggests that protein transport through the Golgi stack is mediated by a new type of coated vesicle that does not contain clathrin. The concentration of G protein in the coated buds reflects the local concentration of G protein in the cisternae, raising the possibility that the Golgi coated vesicles may be “bulk” membrane carriers.
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