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. 1984 Dec;39(2 Pt 1):405-16.
doi: 10.1016/0092-8674(84)90019-9.

Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine

W E Balch, W G Dunphy, W A Braell, J E Rothman

Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine

W E Balch et al. Cell. 1984 Dec.

Abstract

Transport of the VSV-encoded glycoprotein (G protein) between successive compartments of the Golgi has been reconstituted in a cell-free system and is measured, in a rapid and sensitive new assay, by the coupled incorporation of 3H-N-acetylglucosamine (GlcNAc). This glycosylation occurs when G protein is transported during mixed incubations from the "donor" compartment in Golgi from VSV-infected CHO clone 15B cells (missing a key Golgi GlcNAc transferase) to the next, successive "acceptor" compartment (containing the GlcNAc transferase) in Golgi from wild-type CHO cells. Golgi fractions used in this assay have been extensively purified, and account for all of the donor and acceptor activity in the cells. Together with several other lines of evidence, this indicates that the cell-free system is highly specific, measuring only transport between sequential compartments in the Golgi stack. Transport in vitro is almost as efficient as in the cell, and requires ATP and the cytosol fraction in addition to protein components on the cytoplasmic surface of the Golgi membranes.

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Comment in

  • The mechanisms of vesicle budding and fusion.
    Bonifacino JS, Glick BS. Bonifacino JS, et al. Cell. 2004 Jan 23;116(2):153-66. doi: 10.1016/s0092-8674(03)01079-1. Cell. 2004. PMID: 14744428 Review.
  • Vesicle traffic in vitro.
    Balch WE. Balch WE. Cell. 2004 Jan 23;116(2 Suppl):S17-9, 2 p following S19. doi: 10.1016/s0092-8674(03)00970-x. Cell. 2004. PMID: 15055576 No abstract available.

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