Selected article for: "e1 arrest and Golgi complex"
Title: The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre- Golgi compartment
  • Document date: 1992_8_2
    • ID: 04455ffs_56
    Snippet: The results in this paper demonstrate that RV E1 glycoprotein which does not assemble with E2 is unable to be transported to the Golgi complex and accumulates in a novel pre-Golgi compartment consisting of a tubular network of smooth membranes distinct from, but in continuity with the RER. Kinetically, the compartment is located distal to, or at the site where palmitylation of E1 occurs, but proximal to the 15 ~ block which corresponds to the so-.....
    Document: The results in this paper demonstrate that RV E1 glycoprotein which does not assemble with E2 is unable to be transported to the Golgi complex and accumulates in a novel pre-Golgi compartment consisting of a tubular network of smooth membranes distinct from, but in continuity with the RER. Kinetically, the compartment is located distal to, or at the site where palmitylation of E1 occurs, but proximal to the 15 ~ block which corresponds to the so-called intermediate compartment (43, 52) . The site of E1 arrest has distinct properties from the RER, intermediate compartment, or Golgi: (a) membrane proteins that serve as markers of RER or Golgi are excluded from this compartment; (b) agents which disrupt RER (thapsigargin, ionomycin) or Golgi (nocodazole and BFA) integrity did not affect it; and (c) its morphologic organization (network of smooth membranes) Figure 10 . Transport of VSV G protein through the tubular network. CHOE1 ceils were infected with VSV ts045 at 32~ for 60 rain.

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