Okadaic acid induces selective arrest of protein transport in the rough endoplasmic reticulum and prevents export into COPII-coated structures

J G Pryde, T Farmaki, J M Lucocq

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17 Citations (Scopus)

Abstract

Quantitative immunoelectron microscopy and subcellular fractionation established the site of endoplasmic reticulum (ER)-Golgi transport arrest induced by the phosphatase inhibitor okadaic acid (OA). OA induced the disappearance of transitional element tubules and accumulation of the anterograde-transported Chandipura (CHP) virus G protein only in the rough ER (RER) and not at more distal sites. The block was specific to the early part of the anterograde pathway, because CHP virus G protein that accumulated in the intermediate compartment (IC) at 15 degrees C could gain access to Golgi stack enzymes. OA also induced RER accumulation of the IC protein p53/p58 via an IC-RER recycling pathway which was resistant to OA and inhibited by the G protein activator aluminium fluoride. The role of COPII coats in OA transport block was investigated by using immunofluorescence and cell fractionation. In untreated cells the COPII coat protein sec 13p colocalized with p53/p58 in Golgi-IC structures of the juxtanuclear region and peripheral cytoplasm. During OA treatment, p53/p58 accumulated in the RER but was excluded from sec 13p-containing membrane structures. Taken together our data indicate that OA induces an early defect in RER export which acts to prevent entry into COPII-coated structures of the IC region.
Original languageEnglish
Pages (from-to)1125-35
Number of pages11
JournalMolecular and Cellular Biology
Volume18
Issue number2
Publication statusPublished - Feb 1998

Keywords

  • Animals
  • Biological Transport
  • CHO Cells
  • Carrier Proteins
  • Cricetinae
  • Endoplasmic Reticulum, Rough
  • Enzyme Inhibitors
  • GTP-Binding Proteins
  • Mannose-Binding Lectins
  • Membrane Proteins
  • Microscopy, Immunoelectron
  • Okadaic Acid
  • Phosphoproteins
  • Proteins
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins

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