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

Molecular and Cellular Biology
J G PrydeJ M Lucocq

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 whi...Continue Reading

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Citations

Dec 22, 1999·The Journal of Cell Biology·C AlvarezE Sztul
Dec 19, 2012·Journal of Plant Physiology·Justyna T Polit, Ryszard B Nazarski
Sep 25, 2007·Biochemical and Biophysical Research Communications·Lijun Wang, John M Lucocq
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Jan 30, 2021·Frontiers in Cell and Developmental Biology·Brittany J BisnettMichael Boyce
Dec 29, 2010·Journal of Cell Science·Hesso Farhan, Catherine Rabouille

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