Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo.

Abstract

Microinjection of antibodies against a synthetic peptide of a non-clathrin-coated vesicle-associated coat protein, beta-COP, blocks transport of a temperature-sensitive vesicular stomatitis virus glycoprotein (ts-O45-G) to the cell surface. Transport is inhibited upon release of the viral glycoprotein from temperature blocks at 39.5 degrees C (endoplasmic reticulum [ER]) and 15 degrees C (intermediate compartment), but not at 20 degrees C (trans-Golgi network). Ts-O45-G is arrested in tubular membrane structures containing p53 at the interface of the ER and the Golgi stack. This is consistent with inhibition of acquisition of endoglycosidase H resistance of ts-O45-G in injected cells. Secretion of endogenous proteins and maturation of cathepsin D are also inhibited. These data provide in vivo evidence that beta-COP has an important function in biosynthetic membrane traffic in mammalian cells.

• Authors: R Pepperkok, J Scheel, H Horstmann, H P Hauri, G Griffiths, T E Kreis
• Journal: Cell (Cell) Vol. 74 Issue 1 Pg. 71-82 (Jul 16 1993) ISSN: 0092-8674 [Print] United States
• PMID: 8334707 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antibodies
• Coatomer Protein
• Microtubule-Associated Proteins
• Viral Proteins
• Cathepsin D

Topics

• Animals
• Antibodies (pharmacology)
• Biological Transport (drug effects)
• Cathepsin D (metabolism)
• Coatomer Protein
• Endoplasmic Reticulum (metabolism)
• Golgi Apparatus (metabolism)
• Intracellular Membranes (metabolism)
• Microinjections
• Microtubule-Associated Proteins (physiology)
• Temperature
• Vero Cells (metabolism)
• Viral Proteins (metabolism)