Effect of caffeine on intracellular transport of Semliki Forest virus membrane glycoproteins.
The effect of caffeine on the intracellular transport of Semliki Forest virus (SFV) membrane glycoproteins was studied in baby hamster kidney (BHK) cells. The movement of the proteins was affected at two steps in the exocytic pathway. The exit of the proteins from the endoplasmic reticulum (ER) was inhibited by 10 mM caffeine at 20 degrees C, a temperature that normally allows transport to the Golgi complex. At higher temperatures (28 degrees C and 37 degrees C) in the presence of 10 mM caffeine exit from the ER occurred, but the proteins accumulated at intracellular membrane elements. Immunofluorescence localization, endoglycosidase-H analysis, and analysis of the proteolytical cleavage of the p62 precursor protein suggested that transport in the presence of 10 mM caffeine was arrested at the membranes between the trans-Golgi and the plasma membrane.
Kuismanen
E
E
Department of Biochemistry, University of Helsinki, Finland.
Jäntti
J
J
Mäkiranta
V
V
Sariola
M
M
D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D002110:Caffeine / Q000494:pharmacology*; D002478:Cells, Cultured; D006224:Cricetinae; D004721:Endoplasmic Reticulum / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism; D012672:Semliki forest virus; D013696:Temperature; D014759:Viral Envelope Proteins / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000378:metabolism*
D008562:Membrane Glycoproteins; D011134:Polysaccharides; D014759:Viral Envelope Proteins; D014763:Viral Matrix Proteins; D002110:Caffeine