Ricin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.
The B chain of ricin was expressed and delivered to the endoplasmic reticulum of tobacco protoplasts where it disappeared with time in a manner consistent with degradation. This turnover did not occur in the vacuoles or upon secretion. Indeed, several lines of evidence indicate that, in contrast to the turnover of endoplasmic reticulum-targeted ricin A chain in the cytosol, the bulk of expressed ricin B chain was degraded in the secretory pathway.
Chamberlain
Kerry L
KL
Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, United Kingdom.
Marshall
Richard S
RS
Jolliffe
Nicholas A
NA
Frigerio
Lorenzo
L
Ceriotti
Aldo
A
Lord
J Michael
JM
Roberts
Lynne M
LM
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D011523:Protoplasts / Q000166:cytology / Q000378:metabolism*; D012276:Ricin / Q000378:metabolism* / Q000494:pharmacology; D014026:Nicotiana / Q000166:cytology / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism; D000074405:Valosin Containing Protein
D018797:Cell Cycle Proteins; D010940:Plant Proteins; D012276:Ricin; D000251:Adenosine Triphosphatases; D000074405:Valosin Containing Protein