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Ricin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.


ABSTRACT: 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.

SUBMITTER: Chamberlain KL 

PROVIDER: S-EPMC2586253 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Ricin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.

Chamberlain Kerry L KL   Marshall Richard S RS   Jolliffe Nicholas A NA   Frigerio Lorenzo L   Ceriotti Aldo A   Lord J Michael JM   Roberts Lynne M LM  

The Journal of biological chemistry 20081002 48


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. ...[more]

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