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The role of CDC48 in the retro-translocation of non-ubiquitinated toxin substrates in plant cells

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Marshall, Richard S., Jolliffe, Nicholas A., Ceriotti, Aldo, Snowden, Christopher J., Lord, Mike, Frigerio, Lorenzo and Roberts, L. M. (Lynne M.) (2009) The role of CDC48 in the retro-translocation of non-ubiquitinated toxin substrates in plant cells. Journal of Biological Chemistry, Vol.283 . pp. 15869-15877. doi:10.1074/jbc.M709316200

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Official URL: http://dx.doi.org/10.1074/jbc.M709316200

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Abstract

When the catalytic A subunits of the castor
bean toxins ricin and Ricinus communis
agglutinin (denoted as RTA and RCA A,
respectively) are delivered into the
endoplasmic reticulum (ER) of tobacco
protoplasts, they become substrates for ER-associated
protein degradation (ERAD). As
such, these orphan polypeptides are retro-translocated
to the cytosol, where a significant
proportion of each protein is degraded by
proteasomes. Here we begin to characterise
the ERAD pathway in plant cells, showing
that retro-translocation of these lysine-deficient
glycoproteins requires the ATPase
activity of cytosolic CDC48. Lysine
polyubiquitination is not obligatory for this
step. We also show that while RCA A is found
in a mannose-untrimmed form prior to its
retro-translocation, a significant proportion of
newly synthesised RTA cycles via the Golgi
and becomes modified by downstream
glycosylation enzymes. Despite these
differences, both proteins are similarly retro-translocated.

Item Type: Journal Article
Subjects: Q Science > QK Botany
Divisions: Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Library of Congress Subject Headings (LCSH): Castor beans, Ricin, Endoplasmic reticulum, Tobacco, Plant protoplasts, Plant translocation, Glycoproteins
Journal or Publication Title: Journal of Biological Chemistry
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
ISSN: 0021-9258
Official Date: 6 June 2009
Dates:
DateEvent
6 June 2009Published
Volume: Vol.283
Page Range: pp. 15869-15877
DOI: 10.1074/jbc.M709316200
Status: Peer Reviewed
Access rights to Published version: Open Access
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Leverhulme Trust (LT)

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