Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

How ricin and shiga toxin reach the cytosol of target cells : retrotranslocation from the endoplasmic reticulum

Tools
- Tools
+ Tools

Spooner, Robert A. and Lord, Mike (2012) How ricin and shiga toxin reach the cytosol of target cells : retrotranslocation from the endoplasmic reticulum. Current Topics in Microbiology and Immunology, Vol.357 . pp. 19-40. doi:1007/82_2011_154

[img]
Preview
Text
WRAP_Spooner_070468-lf-130711-ctmi_for_wrap.pdf - Accepted Version

Download (7Mb)
Official URL: http://dx.doi.org/1007/82_2011_154

Request Changes to record.

Abstract

A number of protein toxins bind at the surface of mammalian cells and after
endocytosis traffic to the endoplasmic reticulum, where the toxic A chains are
liberated from the holotoxin. The free A chains are then dislocated, or
retrotranslocated, across the ER membrane into the cytosol. Here, in contrast to ER
substrates destined for proteasomal destruction, they undergo folding to a catalytic
conformation and subsequently inactivate their cytosolic targets. These toxins
therefore provide toxic probes for testing the molecular requirements for retrograde
trafficking, the ER processes that prepare the toxic A chains for transmembrane
transport, the dislocation step itself and for the post-dislocation folding that results in
catalytic activity. We describe here the dislocation of ricin A chain and Shiga toxin A
chain, but also consider cholera toxin which bears a superficial structural resemblance
to Shiga toxin. Recent studies not only describe how these proteins breach the ER
membrane, but also reveal aspects of a fundamental cell biological process, that of
ER-cytosol dislocation.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Ricin -- Physiological transport, Verocytotoxins -- Physiological transport, Endoplasmic reticulum
Journal or Publication Title: Current Topics in Microbiology and Immunology
Publisher: Springer New York LLC
ISSN: 0070-217X
Official Date: 2012
Dates:
DateEvent
2012Published
Date of first compliant deposit: 1 August 2016
Volume: Vol.357
Page Range: pp. 19-40
DOI: 1007/82_2011_154
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Wellcome Trust (London, England), National Institutes of Health (U.S.) (NIH)
Grant number: 080566/Z/06/Z (Wellcome), 5U01AI65869-02 (NIH)

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us