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
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

How Ricin Reaches its Target in the Cytosol of Mammalian Cells

Tools
- Tools
+ Tools

Spooner, Robert A., Cook, Jonathan P., Li, Shuyu, Pietroni, Paula and Lord, Mike (J. Mike) (2010) How Ricin Reaches its Target in the Cytosol of Mammalian Cells. In: Toxic Plant Proteins. Plant Cell Monographs, Vol.18 . Springer, pp. 207-224. ISBN 1861-1370

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1007/978-3-642-12176-0_11

Abstract

The cytotoxic plant protein ricin comprises a lectin B chain that binds promiscuously to glycolipids and glycoproteins at the surface of mammalian cells, disulphide-coupled to a toxic A chain which depurinates target ribosomes. To find these cytosolic targets, the A chain has to cross a biological membrane, which is not a simple task for a folded protein. The secretory pathway of eukaryotic cells is reversible and ricin can take advantage of this to move from the plasma membrane, via the Golgi, to the ER whose membrane is crossed to gain access to the cytosol. Since membrane traversal is preceded by an unfolding step, there is a clear requirement for cytosolic re-folding of ricin to gain a catalytic conformation. This final step for ricin is accomplished after triage by cytosolic chaperones, underlining the central role of these in cellular protein folding.

Item Type: Book Item
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Science > Life Sciences (2010- )
Series Name: Plant Cell Monographs
Publisher: Springer
ISBN: 1861-1370
ISSN: 1861-1370
Book Title: Toxic Plant Proteins
Date: 2010
Volume: Vol.18
Number of Pages: 18
Page Range: pp. 207-224
Identification Number: 10.1007/978-3-642-12176-0_11
Status: Not Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
URI: http://wrap.warwick.ac.uk/id/eprint/42906

Request changes to a record

Actions (login required)

View Item View Item
twitter

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