Spooner, Robert A., Cook, Jonathan P., Li, Shuyu, Pietroni, Paula and Lord, 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

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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, Engineering and Medicine > Science > Life Sciences (2010- )
Series Name:	Plant Cell Monographs
Publisher:	Springer
ISBN:	1861-1370
ISSN:	1861-1370
Book Title:	Toxic Plant Proteins
Official Date:	2010
Dates:	Date Event 2010 Published
Volume:	Vol.18
Number of Pages:	18
Page Range:	pp. 207-224
DOI:	10.1007/978-3-642-12176-0_11
Status:	Not Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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