UNSPECIFIED (2005) Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: Co-opting basic mechanisms of endoplasmic reticululm-associated degradation. DISLOCATION AND DEGRADATION OF PROTEINS FROM THE ENDOPLASMIC RETICULUM, 300 . pp. 149-168.

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Abstract

The catalytic polypeptides of certain bacterial and plant protein toxins reach their substrates in the cytosol of mammalian cells by retro-translocation from the endoplasmic reticulum (ER). Emerging evidence indicates that these proteins subvert the ER-associated protein degradation (ERAD) pathway that normally removes misfolded or unassembled proteins from the ER, to achieve retrotranslocation. Upon entering the ER lumen, the toxins are unfolded to be perceived as ERAD substrates. Toxins that retro-translocate from the ER have an unusually low lysine content to avoid ubiquitin-mediated proteasomal degradation. This allows the exported toxins to refold into the proteasome-resistant, biologically active conformation, and leads to cellular intoxication.

Item Type:	Journal Item
Subjects:	Q Science > QR Microbiology > QR180 Immunology Q Science > QR Microbiology
Series Name:	CURRENT TOPICS IN MICROBIOLOGY AND IMMUNOLOGY
Journal or Publication Title:	DISLOCATION AND DEGRADATION OF PROTEINS FROM THE ENDOPLASMIC RETICULUM
Publisher:	SPRINGER-VERLAG BERLIN
ISSN:	0070-217X
Official Date:	2005
Dates:	Date Event 2005 UNSPECIFIED
Volume:	300
Number of Pages:	20
Page Range:	pp. 149-168
Publication Status:	Published

Data sourced from Thomson Reuters' Web of Knowledge

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