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. ISSN 0070-217X

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.

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item