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.
journal_name
Curr Top Microbiol Immunoljournal_title
Current topics in microbiology and immunologyauthors
Lord JM,Roberts LM,Lencer WIdoi
10.1007/3-540-28007-3_7subject
Has Abstractpub_date
2005-01-01 00:00:00pages
149-68eissn
0070-217Xissn
2196-9965journal_volume
300pub_type
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