Linked Life Data

9333321

Source:http://linkedlifedata.com/resource/pubmed/id/9333321

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
1997-10-14
pubmed:abstractText
Several AB-toxins appear to have independently evolved mechanisms by which they undergo retrograde transport from the cell membrane to the endoplasmic reticulum (ER). Recent insights into ER-associated protein degradation (ERAD) now provide clues as to why these toxins have selected the ER as the site of cell entry. We propose that they disguise themselves as misfolded proteins to enter the ERAD pathway. We further link the observation that these toxins have few, if any, lysine residues to the need to escape ubiquitin-mediated protein degradation, the ultimate destination of the ERAD pathway. The actual membrane translocation step remains unclear, but studies on viral immune evasion mechanisms indicate that retrotranslocation across the ER lipid bilayer may involve SEC61. Understanding the internalization process of these toxins opens new avenues for preventing their entry into cells. In addition, this knowledge can be exploited to create protein-based pharmaceuticals that act on cytosolic targets.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11051-4
pubmed:dateRevised
2007-10-11
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells.
pubmed:affiliation
Department of Medical Microbiology and Immunology, University of Alberta, 1-41 Medical Sciences Building, Edmunton, Alberta, Canada T6G 2H7.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't