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2015 ; 50
(6
): 477-88
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A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane
translocation pathways to cause disease
#MMPMID26362261
He K
; Ravindran MS
; Tsai B
Crit Rev Biochem Mol Biol
2015[]; 50
(6
): 477-88
PMID26362261
show ga
A dedicated network of cellular factors ensures that proteins translocated into
the endoplasmic reticulum (ER) are folded correctly before they exit this
compartment en route to other cellular destinations or for secretion. When
proteins misfold, selective ER-resident enzymes and chaperones are recruited to
rectify the protein-misfolding problem in order to maintain cellular
proteostasis. However, when a protein becomes terminally misfolded, it is ejected
into the cytosol and degraded by the proteasome via a pathway called
ER-associated degradation (ERAD). Strikingly, toxins and viruses can hijack
elements of the ERAD pathway to access the host cytosol and cause infection. This
review focuses on emerging data illuminating the molecular mechanisms by which
these toxic agents co-opt the ER-to-cytosol translocation process to cause
disease.