2 results
Conserved C272/278 in b domain regulate the function of
PDI-P5 to make lysozymes trypsin-resistant forms via significant
intermolecular disulfide cross-linking.
Biochim Biophys Acta. 2015 May;1854(5):485-91. doi: 10.1016/j.bbapap.2015.02.014. Epub 2015 Feb 27.
PMID: 25731082
Protein disulfide isomerase-P5 (P5) is thought to have
important functions as an oxidoreductase, however, molecular functions
of P5 have not been fully elucidated. We have reported that P5 has insulin reductase activity and inhibits lysozyme refolding by formation of lysoz …
EMBO Mol Med. 2014 Jun;6(6):732-43. doi: 10.15252/emmm.201302561. Epub 2014 Apr 6.
PMID: 24843047
Free PMC article.
Accumulation of unfolded or misfolded proteins represents
the condition of ER stress and triggers the unfolded protein response
(UPR), a key mechanism linking supply of excess nutrients to insulin resistance and type 2 diabetes in obesity. The ER harbors proteins th …
Protein Disulfide Isomerase A6 Controls the Decay of IRE1α Signaling via Disulfide-Dependent Association
Our data thus suggest that PDIA6 ablation does not significantly induce
IRE1 activation nor does it affect the onset of IRE1 signaling. Rather,
it affects the inactivation of IRE1, as measured by attenuation of
phosphorylation of the sensor, XBP1 splicing, and JNK activation, in
response to both chemical stress and misfolded proteins.
All together, we conclude that PDIA6 affects UPR signaling via the IRE1
and PERK sensors, but not via ATF6. Because PERK and IRE1 do not
heterodimerize and expression or activation of PERK does not impact the
ribonuclease activity of IRE1 (Lin et al., 2009), the data suggest that PDIA6 impacts each sensor independently.
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