High impact information on Pdia4

• Interestingly, depletion of another thiol oxidoreductase, ERp72, had no detectable effect on class I biogenesis, consistent with a specialized role for ERp57 in this process [1].
• Here, ERp72, the other member of the protein disulfide-isomerase family containing three CGHC motifs, was isolated from ER of rat and mouse livers through four sequential chromatographies on DEAE-Toyopearl 650, AF-heparin Toyopearl 650M, and TSK gel G3000SW twice [2].
• Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum [2].
• The proteolytic activity of rat ERp72 was inhibited by cysteine protease inhibitors [2].
• The partial amino acid sequence of rat ERp72 was 93% homologous to that of mouse ERp72 [2].

Biological context of Pdia4

• Analysis of the murine ERp72 promoter region revealed the presence of potential transcriptional control elements characteristic of the promoters of mammalian ER proteins [3].
• The ERp72 promoter contains an 82 bp ER protein traffic response element (ERPTRE) that is sufficient to mediate this response [4].

Anatomical context of Pdia4

• The ERp61 and ERp72 mRNAs were present at 2- to 3-fold higher levels in the pituitary glands of the 10- and 22-day-old mice, than in the adult mice [5].

Other interactions of Pdia4

• Functional characterization of 3 thioredoxin homology domains of ERp72 [6].
• Both ERp60 and ERp72 are entirely protected by the endoplasmic reticulum membrane while ERp99 appears to have a large domain exposed on the cytoplasmic face of the endoplasmic reticulum [7].

References