{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPDIA3, also known as ERp57 or GRP58, is a multifunctional endoplasmic reticulum enzyme that catalyzes disulfide bond formation and isomerization during the oxidative folding of newly synthesized glycoproteins. By interacting with the lectin chaperones calnexin and calreticulin, PDIA3 ensures proper quality control and maturation of many glycoproteins. In addition, its stable, disulfide‐linked association with tapasin within the major histocompatibility complex class I peptide–loading complex is critical for optimal peptide editing and antigen presentation, as well as for the proper assembly of CD1d and other glycoproteins dependent on glucose trimming."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its conventional role in protein folding, PDIA3 participates in diverse signaling-related processes. It functions as the membrane-associated rapid response steroid binding receptor (MARRS) for 1,25-dihydroxyvitamin D₃, thereby mediating non-genomic, rapid steroid hormone signals that influence cellular differentiation and survival. PDIA3 also physically associates with key transcriptional regulators—such as STAT3 and the redox factor Ref-1—to modulate their nuclear translocation and activity, impacting gene expression programs involved in inflammation, apoptosis, and cell proliferation. Furthermore, PDIA3 contributes to the assembly of signaling complexes such as mTORC1, thereby integrating stress responses with growth and metabolic pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, dysregulation of PDIA3 has been implicated in a variety of pathological conditions. Aberrant PDIA3 expression and/or activity has been associated with altered apoptosis and chemoresistance in several cancers—including ovarian, prostate, breast, cervical, hepatocellular carcinoma, and gliomas—as well as with neurodegenerative and fibrotic diseases. In platelet biology, PDIA3 influences integrin activation and thrombus formation, while in models of peripheral nerve injury, its regulation correlates with enhanced regeneration. Moreover, PDIA3 dysfunction has been linked to stress-induced responses in diverse cell types, underscoring its potential as both a prognostic biomarker and a therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Eva-Maria Frickel, Roland Riek, Ilian Jelesarov, et al. 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