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Endoplasmic reticulum protein 44 (ERp44) forms zinc ions (Zn(2+))-bridged homodimers, which dissociate upon client binding.
Results show that ERp44 binds the oxidized but not the reduced form of Prx4; the ERp44-Prx4 complex is formed via thiol-disulfide interchange reactions, and its crystal structure reveals a redox-dependent recognition.
Endogenous ERp44 is O-glycosylated and secreted by human primary endometrial cells, suggesting possible pathophysiological roles of these processes.
findings indicated that overexpression of miR-101 could downregulate ERp44
the decrease in 5-HT uptake rates of GDM trophoblast is the consequence of defective insulin signaling, which entraps SERT with ERp44 and impairs its glycosylation.
Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC).
The ERp44 assembly control cycle couples secretion fidelity and efficiency downstream of the calnexin/calreticulin and BiP-dependent quality control cycles.
contains a thioredoxin domain with a CRFS motif and is induced during ER stress
Ero1alpha and Ero1beta are retained in the endoplasmic reticulum by interactions with PDI and ERp44
ERGIC-53 provides a platform that receives micro(2)L(2) subunits from the BiP-dependent checkpoint, assisting polymerization. In this process, ERp44 couples thiol-dependent assembly and quality control.
ERp44-mediated retention of FGE, indicating that noncovalent interactions between ERp44 and FGE are sufficient to mediate ER retention.
Study shows that SUMF1 interacts with protein disulfide isomerase (PDI) and ERp44, two thioredoxin family members residing in the early secretory pathway, and with ERGIC-53, a lectin that shuttles between the ER and the Golgi.
Crystal structure of ERp44 at a resolution of 2.6 A, is presented.
The role of ERp44 in the dysfunction of endoplasmic reticulum in diabetic nephropathy.
ERp44 plays a critical role in embryonic heart development and is crucial in regulating cardiac cell Ca(2+) signaling, ER stress, ROS-induced oxidative stress, and activation of the intrinsic mitochondrial apoptosis pathway.
ERp44 exclusively recognizes and converts assembly-trapped adiponectin intermediates back to precursors of the biologically potent high molecular weight form.
Data show that endoplasmic reticulum protein 44 (ERp44) forms a mixed disulfide bond with aminopeptidase ERAP1 and controls the release of ERAP1 in a redox-dependent manner to control blood pressure.
Data suggest that ERp44 and Ero1-lalpha play a major role in the assembly of higher-order adiponectin complexes, and highlight the importance of posttranslational events controlling adiponectin levels and the release of adiponectin from adipocytes.
Tissue distribution analysis of Ero1L and ERp44 genes revealed extremely high expression in adipose tissue, and the topology of their phylogenic tree indicates a high degree of conservation among different species.
Results indicated that PPARgamma is an essential regulatory factor for the transcriptional activity of ERp44, which in turn controls the secretion of adiponectin.
Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum (By similarity).
endoplasmic reticulum protein 44
, endoplasmic reticulum resident protein 44-like
, ER protein 44
, endoplasmic reticulum resident protein 44
, endoplasmic reticulum resident protein 44 kDa
, protein disulfide isomerase family A, member 10
, thioredoxin domain containing 4 (endoplasmic reticulum)
, thioredoxin domain-containing protein 4
, endoplasmic reticulum resident protein ERp44
, endoplasmic reticulum resident protein 44kDa