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    ERP44 endoplasmic reticulum protein 44 [ Homo sapiens (human) ]

    Gene ID: 23071, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Biogenesis of secretory immunoglobulin M requires intermediate non-native disulfide bonds and engagement of the protein disulfide isomerase ERp44.

    Biogenesis of secretory immunoglobulin M requires intermediate non-native disulfide bonds and engagement of the protein disulfide isomerase ERp44.
    Giannone C, Chelazzi MR, Orsi A, Anelli T, Nguyen T, Buchner J, Sitia R., Free PMC Article

    02/19/2022
    Protein tyrosine phosphatase receptor type O (PTPRO) knockdown enhances the proliferative, invasive and angiogenic activities of trophoblast cells by suppressing ER resident protein 44 (ERp44) expression in preeclampsia.

    Protein tyrosine phosphatase receptor type O (PTPRO) knockdown enhances the proliferative, invasive and angiogenic activities of trophoblast cells by suppressing ER resident protein 44 (ERp44) expression in preeclampsia.
    Yang Y, Qiu X, Wang F., Free PMC Article

    02/19/2022
    Exosomal ERp44 derived from ER-stressed cells strengthens cisplatin resistance of nasopharyngeal carcinoma.

    Exosomal ERp44 derived from ER-stressed cells strengthens cisplatin resistance of nasopharyngeal carcinoma.
    Xia T, Tian H, Zhang K, Zhang S, Chen W, Shi S, You Y., Free PMC Article

    10/23/2021
    The regulatory network of lncRNA DLX6-AS1/miR-149-5p/ERP44 is possibly related to the progression of preeclampsia.

    The regulatory network of lncRNA DLX6-AS1/miR-149-5p/ERP44 is possibly related to the progression of preeclampsia.
    Liu R, Wang X, Yan Q.

    04/13/2021
    Endoplasmic reticulum protein 44 (ERp44) forms zinc ions (Zn(2+))-bridged homodimers, which dissociate upon client binding.

    Zinc regulates ERp44-dependent protein quality control in the early secretory pathway.
    Watanabe S, Amagai Y, Sannino S, Tempio T, Anelli T, Harayama M, Masui S, Sorrentino I, Yamada M, Sitia R, Inaba K., Free PMC Article

    04/13/2019
    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.

    Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.
    Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X.

    05/6/2017
    Endogenous ERp44 is O-glycosylated and secreted by human primary endometrial cells, suggesting possible pathophysiological roles of these processes.

    Progressive quality control of secretory proteins in the early secretory compartment by ERp44.
    Sannino S, Anelli T, Cortini M, Masui S, Degano M, Fagioli C, Inaba K, Sitia R., Free PMC Article

    11/21/2015
    findings indicated that overexpression of miR-101 could downregulate ERp44

    MiR-101 regulates apoptosis of trophoblast HTR-8/SVneo cells by targeting endoplasmic reticulum (ER) protein 44 during preeclampsia.
    Zou Y, Jiang Z, Yu X, Zhang Y, Sun M, Wang W, Ge Z, De W, Sun L.

    06/27/2015
    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.

    GDM-associated insulin deficiency hinders the dissociation of SERT from ERp44 and down-regulates placental 5-HT uptake.
    Li Y, Hadden C, Singh P, Mercado CP, Murphy P, Dajani NK, Lowery CL, Roberts DJ, Maroteaux L, Kilic F., Free PMC Article

    04/25/2015
    Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC).

    Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.
    Kakihana T, Araki K, Vavassori S, Iemura S, Cortini M, Fagioli C, Natsume T, Sitia R, Nagata K., Free PMC Article

    12/14/2013
    The ERp44 assembly control cycle couples secretion fidelity and efficiency downstream of the calnexin/calreticulin and BiP-dependent quality control cycles.

    A pH-regulated quality control cycle for surveillance of secretory protein assembly.
    Vavassori S, Cortini M, Masui S, Sannino S, Anelli T, Caserta IR, Fagioli C, Mossuto MF, Fornili A, van Anken E, Degano M, Inaba K, Sitia R., Free PMC Article

    09/14/2013
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article

    09/15/2010
    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.

    Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44.
    Fraldi A, Zito E, Annunziata F, Lombardi A, Cozzolino M, Monti M, Spampanato C, Ballabio A, Pucci P, Sitia R, Cosma MP.

    01/21/2010
    Crystal structure of ERp44 at a resolution of 2.6 A, is presented.

    Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail.
    Wang L, Wang L, Vavassori S, Li S, Ke H, Anelli T, Degano M, Ronzoni R, Sitia R, Sun F, Wang CC., Free PMC Article

    01/21/2010
    ERp44-mediated retention of FGE, indicating that noncovalent interactions between ERp44 and FGE are sufficient to mediate ER retention.

    ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum.
    Mariappan M, Radhakrishnan K, Dierks T, Schmidt B, von Figura K.

    01/21/2010
    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.

    Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis.
    Anelli T, Ceppi S, Bergamelli L, Cortini M, Masciarelli S, Valetti C, Sitia R., Free PMC Article

    01/21/2010
    contains a thioredoxin domain with a CRFS motif and is induced during ER stress

    ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family.
    Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R., Free PMC Article

    01/21/2010
    Ero1alpha and Ero1beta are retained in the endoplasmic reticulum by interactions with PDI and ERp44

    Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44.
    Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R.

    01/21/2010
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