MAGED2 controls vasopressin-induced aquaporin-2 expression in collecting duct cells

Reusch, Björn; Bartram, Malte P.; Dafinger, Claudia; Palacio-Escat, Nicolàs; Wenzel, Andrea; Fenton, Robert A.; Sáez-Rodríguez, Julio; Schermer, Bernhard; Benzing, Thomas; Altmüller, Janine; Beck, Bodo B.; Rinschen, Markus M.

doi:10.1016/j.jprot.2021.104424

Cited by 3 publications

(3 citation statements)

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“… 53 In the same study, MAGE D2 was discovered to interact directly with Gαs, and other studies suggested that MAGE D2 modulates GPCR signaling. 53 , 54 , 55 …”

Section: Resultsmentioning

confidence: 99%

Gαs slow conformational transition upon GTP binding and a novel Gαs regulator

Ahn¹,

Provasi²,

Duc³

et al. 2023

iScience

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“… 53 In the same study, MAGE D2 was discovered to interact directly with Gαs, and other studies suggested that MAGE D2 modulates GPCR signaling. 53 , 54 , 55 …”

Section: Resultsmentioning

confidence: 99%

Gαs slow conformational transition upon GTP binding and a novel Gαs regulator

Ahn¹,

Provasi²,

Duc³

et al. 2023

iScience

View full text Add to dashboard Cite

“…Mutations in MAGE D2 have been reported to cause Bartter’s syndrome, a rare autosomal recessive renal tubular disorder (Laghmani et al, 2016). In the same study, MAGE D2 was discovered to interact directly with Gαs, and other studies suggested that MAGE D2 modulates GPCR signaling (Laghmani et al ., 2016; Paek et al, 2017; Reusch et al, 2022).…”

Section: Resultsmentioning

confidence: 99%

Gαs slow conformational transition upon GTP binding and a novel Gαs regulator

Ahn

Provasi

Duc

et al. 2022

Preprint

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G proteins are major signaling partners for G protein–coupled receptors (GPCRs). Although stepwise structural changes during GPCR–G protein complex formation and guanosine diphosphate (GDP) release have been reported, no information is available with regard to guanosine triphosphate (GTP) binding. Here, we used a novel Bayesian integrative modeling framework that combines data from hydrogen–deuterium exchange mass spectrometry, tryptophan–induced fluorescence quenching, and metadynamics simulations to derive a kinetic model and atomic-level characterization of stepwise conformational changes incurred by the β2–adrenergic receptor β2AR–Gs complex after GDP release and GTP binding. Our data suggest rapid GTP binding and GTP–induced dissociation of Gαs from β2AR and Gβγ as opposed to a slow closing of the Gαs α–helical domain (AHD). Yeast–two–hybrid screening using Gαs AHD as bait identified melanoma-associated antigen D2 (MAGE D2) as a novel AHD–binding protein, which was also shown to accelerate the GTP–induced closing of the Gαs AHD.

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“…The melanoma-associated antigen D2 (MAGED2) is a member of the melanoma-associated antigen family which is consistent with Type I genes (MAGE-A, -B and -C) and type II genes (MAGE-D, -E, -F, -G and -H) [4]. MAGED2 has been identi ed as being critical for transcriptional regulation, epigenetic alteration, and cell development and differentiation [5]. Furthermore, numerous studies have shown that MAGED2 is a tumor-speci c antigen that plays an important role in tumor progression and metastasis, including hepatocellular carcinoma[6],gastric cancer [7], and lymphoma [8].…”

Section: Introductionmentioning

confidence: 99%

Expression and prognostic value of Melanoma-associated antigen D2 in gliomas

Yan

Lenahan³

et al. 2022

Preprint

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Introduction The melanoma-associated antigen D4 (MAGED2) is one of the melanoma-associated antigen family members. It is commonly overexpressed in a variety of malignancies. However, the mechanism and function of MAGED2 in glioma remain unknown. Methods The TCGA and Oncomine databases were used to determine the expression level of MAGED2 and its relationship to glioma. MAGED2 protein expression in 98 tumor tissues from glioma patients was measured using RT-qPCR, Western blot and immunohistochemistry, and the associations between MAGED4 expression and clinicopathological factors were evaluated. qRT-PCR and Western blots were used to assess the levels of MAGED2 and CDKN1A expression in glioma U251-MG cells following transfection of MAGED2 CRISPR. CCK-8, colony formation, and EdU assays were used to assess the effect of MAGED2 on U251-MG cell proliferation, and flowcytometry was used to track changes in the cell cycle and cell apoptosis following MAGED2 CRISPR transfection. Results In the current investigation, MAGED2 was shown to be substantially expressed in human glioma tissues, and high MAGED2 expression predicted poor recurrence-free survival (RFS) and overall survival (OS) for glioma patients. The presence of high MAGED2 expression was related to WHO grade, Ki-67, IDH1/2, MGMT, and survival status. Furthermore, MAGED2 expression knockdown significantly inhibited the proliferation and colony formation potential of U251-MG cells by preventing cell cycle arrest at the G0/G1 phase and triggering apoptosis. Moreover, our findings indicated that the mRNA and protein expression levels of CDKN1A were considerably up-regulated in vitro following MAGED2 CRISPR transfection. MAGED2 downregulation inhibited the ability of cell proliferation in the U251-MG cells through restoring CDKN1A. Conclusions To conclude, the current study's findings imply that a high level of MAGED2 expression predicts a poor prognosis for glioma patients. MAGED2 can stimulate the proliferation of glioma U251-MG cells by targeting CDKN1A. MAGED2 may be a possible biomarker for glioma and an important prognostic factor for glioma patients.

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MAGED2 controls vasopressin-induced aquaporin-2 expression in collecting duct cells

Cited by 3 publications

References 54 publications

Gαs slow conformational transition upon GTP binding and a novel Gαs regulator

Gαs slow conformational transition upon GTP binding and a novel Gαs regulator

Gαs slow conformational transition upon GTP binding and a novel Gαs regulator

Expression and prognostic value of Melanoma-associated antigen D2 in gliomas

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