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MAGI-2 immunoreactivity is elevated in prostate cancer and high-grade prostatic intraepithelial neoplasia compared with normal tissue, suggesting that MAGI-2 may contribute to prostate carcinogenesis.
Immunohistochemistry in kidney sections from these patients revealed that mutations resulted in lack of or diminished podocyte MAGI2 expression. Our data support the finding that mutations in the MAGI2 gene are causal for congenital steroid-resistant nephrotic syndrome
MAGI-2 could represent a useful adjunct for diagnosis of prostatic adenocarcinoma
The expression of MAGI2 mRNA was significantly down-regulated in PC3 (show PCSK1 Proteins), LNCaP and DU-145 PCa (show FLVCR1 Proteins) cell lines.
MAGI2, SERPINE2 (show SERPINE2 Proteins), and NT5C3B expression levels are associated with airway wall thickening and additionally with bronchial inflammation, emphysema, and lung function, respectively, all features of chronic obstructive pulmonary disease.
Data show that the miR (show MLXIP Proteins)-134/487b/655 cluster regulates TGF-beta1 (show TGFB1 Proteins)-induced epithelial-mesenchymal transition and affected the resistance to gefitinib by directly targeting membrane-associated guanylate kinase (show GUK1 Proteins), WW, and PDZ domain-containing protein 2 (MAGI2).
In Usher syndrome 1G, mutations in SANS (show USH1G Proteins) eliminate Magi2 binding and thereby deregulate endocytosis, lead to defective ciliary transport modules and ultimately disrupt photoreceptor cell function inducing retinal degeneration.
MAGI2 enhances the sensitivity of BEL-7404 human hepatocellular carcinoma cells to staurosporine-induced apoptosis by increasing PTEN stability.
Common variants in MAGI2 gene are associated with increased risk for cognitive impairment in schizophrenic patients.
Results presented herein provide further evidence for a role of MAGI2 in bipolar affective disorder and schizophrenia etiology.
In summary,MAGI-2 and Fyn (show FYN Proteins) protect dendrin fromNedd4-2-mediated ubiquitination and from nuclear translocation, thereby maintaining the physiologic homeostasis of podocytes, and the lack of MAGI-2 in podocytes results in FSGS (show ACTN4 Proteins).
Magi2 is an essential component of the slit diaphragm complex that is required for nephrin (show NPHS1 Proteins) localization and foot process formation.
MAGI-2 has a critical role in maintaining the functional structure of the slit diaphragm and this molecule has an essential role in the functioning of the kidney filtration barrier.
We showed the expression patterns of MAGI-2 in detail in adult mice. Significant Venus expression was detected in various regions of the brain, also detected in glomeruli of the kidney. We found the novel expression of MAGI-2 in the testis.
MAGI-2 is required for the integrity of the kidney filter and podocyte survival.
elevation of S-SCAM expression in the excitatory neurons of forebrain was sufficient to induce an schizophrenia-like phenotype in mice.
In Usher syndrome 1G, mutations in SANS eliminate Magi2 binding and thereby deregulate endocytosis, lead to defective ciliary transport modules and ultimately disrupt photoreceptor cell function inducing retinal degeneration.
ARIP1 and ARIP2 (show SYNJ2BP Proteins) are co-expressed in some nerve cells and their biological activities are distinct.
Two subsynaptic domains, one containing IgSF9b for synaptic adhesion and the other containing gephyrin (show GPHN Proteins) and GABAA (show GABRg1 Proteins) receptors for synaptic transmission, are interconnected through S-SCAM and neuroligin 2 (show NLGN2 Proteins).
ARIP1 is a key molecule for the regulation of the action of activin in neurones, and also that decreased ARIP1 expression in the lesioned brain may be beneficial to the neurotrophic and neuroprotective roles of activin A (show INHBA Proteins) in recovery after brain injury.
The protein encoded by this gene interacts with atrophin-1. Atrophin-1 contains a polyglutamine repeat, expansion of which is responsible for dentatorubral and pallidoluysian atrophy. This encoded protein is characterized by two WW domains, a guanylate kinase-like domain, and multiple PDZ domains. It has structural similarity to the membrane-associated guanylate kinase homologue (MAGUK) family.
membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
, membrane associated guanylate kinase, WW and PDZ domain containing 2
, Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
, membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2-like
, activin receptor interacting protein 1
, atrophin-1-interacting protein 1
, atrophin-1-interacting protein A
, membrane-associated guanylate kinase inverted 2
, activin receptor-interacting protein 1
, synaptic-scaffolding molecule