Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase.
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MAGI3 localizes to epithelial tight junctions and binds PTEN through a PDZ interaction.
"the phosphatase binds to a PDZ domain of membrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions."
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MAGI3 cooperates with PTEN to regulate AKT and position PTEN near phospholipid signaling pathways.
"Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB."
Identification of MAGI-3 as a transforming growth factor-alpha tail binding protein.
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MAGI3 PDZ1 binds pro-TGF-alpha and promotes efficient TGF-alpha trafficking to the epithelial cell surface.
"Overexpression of MAGI-3 resulted in increased levels of TGFalpha in the basolateral medium of polarized MDCK cells, suggesting that MAGI-3 has a role in efficient trafficking of TGFalpha to the cell surface in polarized epithelial cells."
Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins.
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MAGI3 PDZ1 recognizes the beta1-adrenergic receptor tail and selectively attenuates receptor-induced ERK1/2 activation.
"MAGI-3 co-expression with beta1AR profoundly impaired beta1AR-mediated ERK1/2 activation but had no apparent effect on beta1AR-mediated cyclic AMP generation or agonist-promoted beta1AR internalization."
EG-1 interacts with c-Src and activates its signaling pathway.
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The abstract reports that MED28/EG-1 associates with multiple WW-domain signaling proteins, but does not name MAGI3.
"EG-1 shows interaction with multiple other SH3- and WW-containing molecules involved in various signaling pathways."
Beta-2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI-3.
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MAGI3 PDZ5 binds the beta2-adrenergic receptor and retards its ERK1/2 output.
"beta2AR-stimulated extracellular signal-regulated kinase-1/2 (ERK1/2) activation was substantially retarded by MAGI-3 expression."
Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling.
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The primary study establishes an RNF146-tankyrase-Axin ubiquitin system; the locally extracted main text does not name MAGI3.
"We show that RNF146, tankyrase, and Axin form a protein complex"
Cellular localization and characterization of cytosolic binding partners for Gla domain-containing proteins PRRG4 and PRRG2.
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WW-domain arrays and GST pulldown directly support MAGI3 binding to PRRG4.
"All the tested WW domain-containing proteins (YAP1, YAP2, WWTR1, MAGI-1, MAGI-3, NEDD4, NEDD4L) bound to GST-PRRG4cyto but not to the GST-only control"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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BioPlex supplies cell-line-specific affinity-purification interaction candidates rather than focused functional characterization of MAGI3.
"Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks."
Quantitative fragmentomics allow affinity mapping of interactomes.
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The study maps affinities for a large PDZ-domain/PDZ-binding-motif network, including host-virus interaction space relevant to MAGI3.
"Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM)"
Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase beta (RPTP beta) and tyrosine-phosphorylated proteins.
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MAGI3 is directly localized to selected plasma-membrane and nuclear sites and to epithelial and astrocyte junctions.
"Immunofluorescence and immunoelectron microscopy revealed that MAGI-3 is concentrated in specific sites at the plasma membrane and in the nucleus."
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MAGI3 links receptor tyrosine phosphatase beta to a protein substrate at the plasma membrane.
"These findings suggest a possible role for MAGI-3 as a scaffolding molecule that links receptor tyrosine phosphatase with its substrates at the plasma membrane."
MAGI-3 regulates LPA-induced activation of Erk and RhoA.
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MAGI3 directly binds LPA2 and supports LPA-induced ERK and RhoA activation in SW480 cells.
"These results demonstrate that MAGI-3 interacts directly with LPA(2) and regulates the ability of LPA(2) to activate Erk and RhoA."
MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap.
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Mouse MAGI3 assembles a FZD4-Ltap complex and positively regulates JNK through Rac.
"MAGI-3 strongly activated JNK in conjunction with frizzled-4 and Ltap, and that this activation required the small GTPase, Rac."
Premature polyadenylation of MAGI3 produces a dominantly-acting oncogene in human breast cancer.
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MAGI3 is a multidomain scaffold with a catalytically inactive guanylate-kinase-like region.
"MAGI3 is a scaffolding protein with 2 WW and 6 PDZ domains, along with a catalytically inactive region of homology to the yeast guanylate kinase"
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Full-length MAGI3 restrains YAP through PDZ6, while a tumor-associated truncated product disrupts that inhibitory complex.
"the C-terminal PDZ6 domain of MAGI3 is essential for MAGI3/YAP interaction"
E3 ubiquitin ligase MAGI3 degrades c-Myc and acts as a predictor for chemotherapy response in colorectal cancer.
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MAGI3 bridges c-Myc to a SKP1-CUL1 ubiquitin-ligase assembly through distinct PDZ domains.
"these results demonstrate the existence of a macromolecular complex c-Myc-MAGI3-SKP1-CUL1"
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MAGI3 promotes c-Myc ubiquitin-dependent proteasomal degradation.
"MAGI3 modulates c-Myc protein stability by promoting c-Myc ubiquitin–proteasome degradation"
UniProtKB Q5TCQ9 MAGI3 record
Manual deep research synthesis for human MAGI3
Manual MAGI3 review notes