| 1990 |
AMOG (ATP1B2) is a homologue of the β-subunit of Na,K-ATPase with 40% amino acid identity to the rat brain Na,K-ATPase β subunit. Immunoaffinity-purified AMOG was associated with a 100 kDa protein comprising the α2 (and possibly α3) isoforms of the Na,K-ATPase catalytic subunit, but not α1. A monoclonal anti-AMOG antibody that blocks adhesion increased ouabain-inhibitable 86Rb+ uptake in intact cultured astrocytes, demonstrating functional association with the Na,K-ATPase pump. AMOG-mediated adhesion occurred at 4°C and in the presence of ouabain, indicating adhesion is independent of Na,K-ATPase pump activity. |
cDNA sequencing, immunoaffinity purification, immunoprecipitation, 86Rb+ uptake assay, monoclonal antibody blocking |
The Journal of cell biology |
High |
1688561
|
| 1992 |
AMOG/β2 expressed by cRNA injection in Xenopus oocytes assembles with endogenous Xenopus α1 or coexpressed Torpedo α1 subunits to form a functional α1/AMOG sodium pump isozyme, as demonstrated by ouabain binding site quantification and ouabain-sensitive 86Rb+ uptake. The α1/AMOG isozyme has slightly lower maximum transport rate and apparent affinity for external K+ than the α1/β1 isozyme. Immunoprecipitation from digitonin extracts confirmed stable association between AMOG and α1 subunits. |
Xenopus oocyte expression system, cRNA injection, ouabain binding assay, 86Rb+ uptake assay, immunoprecipitation |
The Journal of biological chemistry |
High |
1383200
|
| 1993 |
AMOG/β2, but not the β1 subunit of Na,K-ATPase, promotes neurite outgrowth when expressed on L-cells used as substrates for cerebellar and hippocampal neurons. This effect was specifically inhibited by anti-AMOG/β2 antibodies and a neuronal membrane fraction, and partially inhibited by the soluble recombinant extracellular domain of AMOG/β2, demonstrating that the extracellular domain mediates this function via an unknown neuronal receptor. |
Transfection of L-cells, neurite outgrowth assay, antibody blocking, recombinant extracellular domain inhibition |
The Journal of biological chemistry |
High |
7504672
|
| 1988 |
Immunoaffinity-purified AMOG incorporated into liposomes binds specifically to neurons (including PC12 cells) but not to oligodendrocytes, astrocytes, or fibroblasts in cerebellar cultures. Binding was inhibited by Fab fragments of monoclonal AMOG antibodies (but not by L3 anti-carbohydrate antibodies), and was not blocked by antibodies to L1, N-CAM, or L2/HNK-1, demonstrating AMOG acts as an adhesion ligand for specific neuronal subpopulations via a distinct, independent mechanism. |
Liposome reconstitution assay, cell binding assay, Fab fragment inhibition |
The Journal of neuroscience |
Medium |
2457661
|
| 2003 |
Re-expression of AMOG/β2 in AMOG/β2-negative C6 rat glioma cells by transfection increased cell adhesion and decreased migration on Matrigel compared to AMOG/β2-negative counterparts, demonstrating a direct role of AMOG/β2 in controlling glioma cell adhesion and invasion. |
Transfection/re-expression, Matrigel invasion assay, adhesion assay |
Neuropathology and applied neurobiology |
Medium |
12887597
|
| 2013 |
Overexpression of AMOG in GBM cells decreased invasion without affecting migration or proliferation, while knockdown of AMOG in normal human astrocytes increased invasion, establishing a direct role for AMOG/β2 in suppressing glioma invasion. |
Overexpression and siRNA knockdown, Matrigel invasion assay, scratch assay, direct cell counting |
Neuro-oncology |
Medium |
23887941
|
| 2019 |
In cerebellar granule precursor cells, β2-subunit (AMOG) knockdown resulted in increased Merlin/NF2 expression, increased YAP phosphorylation, and decreased N-Ras expression, demonstrating that β2-subunit negatively regulates Merlin/NF2 and thereby modulates Hippo/YAP signaling. β2 knockdown also altered EGFR signaling kinetics in a Merlin-dependent manner and impaired EGF-induced actin cytoskeleton reorganization. Isoform specificity was confirmed: β1 knockdown did not replicate these effects. |
siRNA knockdown, immunoblotting, EGF stimulation assays, actin cytoskeleton imaging |
Molecular neurobiology |
Medium |
31062247
|
| 2019 |
Reduction of AMOG expression in human glioblastoma cells (U-87 MG, U251, SHG44) elevated L1CAM expression, accompanied by decreased cell apoptosis and senescence, establishing an inverse regulatory relationship between AMOG and L1CAM expression in glioma cells. |
siRNA knockdown, immunoblotting, flow cytometry (apoptosis/senescence assays) |
BMC cancer |
Medium |
31510944
|
| 1996 |
Disruption of the AMOG/β2 gene in mice leads to apoptotic (TUNEL-positive, ultrastructurally confirmed) death of photoreceptor cells in the retina beginning around postnatal day 9 and massively by day 16, correlated with elevated GFAP in retinal astrocytes and ectopic GFAP in Müller cells, while other retinal cell types are unaffected. |
AMOG/β2 knockout mice, TUNEL labeling, electron microscopy, immunohistochemistry |
Journal of neurocytology |
Medium |
8793730
|
| 2022 |
The glycosylated extracellular domain of human β2/AMOG can form energetically stable trans-interacting homodimers. CHO fibroblasts transfected with β2 formed larger cell aggregates than controls; tunicamycin treatment reduced aggregation, implicating N-glycans. Protein-protein interaction assays in MDCK and CHO cells showed β2 subunits on the cell surface interact with each other in trans, establishing β2/AMOG as a homophilic adhesion molecule. |
Protein docking (in silico), cell-cell aggregation assay, protein-protein interaction assay (co-culture with differentially tagged constructs), tunicamycin treatment |
International journal of molecular sciences |
Medium |
35887102
|
| 1992 |
The cis-acting positive regulatory element AMRE (sequence GAGGCGGGG at positions -87 to -79) in the rat AMOG/Na,K-ATPase β2 subunit gene promoter enhances promoter activity and acts in a mutually compensating manner with an Sp1 element at -147 to -142, as demonstrated by transient transfection assays in multiple cell lines. |
Transient transfection assay, promoter deletion/mutation analysis |
Journal of biochemistry |
Medium |
1377671
|
| 2017 |
A SINE insertion (227 bp) into the ATP1B2 gene in Belgian Shepherd (Malinois) dogs causes aberrant RNA splicing, reduced ATP1B2 protein expression in the CNS, and results in spongy degeneration with cerebellar ataxia (SDCA2), a phenotype similar to Atp1b2 knockout mice. |
Linkage and homozygosity mapping, whole-genome sequencing, RT-PCR (aberrant splicing), immunohistochemistry |
G3 (Bethesda, Md.) |
Medium |
28620085
|
| 2025 |
In Atp1b2 knock-in mice (expressing β1 instead of β2 under Atp1b2 regulatory elements), cones degenerate rapidly (absent by 4 months) while rods degenerate slowly, demonstrating that β2 is specifically required for cone photoreceptor survival and cannot be fully replaced by β1. Levels of retinoschisin, a secreted retina-specific protein that directly interacts with the β2-subunit, were greatly reduced in mutant retinas, linking β2 to retinoschisin-dependent signaling. |
Knock-in mouse model, immunohistochemistry, in situ hybridization, cell counting |
Cells |
Medium |
40558505
|
| 2017 |
The ACSA-2 antibody epitope was identified as ATP1B2 by overexpression and knockdown assays, immunoblotting, and immunohistochemistry, establishing ATP1B2 as a cell surface marker of astrocytes in adult mouse brain that is stably expressed across multiple CNS injury and disease models. |
Overexpression, siRNA knockdown, immunoblotting, immunohistochemistry, single-cell sequencing |
The Journal of biological chemistry |
Medium |
28373281
|