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critical role played by the PMCA2w/a pump in the control of hair cell function and survival, and provide mechanistic insight into the etiology of deafness and vestibular disorders.
PMCA2 loss plays a role in the ataxic phenotype, but can paradoxically also minimise calcium rises in cerebellar Purkinje neurons, thereby ensuring their resilience and survival.
Loss-of-function variants of ATP2B2 are associated with rapidly progressive hearing impairment.
PMCA2 regulates breast cancer cell proliferation and sensitivity to doxorubicin in basal cell carcinoma.
Cytoskeleton dynamics regulates plasma membrane PMCA2 activity.
Data show that ATPase, calcium transporting, plasma membrane 2 protein (PMCA2) silencing augmented B-cell leukemia 2 family proteins (Bcl-2) inhibitor ABT-263-mediated MDA-MB-231 breast cancer cell death.
NHERF1 acts with PMCA2 to regulate HER2 signaling and membrane retention in breast cancers
PMCA2 interacts with HER2 in specific actin-rich membrane domains.
PMCA2b resulted in rapid and highly PMCA abundance-sensitive clearance of store-operated Ca2+ entry-mediated Ca2+ transients.
SERCA and PMCA pump activities are strongly affected by the localization of F508del-CFTR protein.
ATP2B2 might play a role in the etiology of autism in Chinese Han population.
G293S and V586M mutations in the PMCA2 Calcium Transporting ATPase of the stereocilia are associated with deafness. (Review)
The human mutant of PMCA2 exacerbated the deafness produced by a cadherin 23 mutation. The human mutant failed to impair the Ca(2+) ejection by the pump.
These results provide converging evidence for an association between ATP2B2 gene variants and autism in male subjects
these data suggest that full polarization is a prerequisite for proper positioning of the PMCA2w variants in the apical membrane domain of polarized cells.
It appears that Ca extrusion via the sarcolemmal Ca ATPase occurs only at the t-tubules, and is not regulated by basal PKA activity.
Report a novel interaction between endogenous plasma membrane calcium ATPase (PMCA) and eNOS in endothelial cells. PMCA may negatively modulate eNOS activity, and NO-dependent signal transduction pathways.
Apical scaffolding protein NHERF2 modulates the localization of alternatively spliced plasma membrane Ca2+ pump 2B variants in polarized epithelial cells.
Alternative splicing of the first intracellular loop of PMCA2 alters its membrane targeting
role in the intracellular Ca(2+) extrusion of syncytiotrophoblast-like structure originating from the differentiation of cultured trophoblast cells isolated from human term placenta
Early growth response protein 1 regulates promoter activity of alpha-plasma membrane calcium ATPase 2, a major calcium pump in the brain and auditory system
These findings indicate a novel role for PMCA2 in modality- and sex-dependent pain responsiveness. Female-specific molecular changes potentially account for the altered pain responses
These results indicate that a significant fraction of the postsynaptic NMDAR current is reliant on a perisynaptic extracellular alkaline shift generated by the PMCA.
Our results demonstrate that PMCA2 activity is an important regulator of the dendritic calcium equilibrium controlling Purkinje cell dendritic growth
This study further resolves the interaction between Atp2b2 and Cdh23 in a gene dosage and frequency-dependent manner, and finds that low auditory frequencies are significantly affected by the interaction.
loss of PMCA2 adversely influences the function and organisation of Purkinje neuron synaptic inhibition
The Atp2b2 (Deaf13) mutation leads to a p. R561S substitution in the catalytic core. Mice homozygous for these mutations display profound hearing loss.
Amplitude of depolarization and AMPAR-mediated Ca(2+) transients are significantly higher in cultured PMCA2(+/-) than in PMCA2(+/+) Purkinje cells due to increased Ca(2+) influx.
Plasma membrane calcium pump (PMCA) isoform 4 is targeted to the apical membrane by the w-splice insert from PMCA2.
PMCA1 but not PMCA2 localization is compromized by the loss of Cav1.4 protein.
The murine mutant of PMCA2 overexpressed in model cells (HeLa) displayed an evident defect both in the basal activity of the Ca(2+)pump and in the long range ejection of Ca(2+).
Whole cell patch clamp recordings from PMCA2-/- PNs revealed that they possessed hyperpolarised membrane potentials, reduced frequency and increased irregularity of spontaneous action potential firing.
Data link the reduction in PMCA2 expression with perturbations in CRMP1 expression and death of spinal cord neurons, representing an additional mechanism underlying AMPA/kainate receptor-mediated excitotoxicity with relevance to neurodegeneration in EAE.
PMCA2 missense mutation, Tommy, impairs cytosolic calcium clearance in hair cells and Tommy mice show hearing impairment.
PMCA2 regulates apoptosis during mammary gland involution and predicts outcome in breast cancer
Although PMCA2(+/-) mice exhibited outwardly normal behaviour and little change in their gait pattern, when challenged to run on a narrow beam they exhibited clear deficits in hindlimb coordination.
In homozygous mice structural changes in cochlear hair cells, spiral ganglion neurones and spherical cells in the cochlear nucleus result from PMCA2 mutation and the subsequent accumulation of toxic levels of calcium that alter their functional integrity.
Fifteen days following an 8 h, 113 dB noise exposure, Pmca2+/- mice displayed significant permanent threshold shifts at 16 and 32 kHz that were 15 or 25 dB greater than those observed in Pmca2+/+ littermates.
The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 2. Alternatively spliced transcript variants encoding different isoforms have been identified.
plasma membrane Ca(2+)-ATPase
, plasma membrane Ca2+ pump 2
, plasma membrane calcium ATPase
, plasma membrane calcium pump
, plasma membrane calcium-transporting ATPase 2
, ATPase, Ca++ transporting, plasma membrane 4
, plasma membrane calcium ATPase 2
, ATPase, Ca++ transporting, plasma membrane 2
, plasma membrane calcium-transporting ATPase 4
, deaf waddler
, ATPase isoform 2 Na+K+ transporting beta polypeptide 2
, ATPase isoform 2, Na+K+ transporting, beta polypeptide 2
, plasma membrane Ca++-ATPase
, plasma membrane calcium-transporting ATPase 2-like