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GPHN encodes a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. Additionally we are shipping Gephyrin Antibodies (77) and many more products for this protein.
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duplicated gephyrin genes mediate Moco biosynthesis and control postsynaptic clustering of glycine receptor (show GLRB Proteins)
A missense mutation of gephyrin that was unable to synthesize MoCo and activate MoCo-dependent enzymes was identified.
A yin-yang haplotype pattern encompassing gephyrin consists of 284 divergent nucleotide states and both variants vary drastically from their mutual ancestral haplotype, suggesting rapid evolution.
The N-terminal region of GABRA3 (show GABRA3 Proteins) and the GlyR beta subunit (show POLG Proteins) occupies the same binding site of gephyrin.
Results show that PKC (show PRRT2 Proteins)-dependent phosphorylation of GAP43 (show GAP43 Proteins) plays a critical role in regulating postsynaptic gephyrin aggregation in developing GABAergic synapses.
Structural exonic microdeletions affecting the GPHN gene constitute a rare genetic risk factor for IGE and other neuropsychiatric disorders by an impairment of the GABAergic inhibitory synaptic transmission.
The enhancement of Cb-induced gephyrin clustering by GTP (show AK3 Proteins)-TC10 (show RHOQ Proteins) does not depend on the guanine nucleotide exchange activity of Cb but involves an interaction that resembles reported interactions of other small GTPases with their effectors
abnormal accumulations of gephyrin are highly correlated with the neuropathologic diagnosis of Alzheimer disease in 17 AD versus 14 control cases. Furthermore, gephyrin accumulations were specific for AD.
Rare exonic deletions implicate the synaptic organizer Gephyrin (GPHN) in risk for autism, schizophrenia and seizures.
Extracellular signal-regulated kinase and glycogen synthase kinase 3beta regulate gephyrin postsynaptic aggregation and GABAergic synaptic function in a calpain-dependent mechanism
A reduction in the number of gephyrin clusters in primary neurons reduces GABA signaling.
adult mice lacking interleukin-1 receptor 1 (IL-1R1) exhibit increased expression of both the excitatory scaffolding protein postsynaptic density-95 (PSD-95) and inhibitory scaffolding proteingephyrin, respectively, in the hippocampus.
The results demonstrate that formation of GABAergic synapses containing a postsynaptic gephyrin scaffold is crucial for morphological differentiation, synaptic integration, and long-term survival of adult-born granule cells/
Data suggest that KIF5 regulates gephyrin sorting by a mechanism that involves GSK3 activity.
Pin1 (show PIN1 Proteins)-dependent signaling represents a mechanism to modulate GABAergic transmission by regulating NL2 (show MMEL1 Proteins)/gephyrin interaction.
These results reveal a homeostatic mechanism through which activity regulates the dynamics and function of perisomatic inhibitory synapses, and they identify a CaMKII (show CAMK2G Proteins)-dependent phosphorylation site on gephyrin.
study reveals that palmitoylation of gephyrin by DHHC-12 contributes to dynamic and functional modulation of GABAergic synapses
Within this network, collybistin (show Arhgef9 Proteins) can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides.
these findings suggest that gephyrin may be a key factor in BDNF (show BDNF Proteins)-dependent GABAAR (show GABRG2 Proteins) regulation in the amygdala.
Data suggest that the loss of neurotransmitter receptor (show GRIN1 Proteins) clustering at inhibitory synapses causes the early lethality of gephyrin deficient mice.
Gephyrin is critical for glycine receptor (show GLRB Proteins) clustering in hippocampal neurons.
This gene encodes a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. In nonneuronal tissues, the encoded protein is also required for molybdenum cofactor biosynthesis. Mutations in this gene may be associated with the neurological condition hyperplexia and also lead to molybdenum cofactor deficiency. Numerous alternatively spliced transcript variants encoding different isoforms have been described\; however, the full-length nature of all transcript variants is not currently known.
, gephyrin isoform
, putative glycine receptor-tubulin linker protein