Results 161 to 170 of about 5,161 (196)
Revealing acute consequences of rapid degradation of synaptic fusion proteins at individual synapses using Auxin-Inducible Degron 2 technology. [PDF]
Elbaum-Mendelson L +8 more
europepmc +1 more source
Gephyrin-Lacking PV Synapses on Neocortical Pyramidal Neurons [PDF]
Gephyrin has long been thought of as a master regulator for inhibitory synapses, acting as a scaffold to organize γ-aminobutyric acid type A receptors (GABAARs) at the post-synaptic density.
Alison L Barth +2 more
exaly +9 more sources
Structural basis of dynamic glycine receptor clustering by gephyrin [PDF]
Gephyrin is a bi-functional modular protein involved in molybdenum cofactor biosynthesis and in postsynaptic clustering of inhibitory glycine receptors (GlyRs).
Winfried Weissenhorn +2 more
exaly +8 more sources
Abnormal gephyrin immunoreactivity associated with Alzheimer disease pathologic changes. [PDF]
Many neurodegenerative disorders involve the abnormal accumulation of proteins. In addition to the pathologic hallmarks of neurofibrillary tangles and β-amyloid plaques in Alzheimer disease (AD), here we show that abnormal accumulations of gephyrin, an ...
Duc Duong, Thomas J Montine, Allan Levey
exaly +2 more sources
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Functional Heterogeneity of Gephyrins
Molecular and Cellular Neuroscience, 2000Postsynaptic clustering of the glycine receptor requires the cytoplasmic protein gephyrin, which interacts with the receptor beta subunit. Several variants of gephyrin are generated by alternative splicing and differ by the presence of short amino acid sequences (cassettes) in the N-terminal half of the molecule.
J, Meier +3 more
openaire +2 more sources
Binding of gephyrin to microtubules is regulated by its phosphorylation at Ser270 [PDF]
AbstractGephyrin is a multifunctional scaffolding protein anchoring glycine- and subtypes of GABA type A- receptors at inhibitory postsynaptic membrane specializations by binding to the microtubule (MT) and/or the actin cytoskeleton. However, the conditions under which gephyrin can bind to MTs and its regulation are currently unknown.
Jochen Kuhse, Joachim Kirsch, Eva Kiss
exaly +4 more sources
Interactions of Drebrin and Gephyrin with Profilin
Biochemical and Biophysical Research Communications, 1998Profilin is an actin monomer-binding protein which stimulates actin polymerization. Recent studies have revealed that profilin interacts with VASP, Mena, Bnilp, Bnrlp, and mDia, all of which have the proline-rich domain. Here, we isolated three profilin-binding proteins from rat brain cytosol by glutathione S-transferase-profilin affinity column ...
A, Mammoto +8 more
openaire +2 more sources
Gephyrin expression and clustering affects the size of glutamatergic synaptic contacts.
We have recently shown that disrupting the expression and post-synaptic clustering of gephyrin in cultured hippocampal pyramidal cells, by either gephyrin RNAi (RNA interference) or over-expression of a dominant negative gephyrin-enhanced green ...
Angel L De Blas, Wendou Yu
exaly +2 more sources
Regulation of postsynaptic gephyrin cluster size by protein phosphatase 1
The scaffolding protein gephyrin is essential for the clustering of glycine and GABA(A) receptors (GABA(A)Rs) at inhibitory synapses. Here, we provide evidence that the size of the postsynaptic gephyrin scaffold is controlled by dephosphorylation ...
Heinrich Betz, Gregory A O'Sullivan
exaly +1 more source
1999
Abstract Gephyrin was originally identified as a peripheral membrane protein of 93 kDa, which copurifies with the -mammalian inhibitory glycine receptor upon affinity chromatography.8-10 lmmunoelectron microscopy locates gephyrin to the cytoplasmic face of glycinergic postsynaptic membranes in spinal cord, brain, and retina.
Joachim Kirsch, Heinrich Betz
openaire +1 more source
Abstract Gephyrin was originally identified as a peripheral membrane protein of 93 kDa, which copurifies with the -mammalian inhibitory glycine receptor upon affinity chromatography.8-10 lmmunoelectron microscopy locates gephyrin to the cytoplasmic face of glycinergic postsynaptic membranes in spinal cord, brain, and retina.
Joachim Kirsch, Heinrich Betz
openaire +1 more source

