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anti-Human Arhgef9 Antibodies:
anti-Rat (Rattus) Arhgef9 Antibodies:
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Autism spectrum disorder patient with the smallest inactivating deletion in the collybistin gene.
Collybistin forms a complex with mTOR (show FRAP1 Antibodies) and eIF3 (show EIF3A Antibodies) and by sequestering these proteins downregulates mTORC1 signaling and protein synthesis potentially contributing to intellectual disability and autism.
Impairment of the membrane lipid binding activity of Collybistin R290H and a consequent defect in inhibitory synapse maturation represent a likely molecular pathomechanism of epilepsy and mental retardation in humans.
The enhancement of Cb-induced gephyrin (show GPHN Antibodies) clustering by GTP (show AK3 Antibodies)-TC10 (show RHOQ Antibodies) 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
Phosphorylation of gephyrin (show GPHN Antibodies) in hippocampal neurons by cyclin-dependent kinase (show CDK1 Antibodies) CDK5 (show CDK5 Antibodies) at Ser (show SIGLEC1 Antibodies)-270 is dependent on collybistin.
Data indicate that ARHGEF9 is likely to be responsible for syndromic X-linked mental retardation associated with epilepsy.
These results reveal that G(s) and G(q) signalings regulate hPEM-2 functions through PKA and c-Src (show SRC Antibodies) in Neuro-2a neuroblastoma (show ARHGEF16 Antibodies) cells, respectively.
major regulator of GABAergic postsynaptic gephyrin (show GPHN Antibodies) clustering
Study propose that the collybistin-gephyrin (show GPHN Antibodies) complex has an intimate role in the clustering of GABA(A)Rs containing the alpha2 subunit.
Here we identified residues critical for interaction with gephyrin (show GPHN Antibodies) in the linker region between the SH3 and the DH domains of collybistin.
Results uncover previously unexpected role for CB isoforms downstream of alpha2-containing GABAARs during neuron maturation in a Cdc42 (show CDC42 Antibodies) dependent mechanism.
Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin (show GPHN Antibodies) to plasma membrane phosphoinositides.
data show that collybistin co-clusters with gephyrin (show GPHN Antibodies) and GABA(A) Rs in synaptic puncta and is recruited to postsynaptic specializations early during synapse development; it co-localizes with GABA(A) Rs containing the alpha1, alpha2, or alpha3 subunits
The results of this study provided evidence that the formation of gephyrin (show GPHN Antibodies) scaffolds at inhibitory synapses requires an intact Cb II PH-domain but is Cdc42 (show CDC42 Antibodies)-independent.
The resolution crystal structure of the Cdc42 (show CDC42 Antibodies)-collybistin II complex reveals a novel conformation of the switch I region of Cdc42 (show CDC42 Antibodies), and biochemical data indicate that gephyrin (show GPHN Antibodies) negatively regulates collybistin activity.
Cb is essential for gephyrin (show GPHN Antibodies)-dependent clustering of a specific set of GABA(A) receptors, but not required for glycine receptor (show GLRB Antibodies) postsynaptic localization.
Data provide the first evidence that collybistin deficiency leads to significant changes of GABAergic inhibition, network excitability and synaptic plasticity in vivo.
The protein encoded by this gene is a Rho-like GTPase that switches between the active (GTP-bound) state and inactive (GDP-bound) state to regulate CDC42 and other genes. Defects in this gene are a cause of startle disease with epilepsy (STHEE), also known as hyperekplexia with epilepsy. Three transcript variants encoding different isoforms have been found for this gene.
Cdc42 guanine nucleotide exchange factor (GEF) 9
, Cdc42 guanine nucleotide exchange factor 9
, Cdc42 guanine exchange factor 9
, rho guanine nucleotide exchange factor 9-like
, PEM-2 homolog
, hPEM-2 collybistin
, rac/Cdc42 guanine nucleotide exchange factor 9
, rho guanine nucleotide exchange factor 9
, collybistin I