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De novo, heterozygous, loss-of-function mutations in SYNGAP1 cause a syndromic form of intellectual disability.
This is the first description of a special electroencephalogram phenomenon (normalization with eye opening) in association with SYNGAP1 mutations.
Syngap transgenic mice exhibited alterations in long-term depression and dendritic spine morphology.
Phosphorylation of synaptic GTPase-activating protein (zeige RASA1 Proteine) (synGAP) by Ca2+/calmodulin-dependent protein kinase II (CaMKII) and cyclin-dependent kinase 5 (CDK5 (zeige CDK5 Proteine)) alters the ratio of its GAP activity toward Ras and Rap (zeige LRPAP1 Proteine) GTPases.
Reduced cognition in mutant Syngap1 transgenic mice is caused by isolated damage to developing forebrain neurons.
De novo CHD2 and SYNGAP1 mutations are new causes of epileptic encephalopathies, accounting for 1.2% and 1% of cases, respectively.
De novo missense mutations, p.R579X, and possibly all the other truncating mutations in SYNGAP1 result in a loss of its function, causing intellectual disability, autism, and a specific form of epilepsy.
SYNGAP1 is a brain-specific protein (zeige TPPP3 Proteine) that interacts with key components of the proteins involved in experience-dependent changes in glutamate (zeige GRIN1 Proteine) synapses involved in learning.
We provide evidence that truncating mutations in SYNGAP1 are common in nonsyndromic intellectual disability and can be also associated with autism.
The C2 domain of SynGAP is essential for stimulation of the Rap (zeige LRPAP1 Proteine) GTPase (zeige RACGAP1 Proteine) reaction.
The authors present evidence that synGAP-alpha1 regulates the composition of the postsynaptic density by restricting binding to the PDZ domains of PSD-95 (zeige DLG4 Proteine).
Study found that Syngap1 mutations associated with developmental brain disorders disrupt a critical period of neuronal growth, maturation, and dynamics of dendritic structures known to influence de novo assembly of developing cortical circuits
inactivation of a single copy of syngap1 induced widespread early functional maturation of excitatory connections in the mouse neocortex
These data demonstrate that SynGAP protein acts as a critical developmental repressor of neural excitability that promotes the development of life-long cognitive abilities.
This study demonstrated the functional significance of SynGAP1 signaling in the adult brain by capturing several changes that are dependent on NMDAR (zeige GRIN1 Proteine) and hippocampal integrity.
Overexpression of SynGAP alpha1 versus alpha2 C-termini-containing proteins in hippocampal neurons has opposing effects on synaptic strength, decreasing and increasing miniature excitatory synaptic currents amplitude/frequency, respectively.
SynGAP is an important regulator of the release of the neuropeptide calcitonin gene-related peptide (zeige CALCA Proteine) from primary sensory neurons and can modulate capsaicin-induced hypernociception.
Data show that deletion of SynGAP is associated with notable behavioral as well as morphological phenotypes indicative of hippocampal dysfunction.
The GAP activity of synGAP and its association with PSD-95 (zeige DLG4 Proteine) are important for normal regulation of spine and synapse formation in hippocampal neurons.
The protein encoded by this gene is a major component of the postsynaptic density (PSD), a group of proteins found associated with NMDA receptors at synapses. The encoded protein is phosphorylated by calmodulin-dependent protein kinase II and dephosphorylated by NMDA receptor activation. Defects in this gene are a cause of mental retardation autosomal dominant type 5 (MRD5).
synaptic Ras GTPase activating protein 1
, neuronal RasGAP
, p135 SynGAP
, ras GTPase-activating protein SynGAP
, ras/Rap GTPase-activating protein SynGAP
, synaptic Ras GTPase-activating protein 1
, synaptic Ras-GAP 1
, Ras GTPase-activating protein SynGAP
, synaptic Ras GTPase activating protein 1 homolog
, synaptic Ras GTPase activating protein, 135kDa