Neuroscience

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SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains for SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123 among other sites (2,3). Phosphorylation of SynGAP results in stimulation of GTPase activity of Ras, and PSD95 dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development since mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced LTP and perform poorly in spatial memory tasks (6).

1. Kim, J.H. et al. (1998) Neuron 20, 683-91.
2. Oh, J.S. et al. (2004) J Biol Chem 279, 17980-8.
3. Krapivinsky, G. et al. (2004) Neuron 43, 563-74.
4. Song, B. et al. (2004) Brain Res 1005, 44-50.
5. Komiyama, N.H. et al. (2002) J Neurosci 22, 9721-32.
6. Kim, J.H. et al. (2003) J Neurosci 23, 1119-24.

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SynGAP Antibody

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