- Peptide (C)REKGR(S)VASEYFLE, corresponding to amino acid residues 67-80 of human CACNG7 (Accession P62955). 1st extracellular loop.
- Rat and mouse brain lysates (1:1000-1:5000).
- Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain lysates:1,2. Anti-CACNG7 (extracellular) Antibody (#ACC-109), (1:1000).
3,4. Anti-CACNG7 (extracellular) Antibody, preincubated with CACNG7 (extracellular) Blocking Peptide (#BLP-CC109).
Transmembrane AMPA receptor regulatory proteins (TARPs) serve as auxiliary subunits of AMPA receptors and regulate functional aspects of these receptors such as: fast excitatory synaptic transmission, surface trafficking, synaptic clustering and glutamate affinity. Generally, TARPs are responsible for regulating expression, channel properties and localization of AMPA receptors in the brain1.
TARPs are non-pore-forming integral membrane proteins with four transmembrane domains that are widely expressed in the CNS. TARP family is divided in two: Type I and type II. Type I TARPs include two calcium channel γ subunits: γ5 and γ7, also known as Cacng5 and Cacng7, respectively.They do not traffic AMPAR, they only modulate existing AMPAR channel function2.
CaVγ7 (Transmembrane AMPA Receptor Regulatory Protein Isoform γ7) is highly expressed in Purkinje cells of the cerebellum and in glomerular synapses in the granule cell layer of the cerebellum and significantly enhances glutamate-evoked currents and modulates gating of AMPARs. CaVγ7 appears to derive from cerebellar Golgi cells2,3.
CaVγ7 shows the largest sequence divergence compared to other TARP members. Its structure demonstrates a short C-terminus with an absence of the TTPV motif that is critical in the binding of TARP-associated AMPARs to PSD-95 and in clustering at the synapse3.
Several recent studies have suggested that CaVγ7 has the ability to associate with extrasynaptic calcium-permeable AMPA receptors and plays an important role in regulating the presence of neuronal calcium-permeable AMPA receptors at synapses3. In addition, transfection of TARP CaVγ7 causes AMPA receptors to resensitize upon continued glutamate application3.