SHISA9 (also known as CKAMP44) is a brain-specific, type-I transmembrane protein that modulates AMPA receptor kinetics and synaptic plasticity . Antibodies targeting SHISA9 enable researchers to investigate its interactions, expression patterns, and functional roles in neuronal signaling.
SHISA9 binds PDZ domain-containing proteins via its C-terminal EVTV motif, including:
PSD95/PSD93: Validated via co-immunoprecipitation (co-IP) in HEK293T cells and native brain tissue .
GRIP1, PICK1, Lin7b: Confirmed in yeast two-hybrid and co-IP assays .
Disruption of these interactions (e.g., using TAT-Shisa9 mimetic peptides) accelerates AMPA receptor deactivation and alters synaptic short-term plasticity .
SHISA9 slows AMPA receptor desensitization and recovery kinetics, influencing paired-pulse facilitation in hippocampal neurons .
Blocking SHISA9-PSD95 interactions narrows hippocampal network oscillation frequencies, suggesting a role in synchronizing neuronal activity .
Western Blot: Detects a single band at ~68 kDa in rat brain lysates .
Immunohistochemistry: Localizes SHISA9 to postsynaptic densities in human and mouse brain sections .
Cross-Reactivity: No cross-reactivity with other GLIPR family proteins .
SHISA9 stabilizes AMPA receptors at synapses by anchoring them to PSD95 scaffolds .
Its C-terminal interactions are critical for tuning receptor kinetics and synaptic plasticity .
Antibody-blocking experiments reveal SHISA9’s role in maintaining hippocampal network oscillations .