Topic: CYFIP2

Cytoplasmic FMR1-interacting protein family contains two members, CYFIP1 and CYFIP2, evolutionarily conserved multifunctional proteins. Despite their high sequence homology, varied evidence indicates that CYFIP1 and CYFIP2 have distinct functions in vivo and are linked to different brain disorders. However, the underlying mechanisms remain largely unknown.We conducted reciprocal immunoprecipitation experiments to explore the underlying mechanisms using CYFIP1-2×Myc and CYFIP2-3×Flag knock-in mice. The results revealed that CYFIP1 and CYFIP2 are not significantly co-immunoprecipitated with each

CYFIP2, a component of the WAVE regulatory complex, plays a crucial role in regulating actin dynamics and synaptic function. Through genetic analysis of patients diagnosed with Early Infantile Epileptic Encephalopathy (EIEE), novel mutations in the CYFIP2 gene were identified. Functional studies revealed altered synaptic plasticity and neuronal excitability associated with these mutations. Furthermore, behavioral assays in animal models harboring CYFIP2 mutations demonstrated phenotypes consistent with epileptic encephalopathy. These findings underscore the significance of CYFIP2 in neuronal d

Recently, de novo CYFIP2 variants have been identified in individuals with neurodevelopmental disorders and epilepsy. Considerable progress has revealed CYFIP2’s role as a component of the WAVE regulatory complex controlling actin cytoskeleton dynamics in neuronal development and function. However, its molecular functions remain partially unresolved. In our previous study, we unexpectedly discovered RNA-binding proteins (RBPs) among the CYFIP2 interactome from the neonatal mouse forebrain, suggesting that CYFIP2 may have novel functions in RNA regulation potentially mediated by these RBPs. How