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Leucine-rich repeat and fibronectin type-III domain-containing protein 2 (LRFN2) is a type I transmembrane glycoprotein primarily expressed at synaptic sites and in the retina[2][4]. It contains leucine-rich repeats (LRR), immunoglobulin-like (Ig), and fibronectin type III (Fn3) domains in its extracellular region and a C-terminal PDZ-binding motif intracellularly[2]. LRFN2 acts as a synaptic adhesion molecule that modulates chemical synaptic transmission, regulates postsynaptic organization, promotes neurite outgrowth in hippocampal neurons, and influences the cell surface expression and trafficking of NMDA and AMPA receptor subunits[1][5]. It is implicated in clustering of synaptic receptors, affecting synaptic plasticity and function, and has known roles in the organization of postsynaptic signalplexes, particularly at excitatory synapses[1][4][2]. LRFN2 has been associated with neurodevelopmental and neuropsychiatric conditions such as autism spectrum disorder and epilepsy[1][6]. No drugs are currently known to target LRFN2 directly.
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