Missorting of the Dendritic Cell Adhesion Molecule Telencephalin in Presenilin-Deficient Neurons

摘要: Presenilin deficiency abrogates γ-secretase cleavage, thereby preventing the release of amyloid peptide from β-clipped APP fragment or notch intracellular domain. The presenilins are therefore implicated in such diverse processes as neurodegeneration Alzheimer’s disease and regulation Notch signaling. question remains whether other type I transmembrane proteins pathways subject to presenilin-mediated proteolysis. While two aspartate residues presenilin likely essential for a functional complex, highly conserved carboxyterminal tail also appears be important function. Therefore we screened double hybrid library with short 1 bait. We identified protein that belongs family intercellular cell adhesion molecules, telencephalin. Telencephalin is exclusively expressed neurons telencephalic region, where it abundantly at somatodendritic plasmamembrane. Functionally, telencephalin is, like notch, involved neurite outgrowth. Interestingly, long-term potentiation. confirmed 1/telencephalin interaction using independent approaches. Finally, evidence physiological relevance this comes observation becomes mislocalized differentiated hippocampal neurons. Further research into may shed some light on way influences processing proteins, Notch.