Characterization of the new synaptic protein LAPSER1
Schmeißer, Michael Joachim
LicenseStandard (Fassung vom 01.10.2008)
Neuronal communication is known to be essential for learning and memory while on the cellular level, this communication happens via synapses. As memory formation has been shown to depend upon long lasting plastic changes of the molecular composition within the synapse, synaptic proteins being responsible for these changes are of special interest. This work is focused on the characterization of a newly identified postsynaptic protein called LAPSER1 that belongs to the "Fezzin" family of synaptic proteins. LAPSER1 is highly expressed in brain and localizes to the postsynaptic compartment interacting directly with the major postsynaptic scaffolding molecule ProSAP2/Shank3. It also cross-links spine morphology regulators of the SPAR family to the ProSAP/Shank platform via its conserved C-terminal Fez1 domain. In addition, LAPSER1 interacts with Wnt pathway member beta-Catenin at postsynaptic densities. Upon NMDA (N-methyl-D-aspartate) receptor activation, LAPSER1 rapidly shuttles to the nucleus in a complex with beta-Catenin and tightly regulates the nuclear localization of the latter by enhancing its nuclear export thus repressing beta-Catenin-mediated transcription. Given these results, the characterization of LAPSER1 and the description of its potential role in neurons add important knowledge which will further help to understand the molecular processes of postsynaptic plasticity and memory formation.
Original publicationJournal of Biological Chemistry, 284(42):29146-57, 2009
Subject HeadingsSynapse [GND]
Wnt proteins [MeSH]