[Abstract Title]. - Society for Neuroscience

Time: Sunday, November 16, 2008, 1:00 pm - 5:00 pm
Program#/Poster#: 239.5/E2
Topic: B.08.i. Structural plasticity
Title: “Fezzin” family member LAPSER1 takes part in synapto-nuclear translocation in
hippocampal neurons
Authors: *M. SCHMEISSER, A. M. GRABRUCKER, T. M. BOECKERS;
Inst. of Anat., Ulm Univ., Ulm, Germany
Abstract: The postsynaptic density (PSD), an electron dense structure underneath the
postsynaptic membrane of excitatory synapses in the central nervous system, forms a protein
platform composed of various scaffolding molecules, cytoskeletal elements and members of
neuronal signaling cascades. Recently, we have identified a novel postsynaptic scaffolding
molecule called LAPSER1 which belongs to the “Fezzin” familiy of PSD proteins and interacts
with the PDZ domain of ProSAP/Shank. By in-vitro and in-vivo analysis, we identified a PSD
protein complex that includes LAPSER1 and two of its interaction partners: spine-morphology
regulator SPAR1 and Wnt-pathway member beta-Catenin. Interestingly, LAPSER1 and beta-
Catenin translocate into the nucleus selectively upon NMDA application while SPAR1 stays at
the synapse.
Taken together, our findings show that “Fezzin” family member LAPSER1 has diverse functions
within the neuron. It creates a scaffold within the PSD by homo- and heteromeric interaction
with other Fezzin family members and might serve as an activity-dependent transport molecule
to the nucleus.
Disclosures: M. Schmeisser , None; A.M. Grabrucker, None; T.M. Boeckers, None.
Poster
239. Structural Plasticity at Synapses I
Time: Sunday, November 16, 2008, 1:00 pm - 5:00 pm
Program#/Poster#: 239.6/E3
Topic: B.08.i. Structural plasticity
Support: German Isreali Foundation (827/04)
Deutsche Forschungsgemeinschaft (DE 551/8-1)