[Abstract Title]. - Society for Neuroscience

evidence that the Nogo signaling system plays a role in controlling synaptic plasticity in the
brain and the complex process of transforming transiently stored new information into very long
term memories. Understanding the molecular underpinnings of the synaptic structural
rearrangements that carry lasting memories may help the development of better treatments for
memory dysfunction.
Disclosures: A. Karlen, None; T.E. Karlsson, None; A. Mattsson, None; K. Lundstomer,
None; K. Pernold, None; T. Pham, None; C.M. Backman, None; S.O. Ogren, None; A.F.
Hoffman, None; M.A. Sherling, None; C.R. Lupica, None; B.J. Hoffer, None; C. Spenger,
None; A. Josephson, None; S. Brene, None; L. Olson, None.
Poster
239. Structural Plasticity at Synapses I
Time: Sunday, November 16, 2008, 1:00 pm - 5:00 pm
Program#/Poster#: 239.23/E20
Topic: B.08.i. Structural plasticity
Support: NIH Grant AG031380
Title: Analysis of protein interaction “managers” and their system-wide connections:
universality and plasticity of synapse molecular organizations
Authors: *A. KURAKIN;
Pathology, BIDMC/Harvard Med. Sch., Boston, MA
Abstract: We have developed a suit of biochemical and computational techniques that allows
for the identification of interactors of PDZ, WW, SH3 and other signaling/scaffolding domains
on the scale of a whole proteome. Identification of interacting partners of a given target
domain/protein followed by clustering of identified interactors in the functional space of the
proteome provides a comprehensive overview of the functional connections of the target
domain/protein.
Analysis of proteome-wide functional associations of the PSD95 scaffold indicates that, in
addition to its well-recognized role in managing spatio-temporal dynamics of the post-synaptic
specialization, PSD95 may play an underappreciated role in establishing and maintaining cell
polarity. Two novel protein families found to interact with PSD95, membrane-associated
ubiquitin ligases and viral proteins, will be discussed in the context of the PSD95 biology.
Analysis of interactions of the CIN85/SETA/Ruk protein on the proteome-wide scale suggests
that different intercellular specialized junctions, including neuronal and immunological synapses
and adherens junctions, may represent functionally analogous molecular organizations built of