TY - CONF
T1 - Comparative Bioinformatics Studies Of Mammalian and Insect Postsynaptic Density Complexes and Interaction Networks
AU - Zografos, Lysimachos A.
AU - Pocklington, Andrew
AU - Grant, Seth G. N.
AU - Armstrong, Douglas
N1 - Poster at International Symposium on Integrative Bioinformatics
PY - 2010
Y1 - 2010
N2 - The postsynaptic density (PSD) is a multi-protein complex, consisting of over 1000 proteins, which underlies molecular computation in the brain (Collins et al., 2006). We have previously isolated and analysed proteomics datasets from molecular sub-complexes of the mammalian PSD. The two most recent approaches yielded the NMDA receptor complex or MAGUK-associated signalling complex (NRC/MASC) (Husi et al., 2000; Collins et al., 2006; Pocklington et al., 2006) and the PSD-95 complex (Fernandez et al., 2009). Our previous comparative proteomics and interactomics approaches (Emes et al., 2008; Zografos et al., 2009) showed that most types of PSD proteins were present in the early Metazoan synapse and that the changes in signalling complexity, resulting from gene family duplication and diversification, were predominantly added on specific structural modules of the protein interaction network (PIN). However, wanting to elucidate the lineage specific differences or similarities in the organization of PSD complexes, we decided to directly compare complexes of the mouse (mPSD) and fruit fly's (D. melanogaster) PSD (fPSD). In this poster we will present the results of the first fPSD purification using tagged protein trap lines (Ryder et al., 2007) as well as a comparison with the mPSD by applying a comparative interactomics workflow that uses network motifs (Milo et al., 2002) and graphlets (Przulj, 2006), in combination with molecular function and biological process annotation, to compare protein interaction networks and convergence or divergence in the organisation of different molecular families within the network's topology.
AB - The postsynaptic density (PSD) is a multi-protein complex, consisting of over 1000 proteins, which underlies molecular computation in the brain (Collins et al., 2006). We have previously isolated and analysed proteomics datasets from molecular sub-complexes of the mammalian PSD. The two most recent approaches yielded the NMDA receptor complex or MAGUK-associated signalling complex (NRC/MASC) (Husi et al., 2000; Collins et al., 2006; Pocklington et al., 2006) and the PSD-95 complex (Fernandez et al., 2009). Our previous comparative proteomics and interactomics approaches (Emes et al., 2008; Zografos et al., 2009) showed that most types of PSD proteins were present in the early Metazoan synapse and that the changes in signalling complexity, resulting from gene family duplication and diversification, were predominantly added on specific structural modules of the protein interaction network (PIN). However, wanting to elucidate the lineage specific differences or similarities in the organization of PSD complexes, we decided to directly compare complexes of the mouse (mPSD) and fruit fly's (D. melanogaster) PSD (fPSD). In this poster we will present the results of the first fPSD purification using tagged protein trap lines (Ryder et al., 2007) as well as a comparison with the mPSD by applying a comparative interactomics workflow that uses network motifs (Milo et al., 2002) and graphlets (Przulj, 2006), in combination with molecular function and biological process annotation, to compare protein interaction networks and convergence or divergence in the organisation of different molecular families within the network's topology.
M3 - Poster
ER -