To identify Nak-associated proteins, 0- to 12-hr-old embryos carrying UAS-Flag-nak and arm-GAL4 or tub-GAL4 were collected and lysed for Flag M2 precipitation. The
immunoprecipitates were resolved in SDS-PAGE for SYPRO Ruby staining. Distinct signals appearing in arm > Flag-nak and tub > Flag-nak but not controls were subjected for LC-MS/MS analysis. We thank J.A. Knoblich, T. Uemura, Y.N. Jan, M. Gonzalez-Gaitan, S.L. Schmid, T.D. Murphy, R.W. Carthew, H.J. Bellen, Bloomington Drosophila Stock Center, DGRC, Vienna Drosophila RNAi Center, and DSHB for providing reagents. Protein identification by mass spectrometry analysis was performed at the NRPGM Core Facilities for Proteomics Research funded by the Taiwan National Science Council (NSC96-3112-B-001-018). H.C.C. is supported by American Heart Association Scientist Talazoparib in vitro Development and American Cancer Society Research Scholar grants. C.T.-C. is supported by grants from National Science Council and Academia Sinica of Taiwan. “
“Activity-dependent changes in the
strength of excitatory synapses are thought to be key cellular mechanisms that contribute to the plasticity of neuronal networks underlying learning and memory. Two well-defined cellular models in mammals that Cell Cycle inhibitor measure changes in synaptic strength are long-term potentiation (LTP) and long-term depression (LTD) (Citri and Malenka, 2008, Collingridge et al., 2010 and Shepherd and Huganir, 2007). Like memories, they typically occur in two distinct phases:
an early phase that usually depends on modification of preexisting proteins, and a late phase that is more persistent and dependent on the synthesis of new proteins (Citri and Malenka, 2008, Costa-Mattioli et al., 2009, Richter and Klann, 2009 and Sutton and Schuman, 2006). While the importance of de novo protein synthesis in the long-term nature of both memory and its underlying first forms of synaptic plasticity has been known for a while, a major difficulty has been the identification of the locally translated proteins directly linked to changes in synaptic strength. At hippocampal CA1 synapses, several forms of plasticity that are dependent on protein synthesis have been described, including late-phase NMDA receptor (NMDAR)-dependent LTP and LTD (Citri and Malenka, 2008, Collingridge et al., 2010 and Klann and Dever, 2004), and a form of LTD (mGluR-LTD) that relies on the activation of group I metabotropic glutamate receptors, which consist of mGluR1 and mGluR5 (Huber et al., 2000 and Oliet et al., 1997). Activation of either mGluR1 or mGluR5 can induce LTD in the hippocampal CA1 area (Hou and Klann, 2004 and Volk et al., 2006).
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