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RISS 인기검색어
- 검색키워드
- 저자 : Verpelli, Chiara (검색결과 2 건)
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M. Verpelli,D. Abriola 한국물리학회 2011 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.59 No.23
The evolution of Information Technology has made it possible to provide the Nuclear Data community with various flexible tools customized to respond to individual data queries, to provide visualization, and facilitate dissemination. In another effort to further these developments, the IAEA's Nuclear Data Section has developed a set of applications based on a relational database designed for nuclear structure and decay data. The tools presented in this work mainly use the nuclear structure and decay data obtained from ENSDF and the Nuclear Wallet cards. The present set of applications comprises an interactive Chart of Nuclides (LiveChart) not only presenting the Chart graphically, but also allowing the visualization of data patterns while changing filtering criteria, a web-based query application and a desktop version of the relational database giving support to expert users to customize their data-processing applications. Some examples of the three software tools are presented.
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Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD
Han, Kihoon,Kim, Myoung-Hwan,Seeburg, Daniel,Seo, Jinsoo,Verpelli, Chiara,Han, Seungnam,Chung, Hye Sun,Ko, Jaewon,Lee, Hyun Woo,Kim, Karam,Heo, Won Do,Meyer, Tobias,Kim, Hyun,Sala, Carlo,Choi, Se-Youn Public Library of Science 2009 PLoS biology Vol.7 No.9
<▼1><P>A two step mechanism was identified that regulates receptor endocytosis during the development of long-term depression (LTD), a long-lasting decrease in synaptic transmission.</P></▼1><▼2><P>Long-term depression (LTD) is a long-lasting activity-dependent decrease in synaptic strength. NMDA receptor (NMDAR)–dependent LTD, an extensively studied form of LTD, involves the endocytosis of AMPA receptors (AMPARs) via protein dephosphorylation, but the underlying mechanism has remained unclear. We show here that a regulated interaction of the endocytic adaptor RalBP1 with two synaptic proteins, the small GTPase RalA and the postsynaptic scaffolding protein PSD-95, controls NMDAR-dependent AMPAR endocytosis during LTD. NMDAR activation stimulates RalA, which binds and translocates widespread RalBP1 to synapses. In addition, NMDAR activation dephosphorylates RalBP1, promoting the interaction of RalBP1 with PSD-95. These two regulated interactions are required for NMDAR-dependent AMPAR endocytosis and LTD and are sufficient to induce AMPAR endocytosis in the absence of NMDAR activation. RalA in the basal state, however, maintains surface AMPARs. We propose that NMDAR activation brings RalBP1 close to PSD-95 to promote the interaction of RalBP1-associated endocytic proteins with PSD-95-associated AMPARs. This suggests that scaffolding proteins at specialized cellular junctions can switch their function from maintenance to endocytosis of interacting membrane proteins in a regulated manner.</P></▼2><▼3><P><B>Author Summary</B></P><P>Neurons adapt over time in order to dampen their response to prolonged or particularly strong stimuli. This process, termed long-term depression (LTD), results in a long-lasting decrease in the efficiency of synaptic transmission. One extensively studied form of LTD requires the activation of a specific class of receptors known as NMDA glutamate receptors (NMDARs). A key molecular event initiated by NMDA receptor activation is the stimulation of protein phosphatases. Another key event is internalization via endocytosis of synaptic AMPA glutamate receptors (AMPARs). However, the mechanism by which protein dephosphorylation is coupled to AMPAR endocytosis has remained unclear. Here, we help to define this mechanism. We show that endocytic proteins, including RalBP1, are widely distributed in neurons under normal conditions. Upon NMDAR activation, the small GTPase RalA becomes activated and binds to RalBP1, resulting in the translocation of RalBP1 and RalBP1-associated endocytic proteins to synapses. At the same time, RalBP1 becomes dephosphorylated, which promotes its binding to the postsynaptic scaffold protein PSD-95, a protein that itself associates with AMPARs. This concerted recruitment of endocytic proteins to the vicinity of AMPARs results in AMPAR endocytosis. On the basis of our data, we propose a model in which dual binding of RalBP1 to both RalA and PSD-95 following RalBP1 dephosphorylation is essential for NMDAR-dependent AMPAR endocytosis during LTD.</P></▼3>
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