首页> 外文会议>American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics >REGULATION OF PROTEIN PHOSPHORYLATION AT THE POSTSYNAPTIC DENSITY- GLOBAL ANALYSIS TARGETING SPECIFIC KINASE AND PHOSPHATASE ACTIVITIES
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REGULATION OF PROTEIN PHOSPHORYLATION AT THE POSTSYNAPTIC DENSITY- GLOBAL ANALYSIS TARGETING SPECIFIC KINASE AND PHOSPHATASE ACTIVITIES

机译:在突触后密度 - 全局分析靶向靶向特异性激酶和磷酸酶活性的调节

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1. Dephosphorylation of CaMKII by endogenous phosphatase activity, as well as the effect of a peptide inhibitor of CaMKII, on phosphorylation are residuespecific. 2. Activation of CaMKII correlates with phosphorylation of residues on several scaffold proteins including Shank1, Shank 3, Densin 180, PSD-95 as well as of conserved serine residues near the C-terminals of SAPAP1, SAPAP2 and SAPAP3. Involvement of CaMKII in the phosphorylation of PSD scaffold proteins suggests a role in activity-induced re-organization of the PSD. 3. The effectiveness of phosphorylation by the Ca2+/calmodulin-associated versus autonomous forms of CaMKII was different for different sites. Most notably, autonomous activity was more effective in the phosphorylation of three residues on SynGAP. 4. Patterns of phosphorylation of CaMKII and of other core proteins at the PSD may be able to reflect temporal patterns of postsynaptic Ca2+.
机译:1.通过内源性磷酸酶活性去磷酸化CAMKII,以及CAMKII的肽抑制剂对磷酸化的影响是残留的。 2. Camkii的激活与包括SapaP1,SapaP2和SaPaP3附近的若干支架蛋白质上的几个支架蛋白质上的残基磷酸化与残留物上的残基磷酸化相关。 Camkii参与PSD支架蛋白质磷酸化表明在活性诱导的PSD重新组织中作用。 3.不同部位的Ca2 + /钙调蛋白相关的Ca2 + /钙调蛋白相关的钙化与自主形式的磷酸化的有效性不同。最值得注意的是,自主活性在Syngap上的三个残基的磷酸化方面更有效。 4. CAMKII的磷酸化和PSD中的其他核心蛋白的模式可能能够反射突触后CA2 +的时间模式。

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