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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains
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Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains

机译：通过荧光各向异性定量ERK2蛋白相互作用：PEA-15通过阻断DEJL域的结合来抑制ERK2

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摘要

While mitogen-activated protein kinase signaling pathways constitute highly regulated networks of protein-protein interactions, little quantitative information for these interactions is available. Here we highlight recent fluorescence anisotropy binding studies that focus on the interactions of ERK1 and ERY2 with PEA-15 (antiapoptotic phosphoprotein enriched in astrocytes-15 kDa), a small protein that sequesters ERK2 in the cytoplasm. The regulation of ERK2 by PEA-15 is appraised in the light of a simple equilibrium-binding model for reversible ERK2 nucleoplasmic-cytoplasmic shuttling, which elaborates on the theory of Burack and Shaw (J. Biol. Chem. 280, 3832-3837; 2005). Also highlighted is the recent observation that the peptide N-QKGKPRDLELPLSPSL-C, derived from the docking site for ERK/JNK and LEL (DEJL) in Elk- 1, displaces PEA- 15 from ERK2. It is proposed that the C-terminus of PEA-15 ((LXLXXXXKK129)-L-121) is a reverse DEJL domain [which has a general consensus of R/K Phi(A)-X-3/4-Phi(B), where Phi A and Phi B are hydrophobic residues (Leu, Ile, or Val)], which mediates one arm of a bidentate PEA-15 interaction with ERK2, The notion that PEA-15 is a potent inhibitor of many ERK2-mediated phosphorylations, by virtue of its ability to block ERK2-DEJL domain interactions, is proposed. (c) 2005 Elsevier B.V. All rights reserved.
机译：尽管有丝分裂原激活的蛋白激酶信号转导通路构成了蛋白质-蛋白质相互作用的高度调控的网络，但这些相互作用的定量信息很少。在这里，我们重点介绍了最近的荧光各向异性结合研究，其重点是ERK1和ERY2与PEA-15（富含星形胶质细胞15 kDa的抗凋亡磷蛋白）的相互作用，PEA-15是一种在细胞质中隔离ERK2的小蛋白。根据可逆ERK2核质-胞质穿梭的简单平衡结合模型评估了PEA-15对ERK2的调节，该模型阐述了Burack和Shaw（J. Biol。Chem。280，3832-3837; 2005年）。还强调了最近的观察结果，即衍生自Elk-1中ERK / JNK和LEL（DEJL）对接位点的肽N-QKGKPRDLELPLSPSL-C取代了ERK2的PEA-15。有人提出PEA-15（（LXLXXXXKK129）-L-121）的C端是DEJL反向结构域[其普遍共识是R / K Phi（A）-X-3 / 4-Phi（B ），其中Phi A和Phi B是疏水性残基（Leu，Ile或Val），它介导双齿PEA-15与ERK2相互作用的一个臂，PEA-15是许多ERK2介导的有效抑制剂由于其阻断ERK2-DEJL结构域相互作用的能力，提出了磷酸化。 （c）2005 Elsevier B.V.保留所有权利。

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