Beta-arrestin multimers: does a crowd help or hinder function?
Beta-arrestin multimers: does a crowd help or hinder function?
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DOI：
10.1042/bj20081009
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发表时间：
2008-07-01
期刊：
影响因子：
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通讯作者：
DeFea, Kathryn Anne
中科院分区：
文献类型：
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作者：
DeFea, Kathryn Anne
在这一期的《生化杂志》上，Xu等人描述了他们如何使用点肽阵列来识别β -arrestin-2中的一个独特序列，该序列是多聚化和ERK1/2（细胞外信号相关激酶1/2）支架所必需的。他们提供的证据表明，二聚体可能不仅仅是β -抑制素的“储存形式”，不能与受体相互作用，而是可能增加g蛋白偶联受体信号传导的特异性。他们发现，β -拘捕素-2二聚化界面内的关键带电残基阻断了与ERK1/2的结合以及随后β(2)-肾上腺素能受体对ERK1/2的激活，而内化则不受影响。他们认为，自我关联可能是一种保护β -抑制蛋白支架位点免受特定结合伙伴影响的手段，从而防止关键信号通路的构成性激活。这些研究增强了我们对-抑制素如何作为多种途径的支架来响应不同信号的理解。
In this issue of the Biochemical Journal, Xu et al. describe how they use a spot peptide array to identify a unique sequence within beta-arrestin-2 that is required for both multimerization and ERK1/2 (extracellular-signal-related kinase 1/2) scaffolding. They provide evidence that dimers may serve as more than just 'storage forms' of beta-arrestins, incapable of interacting with receptors but, rather, perhaps, adding to the specificity of G-protein-coupled-receptor signalling. They show that key charged residues within this dimerization interface of beta-arrestin-2 block association with ERK1/2 and subsequent activation of ERK1/2 by beta(2)-adrenergic receptors, while internalization is unaffected. They suggest that self-association may serve as a means of sheltering scaffolding sites on beta-arrestins from specific binding partners to prevent constitutive activation of key signalling pathways. These studies enhance our understanding of how beta-arrestins can juggle their roles as scaffolds of multiple pathways in response to diverse signals.