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首页> 外文期刊>Molecular and Cellular Biology >The Abundance of Cell Cycle Regulatory Protein Cdc4p Is Controlled by Interactions between Its F Box and Skp1p
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The Abundance of Cell Cycle Regulatory Protein Cdc4p Is Controlled by Interactions between Its F Box and Skp1p

机译：细胞周期调节蛋白Cdc4p的丰度受其F框和Skp1p之间的相互作用控制。

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Posttranslational modification of a protein by ubiquitin usually results in rapid degradation of the ubiquitinated protein by the proteasome. The transfer of ubiquitin to substrate is a multistep process. Cdc4p is a component of a ubiquitin ligase that tethers the ubiquitin-conjugating enzyme Cdc34p to its substrates. Among the domains of Cdc4p that are crucial for function are the F-box, which links Cdc4p to Cdc53p through Skp1p, and the WD-40 repeats, which are required for binding the substrate for Cdc34p. In addition to Cdc4p, other F-box proteins, including Grr1p and Met30p, may similarly act together with Cdc53p and Skp1p to function as ubiquitin ligase complexes. Because the relative abundance of these complexes, known collectively as SCFs, is important for cell viability, we have sought evidence of mechanisms that modulate F-box protein regulation. Here we demonstrate that the abundance of Cdc4p is subject to control by a peptide segment that we term the R-motif (for “reduced abundance”). Furthermore, we show that binding of Skp1p to the F-box of Cdc4p inhibits R-motif-dependent degradation of Cdc4p. These results suggest a general model for control of SCF activities.
机译：泛素对蛋白质的翻译后修饰通常会导致蛋白酶体对泛素化蛋白质的快速降解。泛素向底物的转移是一个多步过程。 Cdc4p是泛素连接酶的一个组成部分，它将泛素结合酶Cdc34p束缚在其底物上。对功能至关重要的Cdc4p区域是F-box，它通过Skp1p将Cdc4p连接到Cdc53p，而WD-40重复序列是绑定Cdc34p底物所必需的。除了Cdc4p，其他的F-box蛋白，包括Grr1p和Met30p，也可以类似地与Cdc53p和Skp1p共同发挥泛素连接酶复合体的功能。因为这些复合物的相对丰度（统称为SCF）对于细胞生存力很重要，所以我们寻求了调节F-box蛋白调控机制的证据。在这里，我们证明Cdc4p的丰度受称为R-基序的肽段控制（“减少的丰度”）。此外，我们显示，Skp1p与Cdc4p的F-box结合会抑制Cdc4p的R-基序依赖性降解。这些结果提出了控制SCF活动的通用模型。

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