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Phosphorylation of Cdc5 regulates its accumulation

机译：Cdc5的磷酸化调节其积累

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Background Cdc5 (polo kinase/Plk1) is a highly conserved key regulator of the S. cerevisiae cell cycle from S-phase until cytokinesis. However, much of the regulatory mechanisms that govern Cdc5 remain to be determined. Cdc5 is phosphorylated on up to 10 sites during mitosis. In this study, we investigated the function of phosphorylation site T23, the only full consensus Cdk1 (Cdc28) phosphorylation site present. Findings Cdc5T23A introduces a degron that reduces its cellular amount to undetectable levels, which are nevertheless sufficient for normal cell proliferation. The degron acts in cis and is reversed by N-terminal GFP-tagging. Cdk1 kinase activity is required to maintain Cdc5 levels during G2. This, Cdk1 inhibited, Cdc5 degradation is APC/CCdh1 independent and requires new protein synthesis. Cdc5T23E is hyperactive, and reduces the levels of Cdc5 (in trans) and drastically reduces Clb2 levels. Conclusions Phosphorylation of Cdc5 by Cdk1 is required to maintain Cdc5 levels during G2. However, phosphorylation of T23 (probably by Cdk1) caps Cdc5 and other CLB2 cluster protein accumulation, preventing potential protein toxicity, which may arise from their overexpression or from APC/CCdh1 inactivation.
机译：背景Cdc5（polo激酶/ Plk1）是啤酒酵母细胞从S期到胞质分裂的高度保守的关键调节因子。但是，控制Cdc5的许多调节机制仍有待确定。在有丝分裂期间，Cdc5在多达10个位点被磷酸化。在这项研究中，我们调查了磷酸化位点T23的功能，这是目前唯一的完全共有的Cdk1（Cdc28）磷酸化位点。 Findings Cdc5 T23A 引入了一种德格隆，它将其细胞数量减少到无法检测的水平，但这足以正常细胞增殖。 degron以顺式作用，并被N端GFP标签逆转。 Cdk1激酶活性是维持G2期间Cdc5水平所必需的。这种Cdk1抑制的Cdc5降解是APC / C Cdh1 独立的，需要新的蛋白质合成。 Cdc5 T23E 具有高活性，可以降低Cdc5（反式）的水平，并可以大大降低Clb2的水平。结论Cdk1磷酸化Cdc5是维持G2期间Cdc5水平所必需的。但是，T23的磷酸化作用（可能是Cdk1作用）限制了Cdc5和其他CLB2簇蛋白的积累，防止了潜在的蛋白毒性，这可能是由于它们的过表达或APC / C Cdh1 失活引起的。

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