Mutations affecting phosphorylation, ubiquitination and turnover of the ABC‐transporter Ste6
Mutations affecting phosphorylation, ubiquitination and turnover of the ABC‐transporter Ste6
复制标题
影响 ABC 转运蛋白 Ste6 磷酸化、泛素化和周转的突变
DOI：
10.1016/s0014-5793(02)03621-9
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发表时间：
2002
期刊：
影响因子：
3.5
通讯作者：
R. Kölling
中科院分区：
文献类型：
--
作者：
R. Kölling
在这份报告中，磷酸化的ABC转运蛋白Ste 6的泛素化和营业额的调节的作用进行了研究。我们证明，Ste 6是在体内磷酸化，这种磷酸化是依赖于一个酸性拉伸（'A盒'）的存在下，在先前显示的连接区是重要的泛素化和快速营业额的Ste 6。通过诱变，两个丝氨酸/苏氨酸残基被确定在A-box区域，是至关重要的泛素化和运输到酵母液泡。在突变体中，磷酸化和泛素化水平之间没有简单的相关性，这表明这两个事件可能不耦合。
In this report, the role of phosphorylation in the regulation of ubiquitination and turnover of the ABC-transporter Ste6 was investigated. We demonstrate that Ste6 is phosphorylated in vivo and that this phosphorylation is dependent on the presence of an acidic stretch (‘A-box’) in the linker region previously shown to be important for ubiquitination and fast turnover of Ste6. By mutagenesis, two serine/threonine residues were identified in the A-box region that are crucial for ubiquitination and trafficking to the yeast vacuole. In the mutants there was no simple correlation between phosphorylation and ubiquitination levels, suggesting that the two events may not be coupled.
影响因子：
56.9
作者：
ROGERS, S;WELLS, R;RECHSTEINER, M
通讯作者：
RECHSTEINER, M
影响因子：
--
作者：
J. Pringle;R. Preston;A. Adams;T. Stearns;D. Drubin;B. Haarer;E. Jones
通讯作者：
J. Pringle;R. Preston;A. Adams;T. Stearns;D. Drubin;B. Haarer;E. Jones