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首页> 外文期刊>Journal of Molecular Biology >Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals.
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Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals.

机译：酵母和哺乳动物中TOR途径的氨基酸传感分支中成分的结构保守性。

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摘要

The highly conserved Rag family GTPases have a role in reporting amino acid availability to the TOR (target of rapamycin) signaling complex, which regulates cell growth and metabolism in response to environmental cues. The yeast Rag proteins Gtr1p and Gtr2p were shown in multiple independent studies to interact with the membrane-associated proteins Gse1p (Ego3p) and Gse2p (Ego1p). However, mammalian orthologs of Gse1p and Gse2p could not be identified. We determined the crystal structure of Gse1p and found it to match the fold of two mammalian proteins, MP1 (mitogen-activated protein kinase scaffold protein 1) and p14, which form a heterodimeric complex that had been assigned a scaffolding function in mitogen-activated protein kinase pathways. The significance of this structural similarity is validated by the recent identification of a physical and functional association between mammalian Rag proteins and MP1/p14. Together, these findings reveal that key components of the TOR signaling pathway are structurally conserved between yeast and mammals, despite divergence of sequence to a degree that thwarts detection through simple homology searches.
机译：高度保守的Rag家族GTPases在向TOR（雷帕霉素的靶标）信号转导复合物报告氨基酸可用性方面起作用，该信号复合物根据环境提示调节细胞生长和代谢。多项独立研究显示，酵母Rag蛋白Gtr1p和Gtr2p与膜相关蛋白Gse1p（Ego3p）和Gse2p（Ego1p）相互作用。但是，无法确定哺乳动物的Gse1p和Gse2p直系同源物。我们确定了Gse1p的晶体结构，发现它与两种哺乳动物蛋白MP1（促分裂原激活的蛋白激酶支架蛋白1）和p14的折叠相匹配，这两种蛋白形成了异二聚体复合物，该复合物在促分裂原激活蛋白中被赋予了支架功能激酶途径。最近鉴定出哺乳动物Rag蛋白与MP1 / p14之间的物理和功能联系，从而证实了这种结构相似性的重要性。总之，这些发现表明，尽管序列的差异在一定程度上阻碍了通过简单同源搜索的检测，但TOR信号通路的关键组成部分在酵母和哺乳动物之间在结构上是保守的。

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