Identification of plasma membrane leucine receptor and elucidation of its link to mTOR signaling pathway

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By comparative quantitative proteomics using mass spectrometry, several candidates for the plasma membrane leucine receptor were identified. Functional analysis of these candidates revealed that one protein plays a role in mTORC1 pathway downstream of growth factor receptors and thereby regulates the activity of mTORC1 cooperatively with amino acids. We also developed a new analytical procedure of mass spectrometry suitable for integral membrane proteins by improving the sample preparation process and mass spectrometric measurement, because the detection and identification of integral membrane proteins were difficult in general. Additionally, to reveal the overall signaling events downstream of leucine receptor, we established a method for quantitative phosphoproteomics. The technical basis fundamentally important for the identification of leucine receptor has been established in this study.