NAIST 奈良先端科学技術大学院大学 バイオサイエンス領域



細胞シグナル研究室助教、建部 恒博士が第15回梅園賞を受賞しました。

梅園賞は、梅園基金の設立趣旨に沿って、熱気溢れる時期にバイオサイエンス研究に精進し、バイオサイエンス研究科において優れた研究成果(論文発表)をあげた本学の助教あるいはポスドク研究員の1 名を顕彰するものです。過去において助教あるいはポスドクとして本学に在籍していた方も選考の対象としてします。対象者が研究の推進に中心的な役割を果たしたと認められる発表論文(2016年6月1日〜2018年5月31日の期間に査読付き国際学術誌に発表されたもの)の学術的価値とオリジナリティの高さに審査の重点が置かれています。受賞者には表彰状と目録が授与されました。

第15回梅園賞受賞者 建部 恒博士のコメント



Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit

Dr. Hisashi Tatebe
(Assistant Professor, Cell Signaling, Division of Biological Science, NAIST)
Target Of Rapamycin (TOR) kinase is an evolutionarily conserved protein kinase that forms structurally and functionally distinct protein complexes TOR complex 1 (TORC1) and TOR complex 2 (TORC2), of which only TORC1 is rapamycin sensitive. In mammals, rapamycin-insensitive TORC2 transmits growth factor signals by phosphorylating and activating a subset of the AGC-family protein kinases such as Akt. Whereas hyperactivation of TORC2 is often associated with cancer development, no TORC2 specific inhibitor has been available to date.

The fission yeast Schizosaccharomyces pombe is a genetically tractable eukaryotic model organism that has been contributing to variety of biological studies over the last several decades. Here, by analyzing fission yeast TORC2 signaling in detail, we revealed that the Sin1 subunit of TORC2 plays a key role in recognition of the TORC2 substrate kinases. While fission yeast Sin1 is dispensable for the assembly and intrinsic catalytic activity of TORC2, Conserved Region In the Middle (CRIM) of Sin1 forms an individual domain that directly binds the TORC2 substrate kinases. Solution structure analysis indicated that Sin1CRIM is a ubiquitin-like domain, of which a characteristic acidic loop is essential for binding the TORC2 substrate kinases. In the fission yeast sin1 null mutant, Sin1CRIM fused with another TORC2 subunit is sufficient to restore phosphorylation of the substrate kinase Gad8 by TORC2. The substrate recognition function is conserved in human Sin1CRIM; thus, Sin1CRIM may serve as a pharmaceutical target to suppress TORC2 hyperactivation.



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