東京大学 · 生化学・遺伝学・分子生物学
Murata教授の研究室は、免疫系における抗原処理のメカニズムを解明するため、リボソームの一種であるプロテアソームの構造と機能に焦点を当てています。特に、胸腺上皮細胞に特異的に発現する新規サブユニットβ5tや、PA28γというプロテアソームアクセサリー因子の機能を解析しており、T細胞の選別や自己免疫のメカニズム解明に貢献しています。これらの研究は、がん免疫療法や自己免疫疾患の治療戦略の基盤を築くことを目指しています。
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Proteasomes are responsible for generating peptides presented by the class I major histocompatibility complex (MHC) molecules of the immune system. Here, we report the identification of a previously unrecognized catalytic subunit called beta5t. beta5t is expressed exclusively in cortical thymic epithelial cells, which are responsible for the positive selection of developing thymocytes. Although the chymotrypsin-like activity of proteasomes is considered to be important for the production of pept
The proteasome activator PA28 binds to both ends of the central catalytic machine, known as the 20 S proteasome, in opposite orientations to form the enzymatically active proteasome. The PA28 family is composed of three members designated alpha, beta, and gamma; PA28alpha and PA28beta form the heteropolymer mainly located in the cytoplasm, whereas PA28gamma forms a homopolymer that predominantly occurs in the nucleus. Available evidence indicates that the heteropolymer of PA28alpha and PA28beta
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