Nuclear export mechanism of misfolded proteins

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K20998
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Cell biology; Functional biochemistry
• Research Institution: The University of Tokyo
• Principal Investigator: Hirayama Shoshiro 東京大学, 大学院薬学系研究科(薬学部), 助教 (80548280)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: ユビキチン / プロテアソーム / タンパク質品質管理 / 細胞内輸送

Outline of Final Research Achievements

In mammalian cells, it is known that the misfolded or the ubiquitinated proteins are sequestered into specific deposition sites in the cytoplasm not in the nucleus such as aggresome and ALIS. Formation of these cytoplasmic aggregates is considered to be cytoprotective. However, it is unknown why aggresome and ALIS form in the cytosol but not in the nucleus.
In this study, we found that the ubiquitinated proteins were exported from the nucleus and cytosol. Furthermore, we also showed that ubiquitin binding protein UBIN and its cofactor POST cooperatively export the ubiquitinated proteins in an exportin dependent manner.

Free Research Field

細胞生物学