Role of Rif in dynamics of nuclear membrane protein emerin

2015 Fiscal Year Final Research Report

• Project/Area Number: 25460367
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: General medical chemistry
• Research Institution: Kobe University
• Principal Investigator: Nishita Michiru 神戸大学, 医学(系)研究科(研究院), 准教授 (30379359)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: Rhoファミリー / 核膜 / ユビキチン化

Outline of Final Research Achievements

Although the shape of the cell nucleus changes depending on physiological and pathological conditions, its underlying mechanisms remain unclear. We have found that inactive form of Rif, an intracellular protein involved in filopodia formation, induces degradation of the nuclear membrane protein, emerin, and nuclear deformation. In this study, we studied the mechanism of Rif-mediated emerin degradation and its role in pathological conditions. Our results suggest that inactive form of Rif itself is ubiquitinated and degraded, leading to degradation of emerin. We have also found that active form of Rif can suppress mislocalization and degradation of emerin, associated with Hutchinson-Gilford progeria syndrome. We have further shown that Rif is involved in growth and invasion of human lung adenocarcinoma cells.

Free Research Field

細胞生物学