Structural study of FIP200, a scaffold protein of mammalian autophagy initiation complex

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K21593
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry; Physical pharmacy
• Research Institution: Microbial Chemistry Research Foundation
• Principal Investigator: SUZUKI Hironori 公益財団法人微生物化学研究会, 微生物化学研究所, 博士研究員 (20625694)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: X線結晶構造解析 / オートファジー

Outline of Final Research Achievements

A lot of proteins involved in autophagy are widely conserved in eukaryotes from budding yeast to humans. However, some proteins are unique factors to higher eukaryotes such as human. One of which is FIP200, a scaffold protein of mammalian autophagy initiation complex.
In this study, we first prepared to stable region to use biochemical analysis and crystallographic studies. Moreover, we crystallized and determined the structure of a part of FIP200. The C-terminal region of FIP200 formed a parallel coiled-coil dimer. This result indicates that the large protein FIP200 functioning as a scaffold protein assumes a parallel dimeric structure.

Free Research Field

構造生物学