Structural basis of LAMP2 aimed to modulate intracellular trafficking of lysosome

2016 Fiscal Year Final Research Report

• Project/Area Number: 25463072
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Surgical dentistry
• Research Institution: Tokyo Medical and Dental University
• Principal Investigator: Miki Yokoyama 東京医科歯科大学, 大学院医歯学総合研究科, 准教授 (70191533)
• Co-Investigator(Renkei-kenkyūsha): SAKAMOTO Kensaku 独立行政法人理化学研究所, 拡張型遺伝暗号システム研究, チームリーダー (50240685) ; SHIROUZU Mikako 独立行政法人理化学研究所, 生命分子システム基盤研究領域, 上級研究員 (70280732)
• Research Collaborator: TERASAWA Kazue
• Project Period (FY): 2013-04-01 – 2017-03-31
• Keywords: リソソーム / LAMP-1 / LAMP-2 / アセンブリ

Outline of Final Research Achievements

Lysosomes play a central role in the intracellular degradation. Lysosomes are also involved in the degradation of bone-matrix after fusion of lysosomes with plasma membranes. Lysosome-associated membrane proteins 1 and 2 (LAMP-1/2) are the most abundant protein components of lysosome membranes and suggested to be involved in the intracellular transport of lysosomes. However, the structural aspects of LAMPs have not been elucidated. In the present study, we demonstrated that (1) the subdomains of LAMP-1 and LAMP-2 adopt the unique β-prism fold, (2) the assembly modes of LAMP-1 and LAMP-2 are different.

Free Research Field

口腔生化学