Structural basis of phospholipid remodeling acyl-transferase LPCAT1

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K06967
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Osaka University (2017); Kyoto University (2015-2016)
• Principal Investigator: ARIYOSHI Mariko 大阪大学, 生命機能研究科, 特任助教(常勤) (80437243)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: リン脂質リモデリング / アシル転移酵素 / カルシウム結合モチーフ / 結晶構造

Outline of Final Research Achievements

Phospholipids are not only the major structural components of membrane lipid bilayers, but also essential determinants of membrane biophysical properties. In addition, phospholipid mediators are involved in crucial signal transduction pathways. Phospholipid remodeling is a fundamental cellular function to generate diverse phospholipids and maintain phospholipid homeostasis. Lpcat1 is one of the acyl-transferases involved in phospholipid remodeling. LPCAT1 contains two canonical EF-hand motifs along with the catalytic domain, and has been supposed that its catalytic activity is regulated in a calcium-dependent manner. We determined the crystal structure of the EF-hand domain of LPCAT1 in apo and calcium bound forms. The crystal structure has revealed its unique domain structure comprised of four EF-hand motifs. Combined with biochemical data, the structural data gain our understanding about calcium binding mode of the EF-hand motifs and its effect on substrate binding.

Free Research Field

構造生物学