- EMDB-22631: PIKfyve/Fig4/Vac14 complex centered on Fig4 - map3 -
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基本情報
登録情報
データベース: EMDB / ID: EMD-22631
タイトル
PIKfyve/Fig4/Vac14 complex centered on Fig4 - map3
マップデータ
PIKfyve complex density map centered on Fig4
試料
複合体: PIKfyve/Fig4/Vac14 complex
タンパク質・ペプチド: Fig4 Sac homology model
キーワード
Lipid kinase / Lipid phosphatase / protein complex / LIPID BINDING PROTEIN
機能・相同性
機能・相同性情報
phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity / Synthesis of PIPs at the late endosome membrane / Synthesis of PIPs at the early endosome membrane / Synthesis of PIPs at the Golgi membrane / 加水分解酵素; エステル加水分解酵素; 1価のリン酸エステル加水分解酵素 / phosphatidylinositol dephosphorylation / phosphatidylinositol biosynthetic process / lipid droplet / late endosome membrane / early endosome membrane ...phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity / Synthesis of PIPs at the late endosome membrane / Synthesis of PIPs at the early endosome membrane / Synthesis of PIPs at the Golgi membrane / 加水分解酵素; エステル加水分解酵素; 1価のリン酸エステル加水分解酵素 / phosphatidylinositol dephosphorylation / phosphatidylinositol biosynthetic process / lipid droplet / late endosome membrane / early endosome membrane / endosome membrane / Golgi membrane / intracellular membrane-bounded organelle 類似検索 - 分子機能
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM131715
米国
引用
ジャーナル: Mol Cell / 年: 2020 タイトル: Insights into Lysosomal PI(3,5)P Homeostasis from a Structural-Biochemical Analysis of the PIKfyve Lipid Kinase Complex. 著者: Joshua A Lees / PeiQi Li / Nikit Kumar / Lois S Weisman / Karin M Reinisch / 要旨: The phosphoinositide PI(3,5)P, generated exclusively by the PIKfyve lipid kinase complex, is key for lysosomal biology. Here, we explore how PI(3,5)P levels within cells are regulated. We find the ...The phosphoinositide PI(3,5)P, generated exclusively by the PIKfyve lipid kinase complex, is key for lysosomal biology. Here, we explore how PI(3,5)P levels within cells are regulated. We find the PIKfyve complex comprises five copies of the scaffolding protein Vac14 and one copy each of the lipid kinase PIKfyve, generating PI(3,5)P from PI3P and the lipid phosphatase Fig4, reversing the reaction. Fig4 is active as a lipid phosphatase in the ternary complex, whereas PIKfyve within the complex cannot access membrane-incorporated phosphoinositides due to steric constraints. We find further that the phosphoinositide-directed activities of both PIKfyve and Fig4 are regulated by protein-directed activities within the complex. PIKfyve autophosphorylation represses its lipid kinase activity and stimulates Fig4 lipid phosphatase activity. Further, Fig4 is also a protein phosphatase acting on PIKfyve to stimulate its lipid kinase activity, explaining why catalytically active Fig4 is required for maximal PI(3,5)P production by PIKfyve in vivo.