3I2W

Crystal structure of EFC/F-BAR domain of Drosophila Syndapin/PACSIN

3I2W の概要

• エントリーDOI: 10.2210/pdb3i2w/pdb
• 分子名称: Syndapin, GLYCEROL, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: efc, fbar, sh3 domain, endocytosis
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69347.19

構造登録者

Edeling, M.A.,Owen, D.J.,Traub, L.M. (登録日: 2009-06-29, 公開日: 2010-03-02, 最終更新日: 2024-11-13)

主引用文献

Edeling, M.A.,Sanker, S.,Shima, T.,Umasankar, P.K.,Honing, S.,Kim, H.Y.,Davidson, L.A.,Watkins, S.C.,Tsang, M.,Owen, D.J.,Traub, L.M.
Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development.
Plos One, 4:e8150-e8150, 2009

PubMed Abstract: PACSIN/Syndapin proteins are membrane-active scaffolds that participate in endocytosis. The structure of the Drosophila Syndapin N-terminal EFC domain reveals a crescent shaped antiparallel dimer with a high affinity for phosphoinositides and a unique membrane-inserting prong upon the concave surface. Combined structural, biochemical and reverse genetic approaches in zebrafish define an important role for Syndapin orthologue, Pacsin3, in the early formation of the notochord during embryonic development. In pacsin3-morphant embryos, midline convergence of notochord precursors is defective as axial mesodermal cells fail to polarize, migrate and differentiate properly. The pacsin3 morphant phenotype of a stunted body axis and contorted trunk is rescued by ectopic expression of Drosophila Syndapin, and depends critically on both the prong that protrudes from the surface of the bowed Syndapin EFC domain and the ability of the antiparallel dimer to bind tightly to phosphoinositides. Our data confirm linkage between directional migration, endocytosis and cell specification during embryonic morphogenesis and highlight a key role for Pacsin3 in this coupling in the notochord.

PubMed: 19997509
DOI: 10.1371/journal.pone.0008150

実験手法

X-RAY DIFFRACTION (2.67 Å)