7Q3D

Structure of the human CPLANE complex

7Q3D の概要

• エントリーDOI: 10.2210/pdb7q3d/pdb
• EMDBエントリー: 13789
• 分子名称: WD repeat-containing and planar cell polarity effector protein fritz homolog, Protein inturned, Protein fuzzy homolog (3 entities in total)
• 機能のキーワード: ciliogenesis, ciliopathies, longin, lipid binding, protein transport
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 243521.90

構造登録者

Langousis, G.,Cavadini, S.,Kempf, G.,Matthias, P. (登録日: 2021-10-27, 公開日: 2022-04-06, 最終更新日: 2024-07-17)

主引用文献

Langousis, G.,Cavadini, S.,Boegholm, N.,Lorentzen, E.,Kempf, G.,Matthias, P.
Structure of the ciliogenesis-associated CPLANE complex.
Sci Adv, 8:eabn0832-eabn0832, 2022

PubMed Abstract: Dysfunctional cilia cause pleiotropic human diseases termed ciliopathies. These hereditary maladies are often caused by defects in cilia assembly, a complex event that is regulated by the ciliogenesis and planar polarity effector (CPLANE) proteins Wdpcp, Inturned, and Fuzzy. CPLANE proteins are essential for building the cilium and are mutated in multiple ciliopathies, yet their structure and molecular functions remain elusive. Here, we show that mammalian CPLANE proteins comprise a bona fide complex and report the near-atomic resolution structures of the human Wdpcp-Inturned-Fuzzy complex and of the mouse Wdpcp-Inturned-Fuzzy complex bound to the small guanosine triphosphatase Rsg1. Notably, the crescent-shaped CPLANE complex binds phospholipids such as phosphatidylinositol 3-phosphate via multiple modules and a CPLANE ciliopathy mutant exhibits aberrant lipid binding. Our study provides critical structural and functional insights into an enigmatic ciliogenesis-associated complex as well as unexpected molecular rationales for ciliopathies.

PubMed: 35427153
DOI: 10.1126/sciadv.abn0832

実験手法

ELECTRON MICROSCOPY (3.35 Å)