9UHD

Structure of FAM92A BAR domain

9UHD の概要

• エントリーDOI: 10.2210/pdb9uhd/pdb
• 分子名称: CBY1-interacting BAR domain-containing protein 1 (2 entities in total)
• 機能のキーワード: protein binding, lipid binding protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25232.56

構造登録者

Xu, X.,Ren, J.,Li, J. (登録日: 2025-04-14, 公開日: 2025-07-16)

主引用文献

Xu, X.,Ren, J.,Li, J.
Dimerization of the BAR domain-containing protein FAM92A modulates lipid binding and interaction with CBY1.
J.Biol.Chem., 301:110346-110346, 2025

PubMed Abstract: BAR (Bin/Amphiphysin/Rvs) domain proteins drive membrane remodeling critical for cellular processes like ciliogenesis and organelle morphology. FAM92A (family with sequence similarity 92A), a classical BAR protein, regulates ciliary assembly, mitochondrial ultrastructure, and neuronal membrane dynamics, yet its molecular mechanisms remain elusive. Here, we determined the 2.2 Å crystal structure of the mouse FAM92A BAR domain, revealing an antiparallel, crescent-shaped homodimer. Structure-guided mutagenesis revealed that positively charged clusters on the concave surface are critical for lipid binding and identified residues essential for dimerization. We further demonstrated that FAM92A BAR directly binds the N-terminal region of Chibby1 (CBY1), a ciliary protein, with their respective dimerizations synergistically enhancing affinity. These findings elucidate the structural basis of FAM92A's membrane remodeling and CBY1 interaction, providing a molecular framework for its function in ciliogenesis and suggesting broader implications for FAM92 family proteins.

PubMed: 40484380
DOI: 10.1016/j.jbc.2025.110346

実験手法

X-RAY DIFFRACTION (2.21 Å)