2K9U

Solution NMR structure of the Filamin-migfilin complex

2K9U の概要

• エントリーDOI: 10.2210/pdb2k9u/pdb
• NMR情報: BMRB: 16002
• 分子名称: Gamma filamin, Filamin-binding LIM protein 1 (2 entities in total)
• 機能のキーワード: cytoskeletal complex, cell adhesion, cell junction, cell shape, cytoskeleton, lim domain, metal-binding, structural protein
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Cytoplasm, cell cortex: Q8WUP2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15095.87

構造登録者

Ithychanda, S.N.,Qin, J. (登録日: 2008-10-24, 公開日: 2008-12-23, 最終更新日: 2024-05-01)

主引用文献

Ithychanda, S.S.,Das, M.,Ma, Y.Q.,Ding, K.,Wang, X.,Gupta, S.,Wu, C.,Plow, E.F.,Qin, J.
Migfilin, a molecular switch in regulation of integrin activation.
J.Biol.Chem., 284:4713-4722, 2009

PubMed Abstract: The linkage of heterodimeric (alpha/beta) integrin receptors with their extracellular matrix ligands and intracellular actin cytoskeleton is a fundamental step for controlling cell adhesion and migration. Binding of the actin-linking protein, talin, to integrin beta cytoplasmic tails (CTs) induces high affinity ligand binding (integrin activation), whereas binding of another actin-linking protein, filamin, to the integrin beta CTs negatively regulates this process by blocking the talin-integrin interaction. Here we show structurally that migfilin, a novel cytoskeletal adaptor highly enriched in the integrin adhesion sites, strongly interacts with the same region in filamin where integrin beta CTs bind. We further demonstrate that the migfilin interaction dissociates filamin from integrin and promotes the talin/integrin binding and integrin activation. Migfilin thus acts as a molecular switch to disconnect filamin from integrin for regulating integrin activation and dynamics of extracellular matrix-actin linkage.

PubMed: 19074766
DOI: 10.1074/jbc.M807719200

実験手法

SOLUTION NMR