+検索条件
-Structure paper
タイトル | Allosteric regulation controls actin-bundling properties of human plastins. |
---|---|
ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 6, Page 519-528, Year 2022 |
掲載日 | 2022年5月19日 |
著者 | Christopher L Schwebach / Elena Kudryashova / Richa Agrawal / Weili Zheng / Edward H Egelman / Dmitri S Kudryashov / |
PubMed 要旨 | Plastins/fimbrins are conserved actin-bundling proteins contributing to motility, cytokinesis and other cellular processes by organizing strikingly different actin assemblies as in aligned bundles ...Plastins/fimbrins are conserved actin-bundling proteins contributing to motility, cytokinesis and other cellular processes by organizing strikingly different actin assemblies as in aligned bundles and branched networks. We propose that this ability of human plastins stems from an allosteric communication between their actin-binding domains (ABD1/2) engaged in a tight spatial association. Here we show that ABD2 can bind actin three orders of magnitude stronger than ABD1, unless the domains are involved in an equally strong inhibitory engagement. A mutation mimicking physiologically relevant phosphorylation at the ABD1-ABD2 interface greatly weakened their association, dramatically potentiating actin cross-linking. Cryo-EM reconstruction revealed the ABD1-actin interface and enabled modeling of the plastin bridge and domain separation in parallel bundles. We predict that a strong and tunable allosteric inhibition between the domains allows plastins to modulate the cross-linking strength, contributing to remodeling of actin assemblies of different morphologies defining the unique place of plastins in actin organization. |
リンク | Nat Struct Mol Biol / PubMed:35589838 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 5.1 Å |
構造データ | EMDB-25371: Allosteric Regulation of Human Plastins |
由来 |
|