+検索条件
-Structure paper
| タイトル | Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments. |
|---|---|
| ジャーナル・号・ページ | J Mol Cell Cardiol, Vol. 212, Page 10-15, Year 2025 |
| 掲載日 | 2025年12月22日 |
著者 | Kripa Chitre / Olga E Karpicheva / Chloe J King / Michael J Rynkiewicz / Axel J Fenwick / John F Dawson / D Brian Foster / William Lehman / Anthony Cammarato / ![]() |
| PubMed 要旨 | Electrostatic interactions between actin residues K326 and K328 and tropomyosin bias tropomyosin to an F-actin location where it blocks myosin attachment. K326/328 acetylation neutralizes their ...Electrostatic interactions between actin residues K326 and K328 and tropomyosin bias tropomyosin to an F-actin location where it blocks myosin attachment. K326/328 acetylation neutralizes their charge, potentially disrupting thin filament-based contractile regulation. We verified acetylation of K326/328 on human cardiac actin (ACTC1) and generated recombinant K326/328Q, pseudo-acetylated ACTC1. Pseudo-acetylation reduced inhibition of myosin-driven motility of F-actin-tropomyosin and F-actin-tropomyosin-troponin at low Ca. Cryo-EM-based and computational modeling revealed that pseudo-acetylation did not alter tropomyosin positioning along F-actin but decreased local F-actin-tropomyosin interaction energy. Thus, by reducing the energetic demands required for myosin to displace tropomyosin, ACTC1 K326/328 acetylation may promote contractile activation. |
リンク | J Mol Cell Cardiol / PubMed:41443503 |
| 手法 | EM (らせん対称) |
| 解像度 | 2.79 - 3.12 Å |
| 構造データ | EMDB-73993, PDB-9zbl: EMDB-73996, PDB-9zbp: |
| 化合物 | ![]() ChemComp-ADP: ![]() ChemComp-MG: |
| 由来 |
|
キーワード | MOTOR PROTEIN / F-actin / tropomyosin / muscle / cryo-EM structure / motor proteins / Lysine acetylation / steric regulation |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク





homo sapiens (ヒト)
キーワード