+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-17558 | |||||||||
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タイトル | Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | Complex / CONTRACTILE PROTEIN | |||||||||
機能・相同性 | 機能・相同性情報 cytoskeletal calyx / tubulobulbar complex / meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / muscle cell projection membrane / meiotic cytokinesis / lamellipodium organization / Advanced glycosylation endproduct receptor signaling / spindle localization ...cytoskeletal calyx / tubulobulbar complex / meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / muscle cell projection membrane / meiotic cytokinesis / lamellipodium organization / Advanced glycosylation endproduct receptor signaling / spindle localization / RHOF GTPase cycle / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / site of polarized growth / UCH proteinases / Gap junction degradation / Formation of annular gap junctions / RHOF GTPase cycle / RHOD GTPase cycle / Clathrin-mediated endocytosis / actin polymerization-dependent cell motility / COPI-independent Golgi-to-ER retrograde traffic / Arp2/3 protein complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / asymmetric cell division / Arp2/3 complex-mediated actin nucleation / icosahedral viral capsid / Arp2/3 complex binding / F-actin capping protein complex / actin nucleation / WASH complex / COPI-mediated anterograde transport / negative regulation of filopodium assembly / mitotic spindle midzone / modification of postsynaptic actin cytoskeleton / modification of postsynaptic structure / regulation of cell projection assembly / actin cap / regulation of mitophagy / profilin binding / postsynaptic actin cytoskeleton / structural constituent of postsynaptic actin cytoskeleton / Factors involved in megakaryocyte development and platelet production / dense body / regulation of actin filament polymerization / positive regulation of smooth muscle contraction / substrate-dependent cell migration, cell extension / positive regulation of chemotaxis / cell projection organization / cell junction assembly / MHC class II antigen presentation / actin polymerization or depolymerization / barbed-end actin filament capping / focal adhesion assembly / regulation of cell morphogenesis / proline-rich region binding / regulation of lamellipodium assembly / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / podosome / lamellipodium assembly / dendritic spine maintenance / regulation of axon extension / positive regulation of actin filament polymerization / establishment or maintenance of cell polarity / cortical actin cytoskeleton / cortical cytoskeleton / NuA4 histone acetyltransferase complex / filamentous actin / brush border / asymmetric synapse / cilium assembly / RHO GTPases Activate WASPs and WAVEs / positive regulation of double-strand break repair via homologous recombination / positive regulation of lamellipodium assembly / voltage-gated potassium channel complex / positive regulation of substrate adhesion-dependent cell spreading / clathrin-coated pit / cytoskeleton organization / extrinsic apoptotic signaling pathway / ruffle / EPHB-mediated forward signaling / actin filament polymerization / hippocampal mossy fiber to CA3 synapse / axonogenesis / receptor-mediated endocytosis / neuron projection morphogenesis / ribonucleoside triphosphate phosphatase activity / cellular response to nerve growth factor stimulus / cell projection / cell motility / negative regulation of extrinsic apoptotic signaling pathway / actin filament / FCGR3A-mediated phagocytosis / intracellular protein transport 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) / Sus scrofa (ブタ) / Mus musculus (ハツカネズミ) / Amanita phalloides (タマゴテングタケ) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.3 Å | |||||||||
データ登録者 | Liu T / Moores CA | |||||||||
資金援助 | European Union, 1件
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引用 | ジャーナル: Nat Struct Mol Biol / 年: 2024 タイトル: Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament. 著者: Tianyang Liu / Luyan Cao / Miroslav Mladenov / Antoine Jegou / Michael Way / Carolyn A Moores / 要旨: Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane ...Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane trafficking. Cortactin is important for actin branch stabilization, but the mechanism by which this occurs is unclear. Given this, we determined the structure of vertebrate cortactin-stabilized Arp2/3 actin branches using cryogenic electron microscopy. We find that cortactin interacts with the new daughter filament nucleated by the Arp2/3 complex at the branch site, rather than the initial mother actin filament. Cortactin preferentially binds activated Arp3. It also stabilizes the F-actin-like interface of activated Arp3 with the first actin subunit of the new filament, and its central repeats extend along successive daughter-filament subunits. The preference of cortactin for activated Arp3 explains its retention at the actin branch and accounts for its synergy with other nucleation-promoting factors in regulating branched actin network dynamics. | |||||||||
履歴 |
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-構造の表示
添付画像 |
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-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_17558.map.gz | 163.1 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-17558-v30.xml emd-17558.xml | 34.6 KB 34.6 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_17558_fsc.xml | 14.6 KB | 表示 | FSCデータファイル |
画像 | emd_17558.png | 72 KB | ||
Filedesc metadata | emd-17558.cif.gz | 9.3 KB | ||
その他 | emd_17558_half_map_1.map.gz emd_17558_half_map_2.map.gz | 301.6 MB 301.6 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-17558 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17558 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_17558_validation.pdf.gz | 1.1 MB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_17558_full_validation.pdf.gz | 1.1 MB | 表示 | |
XML形式データ | emd_17558_validation.xml.gz | 24 KB | 表示 | |
CIF形式データ | emd_17558_validation.cif.gz | 31.3 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17558 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17558 | HTTPS FTP |
-関連構造データ
関連構造データ | 8p94MC C: 同じ文献を引用 (文献) M: このマップから作成された原子モデル |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_17558.map.gz / 形式: CCP4 / 大きさ: 325 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.067 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-ハーフマップ: #2
ファイル | emd_17558_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_17558_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
+全体 : Cortactin stabilizes Arp2/3-complex nucleated actin branches with...
+超分子 #1: Cortactin stabilizes Arp2/3-complex nucleated actin branches with...
+超分子 #2: Human Arp2/3 C1BC5L complex
+超分子 #3: Porcine actin, cytoplasmic 1
+超分子 #4: Mouse cortactin
+超分子 #5: Mouse capping protein
+超分子 #6: Phalloidin
+分子 #1: Actin-related protein 3
+分子 #2: Actin-related protein 2
+分子 #3: Actin-related protein 2/3 complex subunit 1B
+分子 #4: Actin-related protein 2/3 complex subunit 2
+分子 #5: Actin-related protein 2/3 complex subunit 3
+分子 #6: Actin-related protein 2/3 complex subunit 4
+分子 #7: Actin-related protein 2/3 complex subunit 5-like protein
+分子 #8: Actin, cytoplasmic 1
+分子 #9: Src substrate cortactin
+分子 #10: F-actin-capping protein subunit alpha-1
+分子 #11: Isoform 2 of F-actin-capping protein subunit beta
+分子 #12: Phalloidin
+分子 #13: ADENOSINE-5'-DIPHOSPHATE
+分子 #14: MAGNESIUM ION
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.5 詳細: 20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT |
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凍結 | 凍結剤: ETHANE / チャンバー内湿度: 98 % / チャンバー内温度: 295.15 K / 装置: LEICA EM GP / 詳細: Back blotting. |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) 平均電子線量: 49.4 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.4 µm / 最小 デフォーカス(公称値): 0.9 µm / 倍率(公称値): 81000 |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
+画像解析
-原子モデル構築 1
初期モデル | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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精密化 | プロトコル: OTHER |
得られたモデル | PDB-8p94: |