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基本情報
登録情報 | データベース: EMDB / ID: EMD-4177 | |||||||||
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タイトル | Cryo-EM structure of two dynein tail domains bound to dynactin and HOOK3 | |||||||||
![]() | Cryo-EM map showing two dynein tails bound to dynactin and HOOK3 | |||||||||
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![]() | TDH / DDH / Complex / dynein/dynactin/HOOK3 / MOTOR PROTEIN | |||||||||
機能・相同性 | ![]() RHOD GTPase cycle / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / Gap junction degradation / Formation of annular gap junctions / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions ...RHOD GTPase cycle / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / Gap junction degradation / Formation of annular gap junctions / 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 / UCH proteinases / Clathrin-mediated endocytosis / RHOF GTPase cycle / dynactin complex / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / transport along microtubule / visual behavior / WASH complex / F-actin capping protein complex / positive regulation of intracellular transport / dynein light chain binding / negative regulation of filopodium assembly / regulation of metaphase plate congression / dynein heavy chain binding / establishment of spindle localization / axonemal dynein complex / positive regulation of spindle assembly / ciliary tip / structural constituent of postsynaptic actin cytoskeleton / dense body / Intraflagellar transport / dynein complex / Neutrophil degranulation / P-body assembly / COPI-independent Golgi-to-ER retrograde traffic / minus-end-directed microtubule motor activity / barbed-end actin filament capping / dynein light intermediate chain binding / cytoplasmic dynein complex / regulation of cell morphogenesis / regulation of lamellipodium assembly / retrograde axonal transport / nuclear migration / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / COPI-mediated anterograde transport / centrosome localization / microtubule motor activity / dynein intermediate chain binding / dynein complex binding / NuA4 histone acetyltransferase complex / microtubule-based movement / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / stress granule assembly / Mitotic Prometaphase / cytoplasmic microtubule organization / EML4 and NUDC in mitotic spindle formation / regulation of mitotic spindle organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / axon cytoplasm / Recruitment of mitotic centrosome proteins and complexes / cytoskeleton organization / Recruitment of NuMA to mitotic centrosomes / Resolution of Sister Chromatid Cohesion / Anchoring of the basal body to the plasma membrane / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / sarcomere / AURKA Activation by TPX2 / axonogenesis / cellular response to nerve growth factor stimulus / mitotic spindle organization / filopodium / RHO GTPases Activate Formins / cell motility / actin filament / 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 / cell morphogenesis / kinetochore / cilium / Aggrephagy / microtubule cytoskeleton organization / HCMV Early Events / Separation of Sister Chromatids / Regulation of PLK1 Activity at G2/M Transition / azurophil granule lumen / actin filament binding 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 6.7 Å | |||||||||
![]() | Lau CK / Urnavicius L | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Cryo-EM shows how dynactin recruits two dyneins for faster movement. 著者: Linas Urnavicius / Clinton K Lau / Mohamed M Elshenawy / Edgar Morales-Rios / Carina Motz / Ahmet Yildiz / Andrew P Carter / ![]() ![]() ![]() 要旨: Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. ...Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine. | |||||||||
履歴 |
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構造の表示
ムービー |
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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 | ![]() | 44.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 52 KB 52 KB | 表示 表示 | ![]() |
画像 | ![]() | 79.6 KB | ||
Filedesc metadata | ![]() | 10 KB | ||
その他 | ![]() ![]() | 668.2 MB 669.7 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 327.2 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 326.4 KB | 表示 | |
XML形式データ | ![]() | 17.8 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 6f38MC ![]() 4168C ![]() 4169C ![]() 4170C ![]() 4171C ![]() 4172C ![]() 5owoC ![]() 6f1tC ![]() 6f1uC ![]() 6f1vC ![]() 6f1yC ![]() 6f1zC ![]() 6f3aC M: このマップから作成された原子モデル C: 同じ文献を引用 ( |
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類似構造データ |
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Cryo-EM map showing two dynein tails bound to dynactin and HOOK3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.42 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
-ハーフマップ: #1
ファイル | emd_4177_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: #2
ファイル | emd_4177_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 |
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試料の構成要素
+全体 : Complex of two dynein tail domains bound to dynactin and HOOK3
+超分子 #1: Complex of two dynein tail domains bound to dynactin and HOOK3
+超分子 #2: Dynactin
+超分子 #3: Dynein
+超分子 #4: HOOK3
+分子 #1: ARP1 actin related protein 1 homolog A
+分子 #2: Actin, cytoplasmic 1
+分子 #3: Actin related protein 10 homolog
+分子 #4: Capping protein (Actin filament) muscle Z-line, alpha 1
+分子 #5: F-actin capping protein beta subunit
+分子 #6: Dynactin Subunit 2
+分子 #7: Dynactin Subunit 2
+分子 #8: Dynactin Subunit 3
+分子 #9: Dynactin Subunit 2
+分子 #10: Dynactin 6
+分子 #11: Dynactin subunit 5
+分子 #12: HOOK3
+分子 #13: Dynactin Subunit 4
+分子 #14: Dynactin Subunit 1
+分子 #15: Dynactin subunit 2
+分子 #16: Dynactin subunit 2
+分子 #17: Dynactin subunit 2
+分子 #18: Dynactin subunit 2
+分子 #19: Cytoplasmic dynein 1 heavy chain 1
+分子 #20: Cytoplasmic dynein 1 intermediate chain 2
+分子 #21: Cytoplasmic dynein 1 light intermediate chain 2
+分子 #22: Dynein light chain roadblock-type 1
+分子 #23: Dynactin Subunit 1
+分子 #24: ADENOSINE-5'-DIPHOSPHATE
+分子 #25: ADENOSINE-5'-TRIPHOSPHATE
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.2 |
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凍結 | 凍結剤: ETHANE |
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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: FEI FALCON III (4k x 4k) 検出モード: INTEGRATING / 平均電子線量: 45.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
初期モデル | モデルのタイプ: EMDB MAP EMDB ID: 詳細: Model low pass filtered to 50 Angstroms |
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最終 再構成 | 想定した対称性 - 点群: C1 (非対称) / 解像度のタイプ: BY AUTHOR / 解像度: 6.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 23407 |
初期 角度割当 | タイプ: PROJECTION MATCHING / ソフトウェア - 名称: RELION |
最終 角度割当 | タイプ: PROJECTION MATCHING / ソフトウェア - 名称: RELION |
-原子モデル構築 1
精密化 | 空間: REAL / プロトコル: FLEXIBLE FIT / 当てはまり具合の基準: Corellation Coefficient |
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得られたモデル | ![]() PDB-6f38: |