登録情報 データベース : EMDB / ID : EMD-11313 構造の表示 ダウンロードとリンクタイトル Cryo-EM structure of the dynactin complex at 3.8 Angstrom resolution マップデータ 詳細 試料複合体 : Dynactin complexリガンド : x 3種 詳細 キーワード Dynactin / Complex / Scaffold / Cytoskeleton / STRUCTURAL PROTEIN機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
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 / WASH complex / F-actin capping protein complex / negative regulation of filopodium assembly / cytoskeleton-dependent cytokinesis / cell tip / structural constituent of postsynaptic actin cytoskeleton / microtubule plus-end / dense body / dynein complex / Neutrophil degranulation / barbed-end actin filament capping / microtubule plus-end binding / regulation of cell morphogenesis / RHO GTPases activate IQGAPs / regulation of lamellipodium assembly / RHO GTPases Activate Formins / nuclear migration / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / microtubule associated complex / COPI-mediated anterograde transport / dynein complex binding / NuA4 histone acetyltransferase complex / establishment of mitotic spindle orientation / cleavage furrow / stress fiber / cytoplasmic microtubule organization / axon cytoplasm / cytoskeleton organization / centriole / sarcomere / axonogenesis / mitotic spindle organization / 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 / spindle pole / spindle / actin filament binding / actin cytoskeleton / nuclear envelope / actin binding / cell cortex / midbody / actin cytoskeleton organization / microtubule / cytoskeleton / hydrolase activity / cell division / axon / focal adhesion / centrosome / synapse / protein kinase binding / protein-containing complex / ATP binding / membrane / nucleus / plasma membrane / cytoplasm 類似検索 - 分子機能 Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 / Dynactin p62 family / : / Dynein associated protein / Dynein associated protein / Dynamitin / Dynamitin / Dynactin subunit 6 ... Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 / Dynactin p62 family / : / Dynein associated protein / Dynein associated protein / Dynamitin / Dynamitin / Dynactin subunit 6 / Dynactin subunit 5 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Trimeric LpxA-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain 類似検索 - ドメイン・相同性 Dynactin subunit 5 / Dynactin subunit 1 / Dynactin subunit 4 / Dynactin subunit 2 / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Dynactin subunit 6 / Dynactin subunit 3 / Alpha-centractin / Actin-related protein 10 / Actin, cytoplasmic 1 類似検索 - 構成要素生物種 Sus scrofa (ブタ)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.8 Å 詳細 データ登録者Lau CK / Lacey SE 資金援助 英国, 2件 詳細 詳細を隠すOrganization Grant number 国 Medical Research Council (MRC, United Kingdom) MC_UP_A025_1011 英国 Wellcome Trust WT210711 英国
引用ジャーナル : EMBO J / 年 : 2021タイトル : Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end.著者 : Clinton K Lau / Francis J O'Reilly / Balaji Santhanam / Samuel E Lacey / Juri Rappsilber / Andrew P Carter / 要旨 : Dynactin is a 1.1 MDa complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In order to do this, it forms a tripartite complex with dynein and a coiled- ... Dynactin is a 1.1 MDa complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In order to do this, it forms a tripartite complex with dynein and a coiled-coil adaptor. Dynactin consists of an actin-related filament whose length is defined by its flexible shoulder domain. Despite previous cryo-EM structures, the molecular architecture of the shoulder and pointed end of the filament is still poorly understood due to the lack of high-resolution information in these regions. Here we combine multiple cryo-EM datasets and define precise masking strategies for particle signal subtraction and 3D classification. This overcomes domain flexibility and results in high-resolution maps into which we can build the shoulder and pointed end. The unique architecture of the shoulder securely houses the p150 subunit and positions the four identical p50 subunits in different conformations to bind dynactin's filament. The pointed end map allows us to build the first structure of p62 and reveals the molecular basis for cargo adaptor binding to different sites at the pointed end. 履歴 登録 2020年7月6日 - ヘッダ(付随情報) 公開 2020年7月29日 - マップ公開 2020年7月29日 - 更新 2024年5月1日 - 現状 2024年5月1日 処理サイト : PDBe / 状態 : 公開
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