登録情報 データベース : EMDB / ID : EMD-48106 ダウンロードとリンクタイトル Lgl2 bound to the aPKCiota-Par6a complex in its nucleotide-free form. マップデータ 詳細 試料複合体 : A ternary complex of Lgl2 with aPKC iota and Par6A (nucleotide-free)タンパク質・ペプチド : Lethal Giant Larvae homolog 2 (Lgl2)タンパク質・ペプチド : Atypical protein kinase C (aPKC) iotaタンパク質・ペプチド : Partitioning defective 6 homolog alpha (Par6A) 詳細 キーワード Cell Polarity / Kinase / Complex. / LIPID BINDING 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
establishment of spindle orientation / establishment or maintenance of polarity of embryonic epithelium / Golgi vesicle budding / diacylglycerol-dependent, calcium-independent serine/threonine kinase activity / PAR polarity complex / Tight junction interactions / regulation of establishment or maintenance of cell polarity / protein kinase C / establishment of apical/basal cell polarity / diacylglycerol-dependent serine/threonine kinase activity ... establishment of spindle orientation / establishment or maintenance of polarity of embryonic epithelium / Golgi vesicle budding / diacylglycerol-dependent, calcium-independent serine/threonine kinase activity / PAR polarity complex / Tight junction interactions / regulation of establishment or maintenance of cell polarity / protein kinase C / establishment of apical/basal cell polarity / diacylglycerol-dependent serine/threonine kinase activity / L-leucine transport / myosin II binding / negative regulation of glial cell apoptotic process / regulation of Notch signaling pathway / eye photoreceptor cell development / branching involved in labyrinthine layer morphogenesis / Schmidt-Lanterman incisure / Golgi to plasma membrane transport / establishment or maintenance of epithelial cell apical/basal polarity / cellular response to chemical stress / membrane organization / cell-cell junction organization / tight junction / cortical actin cytoskeleton organization / protein targeting to membrane / labyrinthine layer blood vessel development / cortical actin cytoskeleton / positive regulation of Notch signaling pathway / establishment of cell polarity / cell leading edge / exocytosis / brush border / positive regulation of glial cell proliferation / positive regulation of endothelial cell apoptotic process / bicellular tight junction / regulation of postsynaptic membrane neurotransmitter receptor levels / p75NTR recruits signalling complexes / intercellular bridge / vesicle-mediated transport / cytoskeleton organization / secretion / response to interleukin-1 / GTPase activator activity / actin filament organization / post-embryonic development / protein localization to plasma membrane / positive regulation of D-glucose import / adherens junction / positive regulation of protein localization to plasma membrane / PDZ domain binding / positive regulation of NF-kappaB transcription factor activity / positive regulation of neuron projection development / phospholipid binding / Pre-NOTCH Transcription and Translation / Schaffer collateral - CA1 synapse / multicellular organism growth / cellular response to insulin stimulus / KEAP1-NFE2L2 pathway / cell migration / microtubule cytoskeleton / negative regulation of neuron apoptotic process / protein phosphorylation / protein kinase activity / endosome / intracellular signal transduction / cilium / apical plasma membrane / Golgi membrane / cell division / protein serine kinase activity / intracellular membrane-bounded organelle / protein serine/threonine kinase activity / negative regulation of apoptotic process / glutamatergic synapse / extracellular exosome / zinc ion binding / nucleoplasm / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 Lethal(2) giant larvae protein / Lethal giant larvae homologue 2 / LLGL2 / Atypical protein kinase C iota type, catalytic domain / Protein kinase C / Protein kinase C, PB1 domain / PB1 domain / PB1 domain / PB1 domain / : ... Lethal(2) giant larvae protein / Lethal giant larvae homologue 2 / LLGL2 / Atypical protein kinase C iota type, catalytic domain / Protein kinase C / Protein kinase C, PB1 domain / PB1 domain / PB1 domain / PB1 domain / : / PB1 domain profile. / Protein kinase, C-terminal / Protein kinase C terminal domain / Diacylglycerol/phorbol-ester binding / Phorbol esters/diacylglycerol binding domain (C1 domain) / Zinc finger phorbol-ester/DAG-type signature. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C1-like domain superfamily / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / WD domain, G-beta repeat / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily 類似検索 - ドメイン・相同性 Protein kinase C iota type / LLGL scribble cell polarity complex component 2 / Isoform 2 of Partitioning defective 6 homolog alpha 類似検索 - 構成要素生物種 Homo sapiens (ヒト)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 4.05 Å 詳細 データ登録者Almagor L / Weis WI 資金援助 1件 詳細 詳細を隠すOrganization Grant number 国 Not funded
引用ジャーナル : Commun Biol / 年 : 2025タイトル : Polarity protein Par6 facilitates the processive phosphorylation of Lgl via a dynamic interaction with aPKC.著者 : Lior Almagor / William I Weis / 要旨 : Polarity along an apical-basal axis is essential for epithelial cell shape and function. The atypical protein Kinase-C (aPKC) and its regulatory partner Par6 form a complex that is essential for ... Polarity along an apical-basal axis is essential for epithelial cell shape and function. The atypical protein Kinase-C (aPKC) and its regulatory partner Par6 form a complex that is essential for polarization, a primary function of which is to phosphorylate the Lethal giant larvae (Lgl) protein to prevent it from binding to the apical membrane (thereby facilitating its basolateral localization). Par6 binds Lgl directly and is essential for this process, but its mechanism was obscure. Here, we utilize cryo-EM and various biochemical techniques to characterize the interaction of Lgl2 with the aPKCι/Par6 complex and to study the roles of Par6 in promoting Lgl2 phosphorylation. We find that Par6 proteins stabilize a ternary Lgl2/aPKCι/Par6 complex that involves a unique multi-surface interaction of Lgl2 with both aPKCι and Par6. Importantly, we find Par6b induces processive phosphorylation that results in a multi-phosphorylated Lgl2 after a single interaction with the aPKCι/Par6b complex. This is enabled by a Par6b/Lgl2 interaction that maintains contact of Lgl2 with the kinase throughout its distinct nucleotide-binding states. Our results reveal the mechanistic basis for the efficient regulation of Lgl's membrane binding by aPKC/Par6 and provide invaluable structural data for further understanding the mechanisms of this polarity complex. 履歴 登録 2024年11月28日 - ヘッダ(付随情報) 公開 2025年7月2日 - マップ公開 2025年7月2日 - 更新 2025年7月16日 - 現状 2025年7月16日 処理サイト : RCSB / 状態 : 公開
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