- PDB-7jl4: Crystal structure of TRIM65 PSpry domain -
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基本情報
登録情報
データベース: PDB / ID: 7jl4
タイトル
Crystal structure of TRIM65 PSpry domain
要素
Tripartite motif-containing protein 65
キーワード
IMMUNE SYSTEM / RIG-I-like helicase / Ubiquitin E3 ligase
機能・相同性
機能・相同性情報
positive regulation of protein oligomerization / type I interferon-mediated signaling pathway / positive regulation of interferon-alpha production / protein K63-linked ubiquitination / protein K48-linked ubiquitination / positive regulation of autophagy / antiviral innate immune response / positive regulation of interferon-beta production / RING-type E3 ubiquitin transferase / negative regulation of inflammatory response ...positive regulation of protein oligomerization / type I interferon-mediated signaling pathway / positive regulation of interferon-alpha production / protein K63-linked ubiquitination / protein K48-linked ubiquitination / positive regulation of autophagy / antiviral innate immune response / positive regulation of interferon-beta production / RING-type E3 ubiquitin transferase / negative regulation of inflammatory response / ubiquitin protein ligase activity / positive regulation of protein phosphorylation / zinc ion binding / nucleoplasm / cytosol / cytoplasm 類似検索 - 分子機能
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
米国
引用
ジャーナル: Mol Cell / 年: 2021 タイトル: Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases. 著者: Kazuki Kato / Sadeem Ahmad / Zixiang Zhu / Janet M Young / Xin Mu / Sehoon Park / Harmit S Malik / Sun Hur / 要旨: RNA helicases and E3 ubiquitin ligases mediate many critical functions in cells, but their actions have largely been studied in distinct biological contexts. Here, we uncover evolutionarily conserved ...RNA helicases and E3 ubiquitin ligases mediate many critical functions in cells, but their actions have largely been studied in distinct biological contexts. Here, we uncover evolutionarily conserved rules of engagement between RNA helicases and tripartite motif (TRIM) E3 ligases that lead to their functional coordination in vertebrate innate immunity. Using cryoelectron microscopy and biochemistry, we show that RIG-I-like receptors (RLRs), viral RNA receptors with helicase domains, interact with their cognate TRIM/TRIM-like E3 ligases through similar epitopes in the helicase domains. Their interactions are avidity driven, restricting the actions of TRIM/TRIM-like proteins and consequent immune activation to RLR multimers. Mass spectrometry and phylogeny-guided biochemical analyses further reveal that similar rules of engagement may apply to diverse RNA helicases and TRIM/TRIM-like proteins. Our analyses suggest not only conserved substrates for TRIM proteins but also, unexpectedly, deep evolutionary connections between TRIM proteins and RNA helicases, linking ubiquitin and RNA biology throughout animal evolution.