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NOVEL UBIQUITIN LIGASE AND USE THEREOF

外国特許コード F110005894
整理番号 5093,S2011-0390-N0
掲載日 2011年11月9日
出願国 世界知的所有権機関(WIPO)
国際出願番号 2010JP063345
国際公開番号 WO 2011016540
国際出願日 平成22年8月6日(2010.8.6)
国際公開日 平成23年2月10日(2011.2.10)
優先権データ
  • 特願2009-184878 (2009.8.7) JP
発明の名称 (英語) NOVEL UBIQUITIN LIGASE AND USE THEREOF
発明の概要(英語) Disclosed is a novel ubiquitin ligase which has an activity of forming a linear polyubiquitin chain and can be expressed and purified with high efficiency. Specifically disclosed is a complex of (a) a protein comprising a part of HOIP and containing at least a UBA region and a RING-IBR-RING region and (b) at least one protein capable of forming a complex with the component (a). It is found that the complex is a novel ubiquitin ligase which has an activity of forming a linear polyubiquitin chain and can be expressed and purified with high efficiency.
従来技術、競合技術の概要(英語) BACKGROUND ART
Ubiquitin activating enzymes (E1) modified system, (E2) ubiquitin conjugating enzyme, ubiquitin ligase (E3) by the action of the enzyme of the group 3, ubiquitin ligase is selected to selectively identify the substrate, largely on the protein ubiquitin like a polyubiquitin chain is added to each other to form a, controls the functions of the protein post-translational modification system. Initially is found, a poly - ubiquitinated proteins all comprise the decomposition has been believed to be directed, enlarged concept is that, at present a variety of manner to control the function of the protein has been elucidated. Binding modes on a living body between the various kinds of poly-ubiquitin chain exist, depending on the type thereof modified proteins control mode are different being. Conventional ubiquitin-ubiquitin chains of the lysine side chain via isodesmosine produced by has been considered, the present inventors have N-terminal methionine N through a linear polyubiquitin chain is formed, and, a linear poly-ubiquitination is NF-κB involves activation of the shown ahead of the world.
Specifically, the present inventors, and complex HOIP HOIL-1L-ubiquitin chains are straight-chained found to generate a ubiquitin ligase, and a complex HOIP HOIL-1L designated LUBAC(linear ubiquitin chain assemble complex) (see non-patent document 1). In addition, the ubiquitin ligase LUBAC, classical pathway activation in NF-κB, IκB kinase involved in the stage, IκB kinase IKK complexes NEMO (NF-κ B essential modulator) ubiquitination in a linear, NF-κB causes selective activation of the revealed (see non-patent document 2).
The present inventors have further, linear polyubiquitin chains also Sharpin to found that a component of a ubiquitin ligase, Sharpin, two proteins of 3 and HOIP HOIL-1L, or HOIP HOIP HOIL-1L Sharpin and two proteins of 2 and or a ubiquitin ligase complex and will be referred to as LUBAC. With respect to Sharpin, cpdm natural mutant mice have called mouse Sharpin, or chronic dermatitis of the immune system such as deletions of a Peyer's exhibit symptoms of abnormality or the like have been reported (see non-patent document 3).
  • 出願人(英語)
  • ※2012年7月以前掲載分については米国以外のすべての指定国
  • KYOTO UNIVERSITY
  • 発明者(英語)
  • IWAI, Kazuhiro
国際特許分類(IPC)
指定国 National States: AE AG AL AM AO AT AU AZ BA BB BG BH BR BW BY BZ CA CH CL CN CO CR CU CZ DE DK DM DO DZ EC EE EG ES FI GB GD GE GH GM GT HN HR HU ID IL IN IS JP KE KG KM KN KP KR KZ LA LC LK LR LS LT LU LY MA MD ME MG MK MN MW MX MY MZ NA NG NI NO NZ OM PE PG PH PL PT RO RS RU SC SD SE SG SK SL SM ST SV SY TH TJ TM TN TR TT TZ UA UG US UZ VC VN ZA ZM ZW
ARIPO: BW GH GM KE LR LS MW MZ NA SD SL SZ TZ UG ZM ZW
EAPO: AM AZ BY KG KZ MD RU TJ TM
EPO: AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LT LU LV MC MK MT NL NO PL PT RO SE SI SK SM TR
OAPI: BF BJ CF CG CI CM GA GN GQ GW ML MR NE SN TD TG
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