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Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit

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dc.contributor.author Tatebe, Hisashi
dc.contributor.author Murayama, Shinichi
dc.contributor.author Yonekura, Toshiya
dc.contributor.author Hatano, Tomoyuki
dc.contributor.author Richter, David
dc.contributor.author Furuya, Tomomi
dc.contributor.author Kataoka, Saori
dc.contributor.author Furuita, Kyoko
dc.contributor.author Kojima, Chojiro
dc.contributor.author Shiozaki, Kazuhiro
dc.contributor.author Sonenberg, Nahum
dc.date.accessioned 2017-03-07T02:40:06Z
dc.date.available 2017-03-07T02:40:06Z
dc.date.issued 2017-03-07
dc.identifier.issn 2050-084X
dc.identifier.uri http://hdl.handle.net/10061/11391
dc.description.abstract The target of rapamycin (TOR) protein kinase forms multi-subunit TOR complex 1 (TORC1) and TOR complex 2 (TORC2), which exhibit distinct substrate specificities. Sin1 is one of the TORC2-specific subunit essential for phosphorylation and activation of certain AGC-family kinases. Here, we show that Sin1 is dispensable for the catalytic activity of TORC2, but its conserved region in the middle (Sin1CRIM) forms a discrete domain that specifically binds the TORC2 substrate kinases. Sin1CRIM fused to a different TORC2 subunit can recruit the TORC2 substrate Gad8 for phosphorylation even in the sin1 null mutant of fission yeast. The solution structure of Sin1CRIM shows a ubiquitin-like fold with a characteristic acidic loop, which is essential for interaction with the TORC2 substrates. The specific substrate-recognition function is conserved in human Sin1CRIM, which may represent a potential target for novel anticancer drugs that prevent activation of the mTORC2 substrates such as AKT. ja_JP
dc.language.iso en ja_JP
dc.publisher eLife Sciences Publications, Ltd ja_JP
dc.rights © 2017, Tatebe et al ja_JP
dc.rights This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. ja_JP
dc.subject target of rapamycin ja_JP
dc.subject SIN1 ja_JP
dc.subject AKT ja_JP
dc.subject substrate specificity ja_JP
dc.subject TOR complex 2 ja_JP
dc.title Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit ja_JP
dc.type.nii Journal Article ja_JP
dc.contributor.transcription ヨネクラ, トシヤ
dc.contributor.transcription フルイタ, キョウコ
dc.contributor.transcription コジマ, チョウジロウ
dc.contributor.transcription シオザキ, カズヒロ
dc.contributor.transcription タテベ, ヒサシ
dc.contributor.transcription ハタノ, トモユキ
dc.contributor.transcription フルヤ, トモミ
dc.contributor.alternative 建部, 恒
dc.contributor.alternative 米倉, 敏哉
dc.contributor.alternative 古板, 恭子
dc.contributor.alternative 児島, 長次郎
dc.contributor.alternative 塩﨑, 一裕
dc.contributor.alternative 秦野, 智行
dc.contributor.alternative 古谷, 知美
dc.identifier.fulltexturl https://dx.doi.org/10.7554/eLife.19594 ja_JP
dc.textversion publisher ja_JP
dc.identifier.volume 6 ja_JP
dc.relation.doi info:doi/10.7554/eLife.19594 ja_JP
dc.identifier.artnum e19594 ja_JP
dc.identifier.NAIST-ID 73296634 ja_JP
dc.identifier.NAIST-ID 82048331 ja_JP
dc.identifier.NAIST-ID 73296618 ja_JP

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