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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 en
dc.contributor.author Murayama, Shinichi en
dc.contributor.author Yonekura, Toshiya en
dc.contributor.author Hatano, Tomoyuki en
dc.contributor.author Richter, David en
dc.contributor.author Furuya, Tomomi en
dc.contributor.author Kataoka, Saori en
dc.contributor.author Furuita, Kyoko en
dc.contributor.author Kojima, Chojiro en
dc.contributor.author Shiozaki, Kazuhiro en
dc.contributor.author Sonenberg, Nahum en
dc.date.accessioned 2017-03-07T02:40:06Z en
dc.date.available 2017-03-07T02:40:06Z en
dc.date.issued 2017-03-07 en
dc.identifier.issn 2050-084X en
dc.identifier.uri http://hdl.handle.net/10061/11391 en
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. en
dc.language.iso en en
dc.publisher eLife Sciences Publications, Ltd en
dc.rights © 2017, Tatebe et al ja
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. en
dc.subject target of rapamycin en
dc.subject SIN1 en
dc.subject AKT en
dc.subject substrate specificity en
dc.subject TOR complex 2 en
dc.title Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit en
dc.type.nii Journal Article en
dc.contributor.transcription ヨネクラ, トシヤ ja
dc.contributor.transcription フルイタ, キョウコ ja
dc.contributor.transcription コジマ, チョウジロウ ja
dc.contributor.transcription シオザキ, カズヒロ ja
dc.contributor.transcription タテベ, ヒサシ ja
dc.contributor.transcription ハタノ, トモユキ ja
dc.contributor.transcription フルヤ, トモミ ja
dc.contributor.alternative 建部, 恒 ja
dc.contributor.alternative 米倉, 敏哉 ja
dc.contributor.alternative 古板, 恭子 ja
dc.contributor.alternative 児島, 長次郎 ja
dc.contributor.alternative 塩﨑, 一裕 ja
dc.contributor.alternative 秦野, 智行 ja
dc.contributor.alternative 古谷, 知美 ja
dc.textversion publisher en
dc.identifier.volume 6 en
dc.relation.doi 10.7554/eLife.19594 en
dc.identifier.artnum e19594 en
dc.identifier.NAIST-ID 73296634 en
dc.identifier.NAIST-ID 82048331 en
dc.identifier.NAIST-ID 73296618 en

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