Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 516 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 506 | - |
dc.citation.title | ACS CENTRAL SCIENCE | - |
dc.citation.volume | 2 | - |
dc.contributor.author | Lee, Song-Yi | - |
dc.contributor.author | Lee, Hakbong | - |
dc.contributor.author | Lee, Hye-Kyeong | - |
dc.contributor.author | Lee, Seung-Won | - |
dc.contributor.author | Ha, Sung Chul | - |
dc.contributor.author | Kwon, Taejoon | - |
dc.contributor.author | Seo, Jeong Kon | - |
dc.contributor.author | Lee, Changwook | - |
dc.contributor.author | Rhee, Hyun-Woo | - |
dc.date.accessioned | 2023-12-21T23:17:17Z | - |
dc.date.available | 2023-12-21T23:17:17Z | - |
dc.date.created | 2016-10-11 | - |
dc.date.issued | 2016-08 | - |
dc.description.abstract | Mammalian target of rapamycin (mTOR) signaling is a core pathway in cellular metabolism, and control of the mTOR pathway by rapamycin shows potential for the treatment of metabolic diseases. In this study, we employed a new proximity biotin-labeling method using promiscuous biotin ligase (pBirA) to identify unknown elements in the rapamycin-induced interactome on the FK506-rapamycin binding (FRB) domain in living cells. FKBP25 showed the strongest biotin labeling by FRB-pBirA in the presence of rapamycin. Immunoprecipitation and immunofluorescence experiments confirmed that endogenous FKBP25 has a rapamycin-induced physical interaction with the FRB domain. Furthermore, the crystal structure of the ternary complex of FRB-rapamycin-FKBP25 was determined at 1.67-angstrom resolution. In this crystal structure we found that the conformational changes of FRB generate a hole where there is a methionine-rich space, and covalent metalloid coordination was observed at C2085 of FRB located at the bottom of the hole. Our results imply that FKBP25 might have a unique physiological role related to metallomics in mTOR signaling. | - |
dc.identifier.bibliographicCitation | ACS CENTRAL SCIENCE, v.2, no.8, pp.506 - 516 | - |
dc.identifier.doi | 10.1021/acscentsci.6b00137 | - |
dc.identifier.issn | 2374-7943 | - |
dc.identifier.scopusid | 2-s2.0-85026298484 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20590 | - |
dc.identifier.url | http://pubs.acs.org/doi/full/10.1021/acscentsci.6b00137 | - |
dc.identifier.wosid | 000384750300007 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Proximity-Directed Labeling Reveals a New Rapamycin-Induced Heterodimer of FKBP25 and FRB in Live Cells | - |
dc.type | Article | - |
dc.description.isOpenAccess | TRUE | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | PROTEIN-PROTEIN INTERACTIONS | - |
dc.subject.keywordPlus | LIVING CELLS | - |
dc.subject.keywordPlus | BINDING DOMAIN | - |
dc.subject.keywordPlus | BIOTIN LIGASE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | PROTEOMICS | - |
dc.subject.keywordPlus | CHEMISTRY | - |
dc.subject.keywordPlus | PATHWAY | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.