Cited 75 times in
Effect of phosphorylation and S–S bond-induced dimerization on DNA binding and transcriptional activation by C/EBPβ
DC Field | Value | Language |
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dc.contributor.author | 김재우 | - |
dc.date.accessioned | 2014-12-21T17:17:40Z | - |
dc.date.available | 2014-12-21T17:17:40Z | - |
dc.date.issued | 2007 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/97317 | - |
dc.description.abstract | CCAAT enhancer binding protein β (C/EBPβ) plays an essential role in the cascade that triggers adipocyte differentiation. C/EBPβ activates transcription of C/EBPα and peroxisome proliferator-activated receptor-γ, transcriptional activators of genes that give rise to the adipocyte phenotype. Sequential phosphorylation of C/EBPβ/liver activating protein (LAP) on Thr188 by MAPK and on Ser184 or Thr179 by glycogen synthase kinase β (GSK3β) is required for acquisition of DNA binding activity and transcriptional activation. To investigate how phosphorylation and dimerization of C/EBPβ/LAP alter these activities, wild-type (Wt) and mutant rC/EBPβs were prepared and purified to assess DNA binding and transcription in cell-free systems. rC/EBPβ/LAP, phosphorylated by MAPK and GSK3β in vitro, produced a >100-fold increase in DNA binding activity. Mutation of the phosphorylation to Glu increased DNA binding activity. Using a cell-free transcription system with nuclear extract from 3T3-L1 preadipocytes and rC/EBPβ/LAP, only doubly phosphorylated rC/EBPβ/LAP (by MAPK and GSK3β) activated transcription driven by Wt C/EBPα, 422/aP2, and SCD1 promoters. Oxidation-induced dimerization of doubly phosphorylated Wt rC/EBPβ/LAP increased DNA binding, whereas unphosphorylated Wt rC/EBPβ/LAP lacked DNA binding activity. Mutation of the C-terminal Cys296 adjacent to the leucine zipper and Cys143 just upstream of the DNA binding domain eliminated phosphorylation-, oxidation-, and dimerization-dependent DNA binding activity, whereas mutation of Cys201 within the basic DNA binding domain had little effect on DNA binding. These findings indicate that dual phosphorylation of C/EBPβ/LAP caused a conformational change that facilitates S–S bond formation and dimerization, rendering the basic region accessible to the C/EBP regulatory element. | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 1800~1804 | - |
dc.relation.isPartOf | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.title | Effect of phosphorylation and S–S bond-induced dimerization on DNA binding and transcriptional activation by C/EBPβ | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Biochemistry & Molecular Biology (생화학,분자생물학) | - |
dc.contributor.googleauthor | Jae-woo Kim | - |
dc.contributor.googleauthor | Qi-Qun Tang | - |
dc.contributor.googleauthor | M. Daniel Lane | - |
dc.contributor.googleauthor | Xi Li | - |
dc.identifier.doi | 10.1073/pnas.0611137104 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A00865 | - |
dc.relation.journalcode | J02550 | - |
dc.identifier.eissn | 1091-6490 | - |
dc.contributor.alternativeName | Kim, Jae Woo | - |
dc.contributor.affiliatedAuthor | Kim, Jae Woo | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 104 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 1800 | - |
dc.citation.endPage | 1804 | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol.104(6) : 1800-1804, 2007 | - |
dc.identifier.rimsid | 50435 | - |
dc.type.rims | ART | - |
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