O-Linked N-Acetylglucosamine Modification on CCAAT Enhancer-binding Protein Î
CCAAT enhancer-binding protein (C/EBP)β is a basic leucine zipper transcription factor family member, and can be phosphorylated, acetylated, and sumoylated. C/EBPβ undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation on Thr 188 by MAPK or cyclin A/cdk2 prim...
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| Veröffentlicht in: | The Journal of biological chemistry 2009-07, Vol.284 (29), p.19248 |
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| container_title | The Journal of biological chemistry |
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| creator | Xi Li Henrik Molina Haiyan Huang You-you Zhang Mei Liu Shu-wen Qian Chad Slawson Wagner B. Dias Akhilesh Pandey Gerald W. Hart M. Daniel Lane Qi-Qun Tang |
| description | CCAAT enhancer-binding protein (C/EBP)β is a basic leucine zipper transcription factor family member, and can be phosphorylated,
acetylated, and sumoylated. C/EBPβ undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation
on Thr 188 by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser 184 /Thr 179 by GSK3β, and these phosphorylations are required for the acquisition of DNA binding activity of C/EBPβ. Here we show that
C/EBPβ is modified by O -GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins. The GlcNAcylation sites are Ser 180 and Ser 181 , which are in the regulation domain and are very close to the phosphorylation sites (Thr 188 , Ser 184 , and Thr 179 ) required for the gain of DNA binding activity. Both in vitro and ex vivo experiments demonstrate that GlcNAcylation on Ser 180 and Ser 181 prevents phosphorylation on Thr 188 , Ser 184 , and Thr 179 , as indicated by the decreased relative phosphorylation and DNA binding activity of C/EBPβ delayed the adipocyte differentiation
program. Mutation of both Ser 180 and Ser 181 to Ala significantly increase the transcriptional activity of C/EBPβ. These data suggest that GlcNAcylation regulates both
the phosphorylation and DNA binding activity of C/EBPβ. |
| doi_str_mv | 10.1074/jbc.M109.005678 |
| format | Article |
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acetylated, and sumoylated. C/EBPβ undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation
on Thr 188 by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser 184 /Thr 179 by GSK3β, and these phosphorylations are required for the acquisition of DNA binding activity of C/EBPβ. Here we show that
C/EBPβ is modified by O -GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins. The GlcNAcylation sites are Ser 180 and Ser 181 , which are in the regulation domain and are very close to the phosphorylation sites (Thr 188 , Ser 184 , and Thr 179 ) required for the gain of DNA binding activity. Both in vitro and ex vivo experiments demonstrate that GlcNAcylation on Ser 180 and Ser 181 prevents phosphorylation on Thr 188 , Ser 184 , and Thr 179 , as indicated by the decreased relative phosphorylation and DNA binding activity of C/EBPβ delayed the adipocyte differentiation
program. Mutation of both Ser 180 and Ser 181 to Ala significantly increase the transcriptional activity of C/EBPβ. These data suggest that GlcNAcylation regulates both
the phosphorylation and DNA binding activity of C/EBPβ.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M109.005678</identifier><identifier>PMID: 19478079</identifier><language>eng</language><publisher>American Society for Biochemistry and Molecular Biology</publisher><ispartof>The Journal of biological chemistry, 2009-07, Vol.284 (29), p.19248</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Xi Li</creatorcontrib><creatorcontrib>Henrik Molina</creatorcontrib><creatorcontrib>Haiyan Huang</creatorcontrib><creatorcontrib>You-you Zhang</creatorcontrib><creatorcontrib>Mei Liu</creatorcontrib><creatorcontrib>Shu-wen Qian</creatorcontrib><creatorcontrib>Chad Slawson</creatorcontrib><creatorcontrib>Wagner B. Dias</creatorcontrib><creatorcontrib>Akhilesh Pandey</creatorcontrib><creatorcontrib>Gerald W. Hart</creatorcontrib><creatorcontrib>M. Daniel Lane</creatorcontrib><creatorcontrib>Qi-Qun Tang</creatorcontrib><title>O-Linked N-Acetylglucosamine Modification on CCAAT Enhancer-binding Protein Î</title><title>The Journal of biological chemistry</title><description>CCAAT enhancer-binding protein (C/EBP)β is a basic leucine zipper transcription factor family member, and can be phosphorylated,
acetylated, and sumoylated. C/EBPβ undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation
on Thr 188 by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser 184 /Thr 179 by GSK3β, and these phosphorylations are required for the acquisition of DNA binding activity of C/EBPβ. Here we show that
C/EBPβ is modified by O -GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins. The GlcNAcylation sites are Ser 180 and Ser 181 , which are in the regulation domain and are very close to the phosphorylation sites (Thr 188 , Ser 184 , and Thr 179 ) required for the gain of DNA binding activity. Both in vitro and ex vivo experiments demonstrate that GlcNAcylation on Ser 180 and Ser 181 prevents phosphorylation on Thr 188 , Ser 184 , and Thr 179 , as indicated by the decreased relative phosphorylation and DNA binding activity of C/EBPβ delayed the adipocyte differentiation
program. Mutation of both Ser 180 and Ser 181 to Ala significantly increase the transcriptional activity of C/EBPβ. These data suggest that GlcNAcylation regulates both
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acetylated, and sumoylated. C/EBPβ undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation
on Thr 188 by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser 184 /Thr 179 by GSK3β, and these phosphorylations are required for the acquisition of DNA binding activity of C/EBPβ. Here we show that
C/EBPβ is modified by O -GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins. The GlcNAcylation sites are Ser 180 and Ser 181 , which are in the regulation domain and are very close to the phosphorylation sites (Thr 188 , Ser 184 , and Thr 179 ) required for the gain of DNA binding activity. Both in vitro and ex vivo experiments demonstrate that GlcNAcylation on Ser 180 and Ser 181 prevents phosphorylation on Thr 188 , Ser 184 , and Thr 179 , as indicated by the decreased relative phosphorylation and DNA binding activity of C/EBPβ delayed the adipocyte differentiation
program. Mutation of both Ser 180 and Ser 181 to Ala significantly increase the transcriptional activity of C/EBPβ. These data suggest that GlcNAcylation regulates both
the phosphorylation and DNA binding activity of C/EBPβ.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>19478079</pmid><doi>10.1074/jbc.M109.005678</doi></addata></record> |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| title | O-Linked N-Acetylglucosamine Modification on CCAAT Enhancer-binding Protein Î |
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