The TRAF-interacting protein (TRAIP) is a novel E2F target with peak expression in mitosis.

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Date

2015

Type de document
Périmètre
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Serveur académique Lausannois

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Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.18632/oncotarget.3055

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/26369285

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/eissn/1949-2553

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_CD436F3D40E05

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Serveur Académique Lausannois

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Université de Lausanne et CHUV

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info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

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3T3 Cells; Animals; Cell Cycle; Cell Nucleus/metabolism; Cell Proliferation; Cycloheximide/chemistry; E2F1 Transcription Factor/metabolism; E2F2 Transcription Factor/metabolism; E2F4 Transcription Factor/metabolism; Gene Expression Regulation, Neoplastic; Green Fluorescent Proteins/metabolism; HEK293 Cells; HeLa Cells; Humans; Keratinocytes/cytology; Mice; Mitosis; Plasmids/metabolism; Promoter Regions, Genetic; Protein Biosynthesis; Protein Synthesis Inhibitors/chemistry; RNA, Messenger/metabolism; Ubiquitin-Protein Ligases/metabolism

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Expressive behavior

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C. Chapard et al., « The TRAF-interacting protein (TRAIP) is a novel E2F target with peak expression in mitosis. », Serveur académique Lausannois, ID : 10.18632/oncotarget.3055

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The TRAF-interacting protein (TRAIP) is an E3 ubiquitin ligase required for cell proliferation. TRAIP mRNA is downregulated in human keratinocytes after inhibition of the PI3K/AKT/mTOR signaling. Since E2F transcription factors are downstream of PI3K/AKT/mTOR we investigated whether they regulate TRAIP expression. E2F1 expression significantly increased the TRAIP mRNA level in HeLa cells. Reporter assays with the 1400 bp 5'-upstream promoter in HeLa cells and human keratinocytes showed that E2F1-, E2F2- and E2F4-induced upregulation of TRAIP expression is mediated by 168 bp upstream of the translation start site. Mutating the E2F binding site within this fragment reduced the E2F1- and E2F2-dependent promoter activities and protein-DNA complex formation in gel shift assays. Abundance of TRAIP mRNA and protein was regulated by the cell cycle with a peak in G2/M. Expression of GFP and TRAIP-GFP demonstrated that TRAIP-GFP protein has a lower steady-state concentration than GFP despite similar mRNA levels. Cycloheximide inhibition experiments indicated that the TRAIP protein has a half-life of around four hours. Therefore, the combination of cell cycle-dependent transcription of the TRAIP gene by E2F and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M. These findings suggest that TRAIP has important functions in mitosis and tumorigenesis.

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