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Influence of proteasomal degradation of RNA‐binding protein dTIS11 on ARE‐mediated decay
Author(s) -
Ngoc Long Vo,
Kruys Véronique,
Gueydan Cyril
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.553.5
Subject(s) - rna , rna binding protein , microbiology and biotechnology , gene expression , phosphorylation , gene , translation (biology) , drosophila melanogaster , messenger rna , chemistry , transcriptional regulation , translational regulation , biology , biochemistry
dTIS11 is an RNA‐binding protein responsible for the processing of AU‐rich element (ARE)‐containing mRNAs in Drosophila melanogaster . In response to immunological challenge, coordination of dTIS11 levels with that of its target genes is crucial for the implementation of their transient expression profiles. We observed that this mechanism could operate in absence of transcriptional regulation of the tis11 gene, suggesting the presence of post‐translational regulation processes. Here, we report that dTIS11 protein stability is tightly regulated in resting drosophila S2 cells, by a process that involves proteasomal activity, phosphorylation and RNA‐binding. Upon immunological challenge, modifications to dTIS11 alter its decay rate, adjusting to the increasing levels of target ARE‐containing mRNAs. This work was supported by a doctoral grant of the Fonds pour la Recherche en Industrie et Agriculture