About: The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G

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About: The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G
Creator	Ageberg, Malin Drott, Kristina Gullberg, Urban Olofsson, Tor Petersson, Jessica Sandén, Carl
Source	Medline; PMC
abstract	BACKGROUND INFORMATION: The interferon (IFN)‐inducible protein TRIM22 (Staf50) is a member of the tripartite motif protein family and has been suggested a role in the regulation of viral replication as well as of protein ubiquitylation. In addition, we have previously shown that TRIM22 is a direct target gene for the tumour suppressor p53. Consistently, over‐expression of TRIM22 inhibits the clonogenic growth of monoblastic U937 cells, suggesting anti‐proliferative or cell death‐inducing effects. RESULTS: Here, we demonstrate that TRIM22 directly or indirectly interacts with the eukaryotic translation initiation factor (eIF)4E, and inhibits the binding of eIF4E to eIF4G, thus disturbing the assembly of the eIF4F complex, which is necessary for cap‐dependent translation. Furthermore, TRIM22 exerts a repressive effect on luciferase reporter protein levels and to some extent on radiolabelled methionine incorporation. Even though all nuclear mRNAs are capped, some are more dependent on eIF4F than others for translation. The translation of one of these mRNAs, IRF‐7C, was indeed found to be repressed in the presence of TRIM22. CONCLUSIONS: Our data suggest TRIM22 to repress protein translation preferably of some specific mRNAs. Taken together, we show that TRIM22 represses translation by inhibiting the binding of eIF4E to eIF4G, suggesting a mechanism for regulation of protein translation, which may be of importance in response to p53 and/or IFN signalling.
has issue date	2012-05-31(xsd:dateTime)
bibo:doi	10.1111/boc.201100099
bibo:pmid	22509910
has license	no-cc
sha1sum (hex)	785e8ce9ed0cb3c8066c30c00d2c3629eeaee2e4
schema:url	https://doi.org/10.1111/boc.201100099
resource representing a document's title	The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G
has PubMed Central identifier	PMC7161774
has PubMed identifier	22509910
schema:publication	Biol Cell
resource representing a document's body	covid:785e8ce9ed0cb3c8066c30c00d2c3629eeaee2e4#body_text
is schema:about of	named entity 'regulation' named entity 'eIF4E' named entity 'REGULATION OF VIRAL REPLICATION' named entity 'ADDITION' named entity 'HAVE' named entity 'EFFECTS' named entity 'P53' named entity 'TRIPARTITE MOTIF' named entity 'PROLIFERATIVE' named entity 'TRIM22' named entity 'tumour suppressor' named entity 'cell' named entity 'protein' named entity 'eIF4G' named entity 'inhibits' named entity 'tumour suppressor' named entity 'U937' named entity 'ubiquitylation' named entity 'IFN' named entity 'protein family' named entity 'over-expression' named entity 'cell death' named entity 'target gene' named entity 'tripartite motif' named entity 'protein' named entity 'TRIM22' named entity 'eIF4G' named entity 'translation initiation factor' named entity 'p53' named entity 'protein' named entity 'cytoplasm' named entity 'TRIM22' named entity 'TRIM22' named entity 'TRIM22' named entity 'biological processes' named entity 'TRIM22' named entity 'proteasome' named entity '293T' named entity 'TRIM22' named entity 'TRIM22' named entity 'intron 1' named entity 'protein synthesis' named entity 'eIF4E' named entity 'molecular weight' named entity 'Assay' named entity 'viral infection' named entity 'protein translation' named entity 'TRIM22' named entity 'methyl' named entity 'TRIM22' named entity 'housekeeping genes' named entity 'kDa' named entity 'mRNAs' named entity 'eGFP' named entity 'translation initiation' named entity 'IRF-7' named entity 'eIF4E' named entity 'IRF-7' named entity 'plasmids' named entity 'protein translation' named entity 'TRIM22' named entity 'TRIM22' named entity 'immunoprecipitation' named entity 'biological processes' named entity '293T' named entity 'p53' named entity 'protein' named entity 'secondary structure' named entity 'cytoplasm' named entity 'nucleus' named entity 'eIF4E' named entity 'cell death' named entity 'TRIM22' named entity 'GAPDH' named entity 'TCA' named entity 'luciferase'

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