The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G.
(2012) In Biology of the Cell 104(8). p.462-475- Abstract
- BACKGROUND INFORMATION: The interferon-inducible protein TRIM22 (Staf50) is a member of the TRIM protein family and has been suggested a role in the regulation of viral replication as well as of protein ubiquitylation. Additionally, we have previously shown that TRIM22 is a direct target gene for the tumour suppressor p53. Consistently, overexpression 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 translation initiation factor eIF4E, and inhibits the binding of eIF4E to eIF4G, thus disturbing the assembly of the eIF4F complex, which is necessary for... (More) - BACKGROUND INFORMATION: The interferon-inducible protein TRIM22 (Staf50) is a member of the TRIM protein family and has been suggested a role in the regulation of viral replication as well as of protein ubiquitylation. Additionally, we have previously shown that TRIM22 is a direct target gene for the tumour suppressor p53. Consistently, overexpression 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 translation initiation factor eIF4E, 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2519339
- author
- Petersson, Jessica LU ; Ageberg, Malin LU ; Sandén, Carl LU ; Olofsson, Tor LU ; Gullberg, Urban LU and Drott, Kristina LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biology of the Cell
- volume
- 104
- issue
- 8
- pages
- 462 - 475
- publisher
- Portland Press
- external identifiers
-
- wos:000307049000005
- pmid:22509910
- scopus:84864766957
- ISSN
- 0248-4900
- DOI
- 10.1111/boc.201100099
- language
- English
- LU publication?
- yes
- id
- b0e9a6ed-e73d-4e41-bfac-3da52f31a00a (old id 2519339)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/22509910?dopt=Abstract
- date added to LUP
- 2016-04-04 08:54:13
- date last changed
- 2022-01-29 07:34:11
@article{b0e9a6ed-e73d-4e41-bfac-3da52f31a00a, abstract = {{BACKGROUND INFORMATION: The interferon-inducible protein TRIM22 (Staf50) is a member of the TRIM protein family and has been suggested a role in the regulation of viral replication as well as of protein ubiquitylation. Additionally, we have previously shown that TRIM22 is a direct target gene for the tumour suppressor p53. Consistently, overexpression of TRIM22 inhibits the clonogenic growth of monoblastic U937 cells, suggesting anti-proliferative or cell death-inducing effects. <br/><br> <br/><br> RESULTS: Here, we demonstrate that TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E, 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. <br/><br> <br/><br> 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.}}, author = {{Petersson, Jessica and Ageberg, Malin and Sandén, Carl and Olofsson, Tor and Gullberg, Urban and Drott, Kristina}}, issn = {{0248-4900}}, language = {{eng}}, number = {{8}}, pages = {{462--475}}, publisher = {{Portland Press}}, series = {{Biology of the Cell}}, title = {{The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G.}}, url = {{http://dx.doi.org/10.1111/boc.201100099}}, doi = {{10.1111/boc.201100099}}, volume = {{104}}, year = {{2012}}, }