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

Petersson, Jessica LU ; Ageberg, Malin LU ; Sandén, Carl LU ; Olofsson, Tor LU ; Gullberg, Urban LU and Drott, Kristina LU (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)
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author
organization
publishing date
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
2012-05-06 17:30:01
date last changed
2017-07-09 04:34:36
@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},
  volume       = {104},
  year         = {2012},
}