Arginine methylation regulates the p53 response.
Activation of the p53 tumour suppressor protein in response to DNA damage leads to apoptosis or cell-cycle arrest. Enzymatic modifications are widely believed to affect and regulate p53 activity. We describe here a level of post-translational control that has an important functional consequence on t...
| Автори: | , , , , , , |
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| Формат: | Journal article |
| Мова: | English |
| Опубліковано: |
2008
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| _version_ | 1826275429566119936 |
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| author | Jansson, M Durant, S Cho, E Sheahan, S Edelmann, M Kessler, B La Thangue, N |
| author_facet | Jansson, M Durant, S Cho, E Sheahan, S Edelmann, M Kessler, B La Thangue, N |
| author_sort | Jansson, M |
| collection | OXFORD |
| description | Activation of the p53 tumour suppressor protein in response to DNA damage leads to apoptosis or cell-cycle arrest. Enzymatic modifications are widely believed to affect and regulate p53 activity. We describe here a level of post-translational control that has an important functional consequence on the p53 response. We show that the protein arginine methyltransferase (PRMT) 5, as a co-factor in a DNA damage responsive co-activator complex that interacts with p53, is responsible for methylating p53. Arginine methylation is regulated during the p53 response and affects the target gene specificity of p53. Furthermore, PRMT5 depletion triggers p53-dependent apoptosis. Thus, methylation on arginine residues is an underlying mechanism of control during the p53 response. |
| first_indexed | 2024-03-06T22:58:34Z |
| format | Journal article |
| id | oxford-uuid:614701b9-78e8-476c-8aab-47c5bd2aa85f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:58:34Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:614701b9-78e8-476c-8aab-47c5bd2aa85f2022-03-26T17:58:45ZArginine methylation regulates the p53 response.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:614701b9-78e8-476c-8aab-47c5bd2aa85fEnglishSymplectic Elements at Oxford2008Jansson, MDurant, SCho, ESheahan, SEdelmann, MKessler, BLa Thangue, NActivation of the p53 tumour suppressor protein in response to DNA damage leads to apoptosis or cell-cycle arrest. Enzymatic modifications are widely believed to affect and regulate p53 activity. We describe here a level of post-translational control that has an important functional consequence on the p53 response. We show that the protein arginine methyltransferase (PRMT) 5, as a co-factor in a DNA damage responsive co-activator complex that interacts with p53, is responsible for methylating p53. Arginine methylation is regulated during the p53 response and affects the target gene specificity of p53. Furthermore, PRMT5 depletion triggers p53-dependent apoptosis. Thus, methylation on arginine residues is an underlying mechanism of control during the p53 response. |
| spellingShingle | Jansson, M Durant, S Cho, E Sheahan, S Edelmann, M Kessler, B La Thangue, N Arginine methylation regulates the p53 response. |
| title | Arginine methylation regulates the p53 response. |
| title_full | Arginine methylation regulates the p53 response. |
| title_fullStr | Arginine methylation regulates the p53 response. |
| title_full_unstemmed | Arginine methylation regulates the p53 response. |
| title_short | Arginine methylation regulates the p53 response. |
| title_sort | arginine methylation regulates the p53 response |
| work_keys_str_mv | AT janssonm argininemethylationregulatesthep53response AT durants argininemethylationregulatesthep53response AT choe argininemethylationregulatesthep53response AT sheahans argininemethylationregulatesthep53response AT edelmannm argininemethylationregulatesthep53response AT kesslerb argininemethylationregulatesthep53response AT lathanguen argininemethylationregulatesthep53response |