The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation.
The p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in the post-transcriptional regulation of inflammatory genes. p38 has been found to regulate both the translation and the stability of inflammatory mRNAs. The mRNAs regulated by p38 share common AU-rich elements (ARE) pr...
Những tác giả chính: | , , , |
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Định dạng: | Journal article |
Ngôn ngữ: | English |
Được phát hành: |
2004
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_version_ | 1826272180580646912 |
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author | Dean, J Sully, G Clark, A Saklatvala, J |
author_facet | Dean, J Sully, G Clark, A Saklatvala, J |
author_sort | Dean, J |
collection | OXFORD |
description | The p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in the post-transcriptional regulation of inflammatory genes. p38 has been found to regulate both the translation and the stability of inflammatory mRNAs. The mRNAs regulated by p38 share common AU-rich elements (ARE) present in their 3'-untranslated regions. AREs act as mRNA instability determinants but also confer stabilisation of the mRNA by the p38 pathway. In recent years, AREs have shown to be binding sites for numerous proteins including HuR, TTP, AUF1, AUF2, FBP1, FBP2 (KSRP), TIA-1, and TIAR. However, it is unclear which protein is responsible for mRNA stabilisation by p38. This review gives an overview of the major ARE-binding proteins and discusses reasons for and against their involvement in p38-mediated mRNA stabilisation. |
first_indexed | 2024-03-06T22:08:28Z |
format | Journal article |
id | oxford-uuid:50fa8e26-63ac-4cfd-bb96-eec6913dfcb9 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T22:08:28Z |
publishDate | 2004 |
record_format | dspace |
spelling | oxford-uuid:50fa8e26-63ac-4cfd-bb96-eec6913dfcb92022-03-26T16:16:46ZThe involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:50fa8e26-63ac-4cfd-bb96-eec6913dfcb9EnglishSymplectic Elements at Oxford2004Dean, JSully, GClark, ASaklatvala, JThe p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in the post-transcriptional regulation of inflammatory genes. p38 has been found to regulate both the translation and the stability of inflammatory mRNAs. The mRNAs regulated by p38 share common AU-rich elements (ARE) present in their 3'-untranslated regions. AREs act as mRNA instability determinants but also confer stabilisation of the mRNA by the p38 pathway. In recent years, AREs have shown to be binding sites for numerous proteins including HuR, TTP, AUF1, AUF2, FBP1, FBP2 (KSRP), TIA-1, and TIAR. However, it is unclear which protein is responsible for mRNA stabilisation by p38. This review gives an overview of the major ARE-binding proteins and discusses reasons for and against their involvement in p38-mediated mRNA stabilisation. |
spellingShingle | Dean, J Sully, G Clark, A Saklatvala, J The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. |
title | The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. |
title_full | The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. |
title_fullStr | The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. |
title_full_unstemmed | The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. |
title_short | The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. |
title_sort | involvement of au rich element binding proteins in p38 mitogen activated protein kinase pathway mediated mrna stabilisation |
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