Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity
| Autor: | Guillaume Bossis, M Brunet Simioni, Jacques Landry, Carmen Garrido, A de Thonel, Marc Piechaczyk, A Bouchot, Eric Fourmaux, Arlette Hammann, Anne-Laure Joly |
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| Přispěvatelé: | Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Protein sumoylation
Transcriptional Activation Cancer Research endocrine system animal structures SUMO protein HSP27 Heat-Shock Proteins Biology urologic and male genital diseases environment and public health Substrate Specificity 03 medical and health sciences Transactivation 0302 clinical medicine Heat Shock Transcription Factors Heat shock protein Genetics Animals Humans Animals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology HSF1 Protein Structure Quaternary Molecular Biology Transcription factor Ubiquitins Heat-Shock Proteins 030304 developmental biology Cell Nucleus 0303 health sciences Molecular biology Hsp70 Cell biology Heat shock factor DNA-Binding Proteins Protein Transport Quaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism 030220 oncology & carcinogenesis embryonic structures Small Ubiquitin-Related Modifier Proteins Protein Multimerization HeLa Cells Molecular Chaperones Transcription Factors |
| Zdroj: | Oncogene Oncogene, Nature Publishing Group, 2009, 28 (37), pp.3332--44. ⟨10.1038/onc.2009.188⟩ |
| ISSN: | 0950-9232 1476-5594 |
| DOI: | 10.1038/onc.2009.188⟩ |
| Popis: | Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsible for HSP expression, is one of the targets of HSP27. In stressed cells, HSP27 enters the nucleus and, in the form of large oligomers, binds to HSF1 and induces its modification by SUMO-2/3 on lysine 298. HSP27-induced HSF1 modification by SUMO-2/3 takes place downstream of the transcription factor phosphorylation on S303 and S307 and does not affect its DNA-binding ability. In contrast, this modification blocks HSF1 transactivation capacity. These data show that HSP27 exerts a feedback inhibition of HSF1 transactivation and enlighten the strictly regulated interplay between HSPs and HSF1. As we also show that HSP27 binds to the SUMO-E2-conjugating enzyme, Ubc9, our study raises the possibility that HSP27 may act as a SUMO-E3 ligase specific for SUMO-2/3. |
| Databáze: | OpenAIRE |
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