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SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
The modification of proteins with SUMO (small ubiquitin-related modifier) plays an important role in determining their functional properties. Importantly though, SUMOylation is a highly dynamic process enabling transient responses to be elicited. This dynamism is controlled by two competing conjugat...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Portland Press Ltd.
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2943748/ https://www.ncbi.nlm.nih.gov/pubmed/20337593 http://dx.doi.org/10.1042/BJ20091948 |
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author | Witty, James Aguilar-Martinez, Elisa Sharrocks, Andrew D. |
author_facet | Witty, James Aguilar-Martinez, Elisa Sharrocks, Andrew D. |
author_sort | Witty, James |
collection | PubMed |
description | The modification of proteins with SUMO (small ubiquitin-related modifier) plays an important role in determining their functional properties. Importantly though, SUMOylation is a highly dynamic process enabling transient responses to be elicited. This dynamism is controlled by two competing conjugating and deconjugating activities. The latter activity is mediated by the SENP [SUMO1/sentrin/SMT3 (suppressor of mif two 3 homologue 1)-specific peptidase] family of SUMO-specific proteases. The transcription factor Elk-1 [ETS (E twenty-six)-like 1] undergoes rapid de-SUMOylation following cellular stimulation with growth factors, and this contributes to its conversion from a SUMO-dependent repressor into a potent transcriptional activator. In the present study we demonstrate an important role for SENP1 in the de-SUMOylation of Elk-1, and therefore an integral role in determining the Elk-1-dependent transcriptional programme. Among the SENPs, Elk-1 preferentially forms a complex with SENP1. This preferential binding is reflected by the higher efficiency of SENP1 in promoting Elk-1 transactivation. Moreover, depletion of SENP1 causes a reciprocal effect and reduces the transactivation properties of Elk-1. Partial redundancy of function with SENP2 is revealed by combinatorial knockdown studies. Importantly, depletion of SENP1 also reduces the activation of the Elk-1 target gene c-FOS. Taken together, these results therefore reveal an important role for SENP1 in the regulation of Elk-1-mediated gene expression in response to mitogenic signalling cues. |
format | Text |
id | pubmed-2943748 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-29437482010-09-23 SENP1 participates in the dynamic regulation of Elk-1 SUMOylation Witty, James Aguilar-Martinez, Elisa Sharrocks, Andrew D. Biochem J Research Article The modification of proteins with SUMO (small ubiquitin-related modifier) plays an important role in determining their functional properties. Importantly though, SUMOylation is a highly dynamic process enabling transient responses to be elicited. This dynamism is controlled by two competing conjugating and deconjugating activities. The latter activity is mediated by the SENP [SUMO1/sentrin/SMT3 (suppressor of mif two 3 homologue 1)-specific peptidase] family of SUMO-specific proteases. The transcription factor Elk-1 [ETS (E twenty-six)-like 1] undergoes rapid de-SUMOylation following cellular stimulation with growth factors, and this contributes to its conversion from a SUMO-dependent repressor into a potent transcriptional activator. In the present study we demonstrate an important role for SENP1 in the de-SUMOylation of Elk-1, and therefore an integral role in determining the Elk-1-dependent transcriptional programme. Among the SENPs, Elk-1 preferentially forms a complex with SENP1. This preferential binding is reflected by the higher efficiency of SENP1 in promoting Elk-1 transactivation. Moreover, depletion of SENP1 causes a reciprocal effect and reduces the transactivation properties of Elk-1. Partial redundancy of function with SENP2 is revealed by combinatorial knockdown studies. Importantly, depletion of SENP1 also reduces the activation of the Elk-1 target gene c-FOS. Taken together, these results therefore reveal an important role for SENP1 in the regulation of Elk-1-mediated gene expression in response to mitogenic signalling cues. Portland Press Ltd. 2010-05-13 2010-06-01 /pmc/articles/PMC2943748/ /pubmed/20337593 http://dx.doi.org/10.1042/BJ20091948 Text en © 2010 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Witty, James Aguilar-Martinez, Elisa Sharrocks, Andrew D. SENP1 participates in the dynamic regulation of Elk-1 SUMOylation |
title | SENP1 participates in the dynamic regulation of Elk-1 SUMOylation |
title_full | SENP1 participates in the dynamic regulation of Elk-1 SUMOylation |
title_fullStr | SENP1 participates in the dynamic regulation of Elk-1 SUMOylation |
title_full_unstemmed | SENP1 participates in the dynamic regulation of Elk-1 SUMOylation |
title_short | SENP1 participates in the dynamic regulation of Elk-1 SUMOylation |
title_sort | senp1 participates in the dynamic regulation of elk-1 sumoylation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2943748/ https://www.ncbi.nlm.nih.gov/pubmed/20337593 http://dx.doi.org/10.1042/BJ20091948 |
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