Modulation of transcriptional corepressor activity of prospero-related homeobox protein (Prox1) by SUMO modification |
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| Authors: | Shan Shi-Fang Wang Lin-Fang Zhai Jian-Wei Qin Yi Ouyang Hua-Fang Kong Yu-Ying Liu Jing Wang Yuan Xie You-Hua |
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| Affiliation: | a Institute of Biochemistry and Cell Biology, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China
b Key Laboratory of Medical Molecular Virology, Institute of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai 200032, China |
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| Abstract: | Prospero-related homeobox protein (Prox1) plays essential roles in the development of many tissues and organs. In the present study, we show that Prox1 is modified by the small ubiquitin-like protein SUMO-1 in cultured cells. Mutation analysis identified at least four potential sumoylation sites within the repression domain of Prox1. Our data indicate that sumoylation of Prox1 reduces its interaction with HDAC3 and as a result downregulates its corepressor activity. These findings suggest that sumoylation may serve as a novel mechanism for the regulation of Prox1’s corepressor activity.Structured summary- MINT-6787569:
- PROX1 (uniprotkb:Q92786) physically interacts (MI:0218) with HDAC3 (uniprotkb:O15379) by anti tag coimmunoprecipitation (MI:0007)
- MINT-6787767:
- PROX1 (uniprotkb:Q92786) physically interacts (MI:0218) with SUMO-1 (uniprotkb:P63165) by anti tag coimmunoprecipitation (MI:0007)
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| Keywords: | DBD, DNA binding domain HDAC, histone deacetylase LRH-1, liver receptor homologue 1 PIAS, protein inhibitor of activated STAT Prox1, prospero-related homeobox SHP, small heterodimer partner SSP3, SUMO-1 specific peptidase 3 SUMO, small ubiquitin-related modifier |
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