ArticleMolecular biology reports2013
SENP2 regulates MEF2A de-SUMOylation in an activity dependent manner.
Article in Molecular biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Review
- Myocyte Enhancer Factor 2A Plays a Central Role in the Regulatory Networks of Cellular Physiopathology.Aging and disease · 2023Review
- The Function of SUMOylation and Its Critical Roles in Cardiovascular Diseases and Potential Clinical Implications.International journal of molecular sciences · 2021Review
- MEF-2 isoforms' (A-D) roles in development and tumorigenesis.Oncotarget · 2019Review
- Sumoylation in Synaptic Function and Dysfunction.Frontiers in synaptic neuroscience · 2016Review
- SENP2 regulates MMP13 expression in a bladder cancer cell line through SUMOylation of TBL1/TBLR1.Scientific reports · 2015Article
- SENP2 regulated the stability of β-catenin through WWOX in hepatocellular carcinoma cell.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- The E3 ligase APC/C-Cdh1 regulates MEF2A-dependent transcription by targeting SUMO-specific protease 2 for ubiquitination and degradation.Cell cycle (Georgetown, Tex.) · 2014Article
- Protein sumoylation in brain development, neuronal morphology and spinogenesis.Neuromolecular medicine · 2013Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SUMOylation has been shown to exert non-negligible influence on transcriptional factors and regulate genes expression by attuning their transcriptional activity. Myocyte-specific enhancer factor-2(MEF2) is a family of transcription factor and play a critical role in embryonic development. The transcriptional activity of MEF2A is highly repressed by SUMOylation in an activity-dependent manner. However, the enzyme that poses de-SUMOylation activity towards MEF2A is still not identified. Here we reported that SENP2 was identified as the major transcriptional dominator and de-SUMOylation enzyme of MEF2A by combining both unbiased shRNA screen and in vivo SUMOylation assays. The SUMOylated form of MEF2A was readily detectable in either SENP2 knockdown cells or knockout embryos. SENP2 markedly enhanced the transcription of MEF2A through directly de-SUMOylation. Moreover, SENP2 protein was accumulated in response to activity-dependent stimuli which in turn mediated activity dependent-regulation of MEF2A de-SUMOylation. Our data clearly show that SENP2 plays an important role in determining the dynamics and functional outcome of MEF2A SUMOylation and transcriptional activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.