ArticleThe Journal of biological chemistry2011
Small ubiquitin-like modifier (SUMO) conjugation impedes transcriptional silencing by the polycomb group repressor Sex Comb on Midleg.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Loss of SUMOylation drives aberrant PRC1 clustering and 3D genome rewiring independent of H3K27me3.Nucleic acids research · 2026Article
- SUMOylation and Viral Infections of the Brain.Pathogens (Basel, Switzerland) · 2022Review
- Article
- SUMOylation in development and neurodegeneration.Development (Cambridge, England) · 2020Review
- Article
- Regulation of transcription factors by sumoylation.Transcription · 2017Review
- Regulation of Smoothened Trafficking and Hedgehog Signaling by the SUMO Pathway.Developmental cell · 2016Article
- SUMO-Enriched Proteome for Drosophila Innate Immune Response.G3 (Bethesda, Md.) · 2015Article
- Sex comb on midleg (Scm) is a functional link between PcG-repressive complexes in Drosophila.Genes & development · 2015Article
- Are we there yet? Initial targeting of the Male-Specific Lethal and Polycomb group chromatin complexes in Drosophila.Open biology · 2014Review
- Regulation of Toll signaling and inflammation by β-arrestin and the SUMO protease Ulp1.Genetics · 2013Article
- SUMO: a multifaceted modifier of chromatin structure and function.Developmental cell · 2013Review
- Article
- SUMOylation in Drosophila Development.Biomolecules · 2012Article
- Emerging roles of the SUMO pathway in development.Cellular and molecular life sciences : CMLS · 2011Review
- RpL22e, but not RpL22e-like-PA, is SUMOylated and localizes to the nucleoplasm of Drosophila meiotic spermatocytes.Nucleus (Austin, Tex.)Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Drosophila protein Sex Comb on Midleg (Scm) is a member of the Polycomb group (PcG), a set of transcriptional repressors that maintain silencing of homeotic genes during development. Recent findings have identified PcG proteins both as targets for modification by the small ubiquitin-like modifier (SUMO) protein and as catalytic components of the SUMO conjugation pathway. We have found that the SUMO-conjugating enzyme Ubc9 binds to Scm and that this interaction, which requires the Scm C-terminal sterile α motif (SAM) domain, is crucial for the efficient sumoylation of Scm. Scm is associated with the major Polycomb response element (PRE) of the homeotic gene Ultrabithorax (Ubx), and efficient PRE recruitment requires an intact Scm SAM domain. Global reduction of sumoylation augments binding of Scm to the PRE. This is likely to be a direct effect of Scm sumoylation because mutations in the SUMO acceptor sites in Scm enhance its recruitment to the PRE, whereas translational fusion of SUMO to the Scm N terminus interferes with this recruitment. In the metathorax, Ubx expression promotes haltere formation and suppresses wing development. When SUMO levels are reduced, we observe decreased expression of Ubx and partial haltere-to-wing transformation phenotypes. These observations suggest that SUMO negatively regulates Scm function by impeding its recruitment to the Ubx major PRE.
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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.