ArticleBiology open2016
Non-Smc element 5 (Nse5) of the Smc5/6 complex interacts with SUMO pathway components.
Article in Biology open, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Multi-subunit collaboration enables Smc5/6 to function as a composite SUMO E3 complex.Nature communications · 2026Article
- Structural and mechanistic perspectives on Nse5/6 regulation of the Smc5/6 complex.Frontiers in molecular biosciences · 2026Review
- SMC5/6-mediated plasmid silencing is directed by SIMC1-SLF2 and antagonized by the SV40 large T antigen.eLife · 2025Article
- Article
- Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.Nature communications · 2021Article
- Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding.The EMBO journal · 2021Article
- Integrative analysis reveals unique structural and functional features of the Smc5/6 complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- SUMO is a pervasive regulator of meiosis.eLife · 2021Article
- Relocation of Collapsed Forks to the Nuclear Pore Complex Depends on Sumoylation of DNA Repair Proteins and Permits Rad51 Association.Cell reports · 2020Article
- Recruitment, loading, and activation of the Smc5-Smc6 SUMO ligase.Current genetics · 2019Review
- Brc1 Promotes the Focal Accumulation and SUMO Ligase Activity of Smc5-Smc6 during Replication Stress.Molecular and cellular biology · 2019Article
- Interaction of the Saccharomyces cerevisiae RING-domain protein Nse1 with Nse3 and the Smc5/6 complex is required for chromosome replication and stability.Current genetics · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Smc5/6 complex in Saccharomyces cerevisiae contains six essential non-Smc elements, Nse1-6. With the exception of Nse2 (also known as Mms21), which is an E3 small ubiquitin-like modifier (SUMO) ligase, very little is understood about the role of these components or their contribution to Smc5/6 functionality. Our characterization of Nse5 establishes a previously unidentified relationship between the Smc5/6 complex and factors of the SUMO pathway. Nse5 physically associates with the E2 conjugating enzyme, Ubc9, where contacts are stabilized by non-covalent interactions with SUMO. SUMO also mediates the interactions between Nse5 and the two PIAS family E3 SUMO ligases, Siz1 and Siz2. Cells carrying the nse5-ts1 allele or lacking either SIZ1 or SIZ2 exhibit a reduction in Smc5 sumoylation upon MMS treatment and demonstrate functional redundancy for SUMO mediated events in the presence of DNA damage. Overall, given the extensive connection between Nse5 and components of the SUMO pathway, we speculate that one function of the Smc5/6 complex might be as a scaffold center to enable sumoylation events in budding yeast.
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