ArticleMolecular cell2009
Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
77 citing papers in PubMed, 127 citations in OpenAlex.
- Molecular basis for the regulation of the SUMOylation activity of the Smc5/6 complex by Esc2.Communications biology · 2026Article
- Rice black-streaked dwarf virus-encoded P6 protein impairs OsPelota-mediated antiviral RNA decay defense via promoting OsSCE1b ubiquitination and degradation in rice.Journal of integrative plant biology · 2025Article
- Structure and Methyl-lysine Binding Selectivity of the HUSH Complex Subunit MPP8.Journal of molecular biology · 2025Article
- Production and Purification of SUMO-UBC9 and SUMO-RANGAP1Methods in molecular biology (Clifton, N.J.) · 2025Article
- Charting the evolutionary path of the SUMO modification system in plants reveals molecular hardwiring of development to stress adaptation.The Plant cell · 2024Review
- UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4.Nature structural & molecular biology · 2024Article
- A SUMO E3 ligase promotes long non-coding RNA transcription to regulate small RNA-directed DNA elimination.eLife · 2024Article
- Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?Pharmacological reviews · 2023Review
- Pervasive SUMOylation of heterochromatin and piRNA pathway proteins.Cell genomics · 2023Article
- Article
- Review
- Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022Review
- Article
- Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.Nature communications · 2021Article
- DNA asymmetry promotes SUMO modification of the single-stranded DNA-binding protein RPA.The EMBO journal · 2021Article
- The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis.EMBO reports · 2021Article
- Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA.Frontiers in plant science · 2021Review
- Review
- SUMO: From Bench to Bedside.Physiological reviews · 2020Review
- Revised annotation and extended characterizations of components of thePlant direct · 2020Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Siz1 is a founding member of the Siz/PIAS RING family of SUMO E3 ligases. The X-ray structure of an active Siz1 ligase revealed an elongated tripartite architecture comprised of an N-terminal PINIT domain, a central zinc-containing RING-like SP-RING domain, and a C-terminal domain we term the SP-CTD. Structure-based mutational analysis and biochemical studies show that the SP-RING and SP-CTD are required for activation of the E2 approximately SUMO thioester, while the PINIT domain is essential for redirecting SUMO conjugation to the proliferating cell nuclear antigen (PCNA) at lysine 164, a nonconsensus lysine residue that is not modified by the SUMO E2 in the absence of Siz1. Mutational analysis of Siz1 and PCNA revealed surfaces on both proteins that are required for efficient SUMO modification of PCNA in vitro and in vivo.
Indexed as
Identifiers
What OpenQuestion holds
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.