ArticleThe Journal of biological chemistry2015
SUMOylation regulates polo-like kinase 1-interacting checkpoint helicase (PICH) during mitosis.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- SUMOylation is destined for regulatory T cell-related immune dysregulation.Cell death discovery · 2026Review
- Ubiquitination in cancer: mechanisms and therapeutic opportunities.Cancer communications (London, England) · 2025Review
- PICH impacts the spindle assembly checkpoint via its DNA translocase and SUMO-interaction activities.Life science alliance · 2025Article
- The interplay of the translocase activity and protein recruitment function of PICH in ultrafine anaphase bridge resolution and genomic stability.Nucleic acids research · 2025Article
- The SUMO-NIP45 pathway processes toxic DNA catenanes to prevent mitotic failure.Nature structural & molecular biology · 2023Article
- Regulation of mitotic chromosome architecture and resolution of ultrafine anaphase bridges by PICH.Cell cycle (Georgetown, Tex.) · 2021Article
- Membrane-cytoplasm translocation of annexin A4 is involved in the metastasis of colorectal carcinoma.Aging · 2021Article
- PICH regulates the abundance and localization of SUMOylated proteins on mitotic chromosomes.Molecular biology of the cell · 2020Article
- Review
- A Flp-SUMO hybrid recombinase reveals multi-layered copy number control of a selfish DNA element through post-translational modification.PLoS genetics · 2019Article
- SUMO targets the APC/C to regulate transition from metaphase to anaphase.Nature communications · 2018Article
- Article
- Non-Catalytic Roles of the Topoisomerase IIα C-Terminal Domain.International journal of molecular sciences · 2017Review
- Resolving Chromatin Bridges With SIMs, SUMOs and PICH.Cell cycle (Georgetown, Tex.) · 2016Article
- SUMO-interacting motifs (SIMs) in Polo-like kinase 1-interacting checkpoint helicase (PICH) ensure proper chromosome segregation during mitosis.Cell cycle (Georgetown, Tex.) · 2016Article
- SUMOylation of DNA topoisomerase IIα regulates histone H3 kinase Haspin and H3 phosphorylation in mitosis.The Journal of cell biology · 2016Article
- Sumoylation of TCF21 downregulates the transcriptional activity of estrogen receptor-alpha.Oncotarget · 2016Article
- SUMOylation-Mediated Regulation of Cell Cycle Progression and Cancer.Trends in biochemical sciences · 2015Review
- SUMO-mediated regulation of DNA damage repair and responses.Trends in biochemical sciences · 2015Review
- SUMOylation of the C-terminal domain of DNA topoisomerase IIα regulates the centromeric localization of Claspin.Cell cycle (Georgetown, Tex.) · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mitotic SUMOylation has an essential role in faithful chromosome segregation in eukaryotes, although its molecular consequences are not yet fully understood. In Xenopus egg extract assays, we showed that poly(ADP-ribose) polymerase 1 (PARP1) is modified by SUMO2/3 at mitotic centromeres and that its enzymatic activity could be regulated by SUMOylation. To determine the molecular consequence of mitotic SUMOylation, we analyzed SUMOylated PARP1-specific binding proteins. We identified Polo-like kinase 1-interacting checkpoint helicase (PICH) as an interaction partner of SUMOylated PARP1 in Xenopus egg extract. Interestingly, PICH also bound to SUMOylated topoisomerase IIα (TopoIIα), a major centromeric small ubiquitin-like modifier (SUMO) substrate. Purified recombinant human PICH interacted with SUMOylated substrates, indicating that PICH directly interacts with SUMO, and this interaction is conserved among species. Further analysis of mitotic chromosomes revealed that PICH localized to the centromere independent of mitotic SUMOylation. Additionally, we found that PICH is modified by SUMO2/3 on mitotic chromosomes and in vitro. PICH SUMOylation is highly dependent on protein inhibitor of activated STAT, PIASy, consistent with other mitotic chromosomal SUMO substrates. Finally, the SUMOylation of PICH significantly reduced its DNA binding capability, indicating that SUMOylation might regulate its DNA-dependent ATPase activity. Collectively, our findings suggest a novel SUMO-mediated regulation of the function of PICH at mitotic centromeres.
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