ArticleThe Journal of biological chemistry2009
SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- The Dynamic Regulation of Daxx-Mediated Transcriptional Inhibition by SUMO and PML NBs.International journal of molecular sciences · 2025Review
- High-throughput discovery and characterization of viral transcriptional effectors in human cells.Cell systems · 2023Article
- Article
- Zinc controls PML nuclear body formation through regulation of a paralog specific auto-inhibition in SUMO1.Nucleic acids research · 2022Article
- Review
- A ceRNA network mediated by LINC00475 in papillary thyroid carcinoma.Open medicine (Warsaw, Poland) · 2022Article
- The distinct roles of zinc finger CCHC-type (ZCCHC) superfamily proteins in the regulation of RNA metabolism.RNA biology · 2021Review
- Crosstalk between MEIS1 and markers of different cell signaling pathways in esophageal squamous cell carcinoma.Molecular biology reports · 2020Article
- ZCCHC12, a novel oncogene in papillary thyroid cancer.Journal of cancer research and clinical oncology · 2017Article
- Aristaless Related Homeobox (ARX) Interacts with β-Catenin, BCL9, and P300 to Regulate Canonical Wnt Signaling.PloS one · 2017Article
- PML, SUMOylation, and Senescence.Frontiers in oncology · 2013Article
- A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulation.The Journal of biological chemistry · 2012Article
- Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search.The Journal of biological chemistry · 2012Article
- ZCCHC12, a potential molecular marker of papillary thyroid carcinoma: a preliminary study.Medical oncology (Northwood, London, England) · 2012Article
- The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies.The Journal of cell biology · 2012Review
- Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin.PLoS pathogens · 2011Article
- Distinctive properties of Arabidopsis SUMO paralogues support the in vivo predominant role of AtSUMO1/2 isoforms.The Biochemical journal · 2011Article
- Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescence-based multiplex assay format.Assay and drug development technologies · 2011Article
- SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability.PloS one · 2011Article
- A small ubiquitin-related modifier-interacting motif functions as the transcriptional activation domain of Krüppel-like factor 4.The Journal of biological chemistry · 2010Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Mutations in Sizn1 (Zcchc12), a novel transcriptional co-activator in the BMP signaling pathway, are associated with X-linked mental retardation. Previously, we demonstrated that Sizn1 positively modulates the BMP signal by interacting with Smad family members and cAMP-responsive element-binding protein-binding protein. To further define the molecular basis of Sizn1 function, we have explored its subcellular localization and generated various deletion mutants to carry out domain analyses. Here, we report that Sizn1 localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs). Sizn1 deletion mutants that disrupt the MA homologous domain or the middle region fail to target to the PML-NB. We show that two SUMO interaction motifs (SIMs) in Sizn1 can bind to SUMO and govern SUMO conjugation to Sizn1 in the absence of the consensus motif for SUMO attachment. Interestingly, the SIM mutant Sizn1 localizes to nuclear bodies, but not to PML-NBs. Thus, SIMs mediate the localization of Sizn1 to PML-NB. Interestingly, mutations in SIM sequences and deletion of the MA homologous domain also affected the transcriptional co-activation function of a Sizn1. Taken together, our data indicate that the SIMs in Sizn1 are required for its PML-NB localization and for the full transcriptional co-activation function in BMP signaling.
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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.