ArticleThe Journal of biological chemistry2014
High mobility group nucleosomal binding domain 2 (HMGN2) SUMOylation by the SUMO E3 ligase PIAS1 decreases the binding affinity to nucleosome core particles.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Central gene transcriptional regulatory networks shaping monocyte development in bone marrow.Frontiers in immunology · 2022Article
- High Mobility Group Proteins in Sepsis.Frontiers in immunology · 2022Review
- Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2-nucleosome association.RSC chemical biology · 2021Article
- A Tale of Usurpation and Subversion: SUMO-Dependent Integrity of Promyelocytic Leukemia Nuclear Bodies at the Crossroad of Infection and Immunity.Frontiers in cell and developmental biology · 2021Review
- Revisiting promyelocytic leukemia protein targeting by human cytomegalovirus immediate-early protein 1.PLoS pathogens · 2020Article
- A deficiency in SUMOylation activity disrupts multiple pathways leading to neural tube and heart defects in Xenopus embryos.BMC genomics · 2019Article
- Effect of HMGN2 on proliferation and apoptosis of MCF-7 breast cancer cells.Oncology letters · 2019Article
- Chromatin regulates IL-33 release and extracellular cytokine activity.Nature communications · 2018Article
- The modulation of MiR-155 and MiR-23a manipulates Klebsiella pneumoniae Adhesion on Human pulmonary Epithelial cells via Integrin α5β1 Signaling.Scientific reports · 2016Article
- Functional characterization of DnSIZ1, a SIZ/PIAS-type SUMO E3 ligase from Dendrobium.BMC plant biology · 2015Article
- Evolution of high mobility group nucleosome-binding proteins and its implications for vertebrate chromatin specialization.Molecular biology and evolution · 2015Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High mobility group nucleosomal binding domain 2 (HMGN2) is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair. In addition, it may have other roles in antimicrobial activity, cell homing, and regulating cytokine release. Although the biochemical properties of HMGN2 protein are regulated by acetylation and phosphorylation, it is not yet known whether HMGN2 activity can also be regulated by SUMOylation. In this study, we demonstrated for the first time that HMGN2 is modified by covalent attachment of small ubiquitin-related modifier 1 (SUMO1) by pro-inflammatory signal and identified the major SUMOylated lysine residues that localize to the HMGN2 nucleosome-binding domain at Lys-17 and Lys-35. SENP1 can deSUMOylate SUMOylated HMGN2, and PIAS1 is the E3 ligase responsible for SUMOylation of HMGN2. Finally, using SUMO1-conjugated HMGN2 purified from a basal SUMOylation system in Escherichia coli, we demonstrated that SUMOylated HMGN2 has decreased the binding affinity to nucleosome core particles in comparison to unSUMOylated HMGN2. These observations potentially provide new perspectives for understanding the functions of HMGN2 in inflammatory reaction.
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