ArticleMolecular and cellular biology2010
Phosphorylation-dependent interaction of SATB1 and PIAS1 directs SUMO-regulated caspase cleavage of SATB1.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- SUMOylation-related genes define prognostic subtypes in stomach adenocarcinoma: integrating single-cell analysis and machine learning analyses.Frontiers in immunology · 2025Article
- The homeodomain transcriptional regulator DVE-1 directs a program for synapse elimination during circuit remodeling.Nature communications · 2023Article
- SUMO Modification of Hepatitis B Virus Core Mediates Nuclear Entry, Promyelocytic Leukemia Nuclear Body Association, and Efficient Formation of Covalently Closed Circular DNA.Microbiology spectrum · 2023Article
- A novel SATB1 protein isoform with different biophysical properties.Frontiers in cell and developmental biology · 2023Article
- SATB1-mediated chromatin landscape in T cells.Nucleus (Austin, Tex.) · 2020Review
- Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility.Nature communications · 2020Article
- Review
- A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.Channels (Austin, Tex.) · 2017Article
- SUMOylation of Rb enhances its binding with CDK2 and phosphorylation at early G1 phase.Cell cycle (Georgetown, Tex.) · 2016Article
- Expression and cell distribution of SENP3 in the cerebral cortex after experimental subarachnoid hemorrhage in rats: a pilot study.Cellular and molecular neurobiology · 2015Article
- Control of protein function through optochemical translocation.ACS synthetic biology · 2014Article
- Crystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.The Journal of biological chemistry · 2014Article
- Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.Physiological reviews · 2014Review
- Hematopoiesis in steady-state versus stress: self-renewal, lineage fate choice, and the conversion of danger signals into cytokine signals in hematopoietic stem cells.Journal of immunology (Baltimore, Md. : 1950) · 2014Review
- Article
- The coming of age of phosphoproteomics--from large data sets to inference of protein functions.Molecular & cellular proteomics : MCP · 2013Review
- Phosphorylated SATB1 is associated with the progression and prognosis of glioma.Cell death & disease · 2013Article
- Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein.Oncogene · 2013Article
- An upregulation of SENP3 after spinal cord injury: implications for neuronal apoptosis.Neurochemical research · 2012Article
- The role of nuclear matrix proteins binding to matrix attachment regions (Mars) in prostate cancer cell differentiation.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Special AT-rich sequence-binding protein 1 (SATB1) is a tissue-restricted genome organizer that provides a key link between DNA loop organization, chromatin modification/remodeling, and transcription factor association at matrix attachment regions (MARs). The SUMO E3 ligase PIAS1 enhances SUMO conjugation to SATB1 lysine-744, and this modification regulates caspase-6 mediated cleavage of SATB1 at promyelocytic leukemia nuclear bodies (PML NBs). Since this regulated caspase cleavage occurs on only a subset of SATB1, and the products are relatively stable, proteolysis likely mediates cellular processes other than programmed cell death. However, the mechanism for the spatial and temporal regulation of SATB1 sumoylation and caspase cleavage is not known. Here we report that these processes are controlled by SATB1 phosphorylation; specifically, PIAS1 interaction with SATB1 is inhibited by phosphorylation. Mutagenesis studies identified interaction of the PIAS SAP (scaffold attachment factor-A/B/acinus/PIAS) motif with SATB1 N-terminal sequences. Notably, phosphorylation of SATB1 at threonine-188 regulates its interaction with PIAS1. Sequences near this phosphorylation site, LXXLL (residues 193 to 197), appear to be conserved among a subset of SUMO substrate proteins. Thus, this motif may be commonly involved in interaction with the PIAS SAP, and phosphorylation may similarly inhibit some of these substrates by preventing their interaction with the ligase.
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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.