GATA4 confers cell type-specific gene expression on genes expressed in cardiovascular, gastro-intestinal, endocrine and neuronal tissues by interacting with various ubiquitous and cell-type-restricted transcriptional regulators. By using yeast two-hybrid screening approach, we have identified PIAS1 as an intestine-expressed GATA4 interacting protein. The physical interaction between GATA4 and PIAS1 was confirmed in mammalian cells by coimmunoprecipitation and two-hybrid analysis. The interacting domains were mapped to the second zinc finger and the adjacent C-terminal basic region of GATA4 and the RING finger and the adjoining C-terminal 60 amino acids of PIAS1. PIAS1 and GATA4 synergistically activated IFABP and SI promoters but not LPH promoters suggesting that PIAS1 differentially activates GATA4 targeted promoters. In primary murine enterocytes PIAS1 was recruited to the GATA4-regulated IFABP promoter. PIAS1 promoted SUMO-1 modification of GATA4 on lysine 366. However, sumoylation was not required for the nuclear localization and stability of GATA4. Further, neither GATA4 sumoylation nor the SUMO ligase activity of PIAS1 was required for coactivation of IFABP promoter by GATA4 and PIAS1. Together, our results demonstrate that PIAS1 is a SUMO ligase for GATA4 that differentially regulates GATA4 transcriptional activity independent of SUMO ligase activity and GATA4 sumoylation.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334497 | PMC |
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0035717 | PLOS |
The human nucleoporin RanBP2/Nup358 interacts with SUMO1-modified RanGAP1 and the SUMO E2 Ubc9 at the nuclear pore complex (NPC) to promote export and disassembly of exportin Crm1/Ran(GTP)/cargo complexes. In mitosis, RanBP2/SUMO1-RanGAP1/Ubc9 remains intact after NPC disassembly and is recruited to kinetochores and mitotic spindles by Crm1 where it contributes to mitotic progression. Interestingly, RanBP2 binds SUMO1-RanGAP1/Ubc9 via motifs that also catalyze SUMO E3 ligase activity.
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January 2025
College of Life Science, Northeast Agricultural University, Harbin 150030, China. Electronic address:
The 26S proteasome is a crucial protease complex responsible for degrading specific proteins to maintain cellular function during salt stress. Previous studies have shown that GmRPN11d, a subunit of the regulatory particle in soybean, is upregulated in response to short-term salt stress. This research discovered that GmRPN11d is localized in the nucleus and cytoplasm, with its expression increasing under high salinity and other stress conditions.
View Article and Find Full Text PDFBreast J
January 2025
Department of Breast and Thyroid Surgery The First Affiliated Hospital of Chongqing Medical University, No. 1 Youyi Rd, Chongqing 400016, China.
Background: The purpose of this study was to analyze SUMO activating enzyme subunit 1 (SAE1) expression in breast cancer (BC). Through bioinformatics analysis and in vitro experiments, the biological function and possibly associated signal pathways of SAE1 in BC were further analyzed.
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Nat Commun
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State Key Laboratory for Animal Disease Control and Prevention, Harbin Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, Harbin, China.
Human ANP32A/B (huANP32A/B) poorly support the polymerase activity of avian influenza viruses (AIVs), thereby limiting interspecies transmission of AIVs from birds to humans. The SUMO-interacting motif (SIM) within NS2 promotes the adaptation of AIV polymerase to huANP32A/B via a yet undisclosed mechanism. Here we show that huANP32A/B are SUMOylated by the E3 SUMO ligase PIAS2α, and deSUMOylated by SENP1.
View Article and Find Full Text PDFFEMS Microbiol Lett
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Department of Biophysics, Yeditepe University School of Medicine, Yeditepe University, Istanbul, Turkey.
Chronological lifespan (CLS) in budding yeast Saccharomyces cerevisiae, which is defined as the time nondividing cells in saturation remain viable, has been utilized as a model to study post-mitotic aging in mammalian cells. CLS is closely related to entry into and maintenance of a quiescent state. Many rearrangements that direct the quiescent state enhance the ability of cells to endure several types of stress.
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