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Morphogen-induced kinase condensates transduce Hh signal by allosterically activating Gli.
Sci Adv
January 2025
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Hedgehog (Hh) morphogen governs embryonic development and tissue homeostasis through the Ci/Gli family transcription factors. Here we report that Hh induces phase separation of the fused (Fu)/Ulk family kinases to allosterically regulate Ci/Gli. We find that Hh-induced phosphorylation of Fu/Ulk3 promotes SUMOylation of their inverted phosphorylation-dependent SUMOylation motifs.
View Article and Find Full Text PDFThe fission yeast SUMO-targeted ubiquitin ligase Slx8 functionally associates with clustered centromeres and the silent mating-type region at the nuclear periphery.
Biol Open
December 2024
Institut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
The SUMO-targeted ubiquitin ligase (STUbL) family is involved in multiple cellular processes via a wide range of mechanisms to maintain genome stability. One of the evolutionarily conserved functions of STUbL is to promote changes in the nuclear positioning of DNA lesions, targeting them to the nuclear periphery. In Schizossacharomyces pombe, the STUbL Slx8 is a regulator of SUMOylated proteins and promotes replication stress tolerance by counteracting the toxicity of SUMO conjugates.
View Article and Find Full Text PDFSENP3: Cancers and diseases.
Biochim Biophys Acta Rev Cancer
January 2025
Kunming University of Science and Technology, Medical School, Kunming 650500, China.
SUMOylation is a protein modification process that involves the covalent attachment of a small ubiquitin-like modifier (SUMO) to a specific lysine residue on the target protein. This modification can influence the function, localization, stability, and interactions of proteins, thereby regulating various cellular processes. Altering the SUMOylation of certain proteins is expected to be a potential approach for treating specific cancers and diseases.
View Article and Find Full Text PDFSUMO1 modification reduces oxidative stress and SUMO1ylated AKAP4 degradation affects frozen-thawed boar sperm quality.
Anim Reprod Sci
December 2024
Department of Animal Science, College of Agriculture, Yanbian University, Yanji, Jilin Province, China. Electronic address:
Low-temperature injury affects normal physiological function and viability of boar sperm during cryopreservation. Small ubiquitin-like modifier (SUMO) modification of proteins after translation is related to the cell stress response but the relationship between SUMO modification and oxidative stress in freeze-thawed sperm remains unclear. A-kinase ankyrin 4 (AKAP4) and its precursor proAKAP4 are two main proteins in mammalian sperm.
View Article and Find Full Text PDFLethal Phenotype and Expansion of the Clinical Spectrum of Biallelic Loss of Function Variant in SENP7 Gene Unveiled by Whole Exome Sequencing.
Clin Genet
January 2025
Prenatal Diagnosis and Fetal Medicine Department, Human Genetics and Genome Research Institute, National Research Centre (NRC), Cairo, Egypt.
SUMOylation involves covalent attachment of small ubiquitin-like modifier (SUMO) proteins to specific lysine residues on target proteins and regulates various aspects of their function. Sentrin-specific proteases (SENPs) are key players in both the conjugation reaction of SUMO proteins to their targets and the subsequent deconjugation of SUMO-conjugated substrates. Here, we provide the first comprehensive prenatal description of a lethal syndrome linked to a novel homozygous stop-gain variant in SENP7 c.
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