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| http://dx.doi.org/10.18632/oncotarget.4605 | DOI Listing |
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Cancer-associated DAXX mutations reveal a critical role for ATRX localization in ALT suppression.
bioRxiv
November 2024
Genetics Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
To maintain genome stability, proliferating cells must enact a program of telomere maintenance. While most tumors maintain telomeres through the action of telomerase, a subset of tumors utilize a DNA-templated process termed Alternative Lengthening of Telomeres or ALT. ALT is associated with mutations in the ATRX/DAXX/H3.
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
February 2025
Kunming University of Science and Technology, Medical School, Kunming 650500, China. Electronic address:
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
February 2025
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.
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