The disordered regions of the methyltransferase SETD2 govern its function by regulating its proteolysis and phase separation
Author:
Funder
National Institute of General Medical Sciences
Stowers Institute for Medical Research
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference81 articles.
1. Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes;Venkatesh;Nature,2012
2. The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation;Dhayalan;J. Biol. Chem.,2010
3. SETD2-dependent histone H3K36 trimethylation is required for homologous recombination repair and genome stability;Pfister;Cell Rep.,2014
4. The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSα;Li;Cell,2013
5. Histone methyltransferase SETD2 modulates alternative splicing to inhibit intestinal tumorigenesis;Yuan;J. Clin. Invest.,2017
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1. Phase Separation of Chromatin Structure-related Biomolecules: A Driving Force for Epigenetic Regulations;Current Protein & Peptide Science;2024-09
2. Catalytic activity of Setd2 is essential for embryonic development in mice: establishment of a mouse model harboring patient-derived Setd2 mutation;Frontiers of Medicine;2024-08-08
3. Set2 regulates Ccp1 and Swc2 to ensure centromeric stability by retargeting CENP-A;Nucleic Acids Research;2024-03-05
4. Protein phase separation disorder as a potentially pervasive pathogenic mechanism of male infertility;Medical Hypotheses;2023-12
5. SETD2 maintains nuclear lamina stability to safeguard the genome;2023-09-29
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