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HDAC6 regulates antibody-dependent intracellular neutralization of viruses via deacetylation of TRIM21

J Biol Chem. 2020; 
Songbo Xie, Linlin Zhang, Dan Dong, Ruixin Ge, Qianqian He, Cunxian Fan, Wei Xie, Jun Zhou, Dengwen Li, Min Liu
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Mutagenesis Services … The deletion mutants of Flag-TRIM21 were directly synthesized and inserted into pcDNA3-HA vector by Genscript (Nanjing, China), and the K/R point mutations were generated by PCR and site-directed mutagenesis with pcDNA3-Flag-TRIM21 as a template … Get A Quote

摘要

Tripartite motif-containing protein 21 (TRIM21) is a cytosolic antibody receptor that targets the internalized virus-antibody complex to the proteasome for degradation. However, the precise mechanism regulating TRIM21 activity is unknown. Here we show that TRIM21 is a substrate of histone deacetylase 6 (HDAC6) and that its function is regulated by acetylation. HDAC6 interacts with TRIM21 through its PRYSPRY motif and deacetylates TRIM21 at lysine 385 and lysine 387, thus promoting its homodimerization. Inhibiting HDAC6 activity increases TRIM21 acetylation, and hyperacetylation blocks TRIM21 dimerization and ubiquitination, preventing its binding to the virus-antibody complex and its degradation via the ubiquit... More

关键词

TRIM21, acetylation, antibody-dependent intracellular neutralization, histone deacetylase 6 (HDAC6), infection, ubiquitin, virus