tetano
Editor, Senior Moderator
J Biol Chem. 2013 Oct 15. [Epub ahead of print]
Negative Regulation of Interferon-Induced Transmembrane Protein 3 by SET7-mediated Lysine Monomethylation.
Shan Z, Han Q, Nie J, Cao X, Chen Z, Yin S, Gao Y, Lin F, Zhou X, Xu K, Fan H, Qian Z, Sun B, Zhong J, Li B, Tsun A.
Source
Institut Pasteur of Shanghai, China;
Abstract
Although lysine methylation is classically known to regulate histone function, its role in modulating antiviral restriction factor activity remains uncharacterized. Interferon-induced transmembrane protein 3 (IFITM3) was found monomethylated on its lysine-88 residue (IFITM3-K88me1) to reduce its antiviral activity, mediated by the lysine methyltransferase SET7. Vesicular Stomatitis virus (VSV) and Influenza A virus (IAV) infection increased IFITM3-K88me1 levels by promoting the interaction between IFITM3 and SET7, suggesting that this pathway could be hijacked to support infection; conversely, IFN-α reduced IFITM3-K88me1 levels. These findings may have important implications in the design of therapeutics targeting protein methylation against infectious diseases.
KEYWORDS:
Antiviral agents, Antiviral host restriction factors, Host defense, Host-pathogen interactions, IFITM3, Lysine methylation, Post translational modification, Protein methylation, SET7
PMID:
24129573
[PubMed - as supplied by publisher]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/24129573
Negative Regulation of Interferon-Induced Transmembrane Protein 3 by SET7-mediated Lysine Monomethylation.
Shan Z, Han Q, Nie J, Cao X, Chen Z, Yin S, Gao Y, Lin F, Zhou X, Xu K, Fan H, Qian Z, Sun B, Zhong J, Li B, Tsun A.
Source
Institut Pasteur of Shanghai, China;
Abstract
Although lysine methylation is classically known to regulate histone function, its role in modulating antiviral restriction factor activity remains uncharacterized. Interferon-induced transmembrane protein 3 (IFITM3) was found monomethylated on its lysine-88 residue (IFITM3-K88me1) to reduce its antiviral activity, mediated by the lysine methyltransferase SET7. Vesicular Stomatitis virus (VSV) and Influenza A virus (IAV) infection increased IFITM3-K88me1 levels by promoting the interaction between IFITM3 and SET7, suggesting that this pathway could be hijacked to support infection; conversely, IFN-α reduced IFITM3-K88me1 levels. These findings may have important implications in the design of therapeutics targeting protein methylation against infectious diseases.
KEYWORDS:
Antiviral agents, Antiviral host restriction factors, Host defense, Host-pathogen interactions, IFITM3, Lysine methylation, Post translational modification, Protein methylation, SET7
PMID:
24129573
[PubMed - as supplied by publisher]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/24129573