No full text
Article (Scientific journals)
Are STATS arginine-methylated?
Komyod, W.; Bauer, U. M.; Heinrich, P. C. et al.
2005In Journal of Biological Chemistry, 280 (23), p. 21700-5
Peer Reviewed verified by ORBi
 

Files


Full Text
No document available.

Send to



Details



Keywords :
1-Phosphatidylinositol 3-Kinase; Mice; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oncostatin M; Peptides; Plasmids; Protein Structure, Tertiary; Receptors, Interleukin-6; Recombinant Fusion Proteins; Recombinant Proteins; STAT1 Transcription Factor; STAT3 Transcription Factor; Signal Transduction; Trans-Activators; Transfection; Tyrosine; Methyltransferases; Methylation; Animals; Arginine; Blotting, Western; Cell Line, Tumor; DNA-Binding Proteins; Extracellular Signal-Regulated MAP Kinases; Fibrosarcoma; Gene Expression Regulation, Neoplastic; Genes, Reporter; Glutathione Transferase; Humans; Immunoprecipitation; Interferon-alpha; Interferons; Interleukin-6; Lysine; Melanoma; p38 Mitogen-Activated Protein Kinases
Abstract :
[en] Transcription factors of the STAT (signal transducer and activator of transcription) family are important in signal transduction of cytokines. They are subject to post-translational modification by phosphorylation on tyrosine and serine residues. Recent evidence suggested that STATs are methylated on a conserved arginine residue within the N-terminal region. STAT arginine methylation has been described to be important for STAT function and loss of arginine methylation was discussed to be involved in interferon resistance of cancer cells. Here we provide several independent lines of evidence indicating that the issue of arginine methylation of STATs has to be reassessed. First, we show that treatment of melanoma and fibrosarcoma cells with inhibitors used to suppress methylation (N-methyl-2-deoxyadenosine, adenosine, dl-homocysteine) had profound and rapid effects on phosphorylation of STAT1 and STAT3 but also on p38 and Erk signaling cascades which are known to cross-talk with the Jak/STAT pathway. Second, we show that anti-methylarginine antibodies did not precipitate specifically STAT1 or STAT3. Third, we show that mutation of Arg(31) to Lys led to destabilization of STAT1 and STAT3, implicating an important structural role of Arg(31). Finally, purified catalytically active protein arginine methyltransferases (PRMT1, -2, -3, -4, and -6) did not methylate STAT proteins, and cotransfection with PRMT1 did not affect STAT1-controlled reporter gene activity. Taken together, our data suggest the absence of arginine methylation of STAT1 and STAT3.
Disciplines :
Biochemistry, biophysics & molecular biology
Identifiers :
UNILU:UL-ARTICLE-2008-707
Author, co-author :
Komyod, W.
Bauer, U. M.
Heinrich, P. C.
Haan, Serge ;  Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > Institute for Biochemistry
Behrmann, Iris ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
External co-authors :
yes
Language :
English
Title :
Are STATS arginine-methylated?
Publication date :
2005
Journal title :
Journal of Biological Chemistry
ISSN :
1083-351X
Publisher :
American Society for Biochemistry and Molecular Biology, Baltimore, United States - Maryland
Volume :
280
Issue :
23
Pages :
21700-5
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBilu :
since 26 April 2013

Statistics


Number of views
69 (1 by Unilu)
Number of downloads
0 (0 by Unilu)

Scopus citations®
 
63
Scopus citations®
without self-citations
58
WoS citations
 
61

Bibliography


Similar publications



Contact ORBilu