Send to

Choose Destination
Bioessays. 2005 Mar;27(3):242-6.

PAD: the smoking gun behind arginine methylation signaling?

Author information

Biochemical Molecular Neurobiology Laboratory, Department of Molecular Biology, New York State Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, NY 10314, USA.


Post-translational modifications (PTM) supply the proteome with functional and regulatory diversity. Modifications including phosphorylation, acetylation and methylation have been identified in eucaryotic proteins. For all but the last, corresponding "de-modifying" enzymes exist to remove the PTM tag returning the protein to its basal state. Recently, a novel mechanism in which peptidylarginine deiminase (PAD4) converts histone H3 and H4 methyl arginine residues into citrulline was proposed to regulate estrogen-responsive gene transcription.1,2 These data, the first to provide a mechanistic basis for the dynamic changes observed in a subset of protein arginine methylated substrates,3 lead to a host of questions concerning the generality of this mechanism for non-histone targets of the protein arginine methyltransferases (PRMTs).

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center