PAD: the smoking gun behind arginine methylation signaling?
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).
Denman
Robert B
RB
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. rbdenman@yahoo.com
D000818:Animals; D001120:Arginine / Q000378:metabolism*; D006801:Humans; D006867:Hydrolases / Q000378:metabolism*; D008745:Methylation; D011499:Protein Processing, Post-Translational; D000080002:Protein-Arginine Deiminase Type 4; D000076342:Protein-Arginine Deiminases; D015398:Signal Transduction
D001120:Arginine; D006867:Hydrolases; C000629235:PADI4 protein, human; D000080002:Protein-Arginine Deiminase Type 4; D000076342:Protein-Arginine Deiminases