title: Interfacing protein lysine acetylation and protein phosphorylation: ancient modifications meet on ancient proteins.
abstract: Recognition that different protein covalent modifications can operate in concert to regulate a single protein has forced us to re-think the relationship between amino acid side chain modifications and protein function. Results presented by Tran et al. 2012 demonstrate the association of a protein phosphatase (PP2A) with a histone/lysine deacetylase (HDA14) on plant microtubules along with a histone/lysine acetyltransferase (ELP3). This finding reveals a regulatory interface between two prevalent covalent protein modifications, protein phosphorylation and acetylation, emphasizing the integrated complexity of post-translational protein regulation found in nature.
authors: University of Calgary, Department of Biological Sciences, Calgary, AB Canada.
authors: Hue T
authors: HT
authors: Tran
authors: R Glen
authors: RG
authors: Uhrig
authors: Mhairi
authors: M
authors: Nimick
authors: Greg B
authors: GB
authors: Moorhead
mesh_terms: D000107:Acetylation; D049452:Green Fluorescent Proteins / Q000378:metabolism; D008239:Lysine / Q000378:metabolism*; D010766:Phosphorylation; D018515:Plant Leaves / Q000166:cytology / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D031307:Vicia faba / Q000166:cytology / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D049452:Green Fluorescent Proteins; D008239:Lysine