title: New roles for old modifications: emerging roles of N-terminal post-translational modifications in development and disease.
abstract: The importance of internal post-translational modification (PTM) in protein signaling and function has long been known and appreciated. However, the significance of the same PTMs on the alpha amino group of N-terminal amino acids has been comparatively understudied. Historically considered static regulators of protein stability, additional functional roles for N-terminal PTMs are now beginning to be elucidated. New findings show that N-terminal methylation, along with N-terminal acetylation, is an important regulatory modification with significant roles in development and disease progression. There are also emerging studies on the enzymology and functional roles of N-terminal ubiquitylation and N-terminal propionylation. Here, will discuss the recent advances in the functional studies of N-terminal PTMs, recount the new N-terminal PTMs being identified, and briefly examine the possibility of dynamic N-terminal PTM exchange.
authors.affiliation: Department of Biochemistry and Molecular Biology, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, Kentucky.
authors.forename: John G
authors.initials: JG
authors.lastname: Tooley
authors.forename: Christine E
authors.initials: CE
authors.lastname: Schaner Tooley
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D004194:Disease; D006801:Humans; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D011506:Proteins
keywords: N-terminal; acetylation; methylation; propionylation; ubiquitylation