title: Protein TAILS: when termini tell tales of proteolysis and function.
abstract: Among the hundreds of posttranslational modifications, limited proteolysis, also known as processing, is special: It is irreversible, near ubiquitous, and by trimming peptide chains from their ends or cutting proteins into two, proteolysis forms shorter chains displaying new termini. The unique chemistry and location of α-amino-termini and carboxyl-termini in a protein engender special chemical and physical properties to a protein. Hence, modification of protein termini is often associated with new biological activities of a protein. We highlight recent proteomic developments enabling high throughput identification of protein termini. This has revolutionized degradomics and protein characterization by mapping the specificity of terminal modifications and of proteases, and has been used to directly identify new protease substrates and molecular pathways altered by proteolysis.
authors.affiliation: University of British Columbia, Department of Oral Biological and Medical Sciences, 4.401 Life Sciences Institute, 2350 Health Sciences Mall, Vancouver, BC, Canada.
authors.forename: Philipp F
authors.initials: PF
authors.lastname: Lange
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Overall
mesh_terms: D000818:Animals; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D010447:Peptide Hydrolases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D059748:Proteolysis; D040901:Proteomics / Q000379:methods*; D013379:Substrate Specificity
chemical_list: D011506:Proteins; D010447:Peptide Hydrolases