title: Profiling of ubiquitin-like modifications reveals features of mitotic control.
abstract: Ubiquitin and ubiquitin-like (Ubl) protein modifications affect protein stability, activity, and localization, but we still lack broad understanding of the functions of Ubl modifications. We have profiled the protein targets of ubiquitin and six additional Ubls in mitosis using a functional assay that utilizes active mammalian cell extracts and protein microarrays and identified 1,500 potential substrates; 80-200 protein targets were exclusive to each Ubl. The network structure is nonrandom, with most targets mapping to a single Ubl. There are distinct molecular functions for each Ubl, suggesting divergent biological roles. Analysis of differential profiles between mitosis and G1 highlighted a previously underappreciated role for the Ubl, FAT10, in mitotic regulation. In addition to its role as a resource for Ubl modifications, our study provides a systematic approach to analyze changes in posttranslational modifications at various cellular states.
authors: Department of Systems Biology, Harvard Medical School, 200 Longwood Avenue, Warren Alpert 536, Boston, MA 02115, USA.
authors: Yifat
authors: Y
authors: Merbl
authors: Phillipe
authors: P
authors: Refour
authors: Hevan
authors: H
authors: Patel
authors: Michael
authors: M
authors: Springer
authors: Marc W
authors: MW
authors: Kirschner
mesh_terms: D006801:Humans; D053858:Metabolic Networks and Pathways; D008938:Mitosis; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D020543:Proteome / Q000032:analysis*; D025801:Ubiquitin / Q000378:metabolism; D014452:Ubiquitins / Q000378:metabolism
chemical_list: D011506:Proteins; D020543:Proteome; C109184:UBD protein, human; D025801:Ubiquitin; D014452:Ubiquitins