title: DeTEKting ubiquitination of APC/C substrates.
abstract: Regulated protein degradation by the ubiquitin-proteasome pathway ensures the unidirectionality of mitotic progression by removing cell-cycle regulators required at earlier stages. The APC/C ubiquitin-protein ligase targets proteins by appending polyubiquitin degradation signals that are subsequently recognized by the 26S proteasome. Reporting in this issue, Jin et al. (2008) identify a TEK motif in both ubiquitin and substrates of APC/C that mediates assembly of these degradation signals.
authors.affiliation: Department of Biochemistry and Molecular Biology, Louisiana State University School of Medicine, New Orleans, LA 70112, USA.
authors.forename: Arthur L
authors.initials: AL
authors.lastname: Haas
authors.forename: Keith D
authors.initials: KD
authors.lastname: Wilkinson
mesh_terms: D020816:Amino Acid Motifs; D064173:Anaphase-Promoting Complex-Cyclosome; D000818:Animals; D006801:Humans; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*; D043743:Ubiquitin-Protein Ligase Complexes / Q000737:chemistry / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D011506:Proteins; D025801:Ubiquitin; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome