{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Klebba JE"],"funding":["Intramural NIH HHS","NCI NIH HHS","PHS HHS"],"pagination":["2255-2261"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3844517"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(22)"],"pubmed_abstract":["Polo-like kinase 4 (Plk4) is a conserved master regulator of centriole assembly. Previously, we found that Drosophila Plk4 protein levels are actively suppressed during interphase. Degradation of interphase Plk4 prevents centriole overduplication and is mediated by the ubiquitin-ligase complex SCF(Slimb/βTrCP). Since Plk4 stability depends on its activity, we studied the consequences of inactivating Plk4 or perturbing its phosphorylation state within its Slimb-recognition motif (SRM). Mass spectrometry of in-vitro-phosphorylated Plk4 and Plk4 purified from cells reveals that it is directly responsible for extensively autophosphorylating and generating its Slimb-binding phosphodegron. Phosphorylatable residues within this regulatory region were systematically mutated to determine their impa"],"journal":["Current biology : CB"],"pubmed_title":["Polo-like kinase 4 autodestructs by generating its Slimb-binding phosphodegron."],"pmcid":["PMC3844517"],"funding_grant_id":["ZIA HL006104","P50 CA95060","P30 CA023074","1ZIAHL006104","P50 CA095060","ZIA HL006104-03"],"pubmed_authors":["Buster DW","Swatkoski S","Rusan NM","Klebba JE","Rogers GC","Gucek M","Nguyen AL"],"additional_accession":[]},"is_claimable":false,"name":"Polo-like kinase 4 autodestructs by generating its Slimb-binding phosphodegron.","description":"Polo-like kinase 4 (Plk4) is a conserved master regulator of centriole assembly. Previously, we found that Drosophila Plk4 protein levels are actively suppressed during interphase. Degradation of interphase Plk4 prevents centriole overduplication and is mediated by the ubiquitin-ligase complex SCF(Slimb/βTrCP). Since Plk4 stability depends on its activity, we studied the consequences of inactivating Plk4 or perturbing its phosphorylation state within its Slimb-recognition motif (SRM). Mass spectrometry of in-vitro-phosphorylated Plk4 and Plk4 purified from cells reveals that it is directly responsible for extensively autophosphorylating and generating its Slimb-binding phosphodegron. Phosphorylatable residues within this regulatory region were systematically mutated to determine their impa","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Nov","modification":"2025-05-29T16:30:45.32Z","creation":"2019-03-27T03:09:27Z"},"accession":"S-EPMC3844517","cross_references":{"pubmed":["24184097"],"doi":["10.1016/j.cub.2013.09.019"]}}