{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu P"],"funding":["National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["1-13"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8738747"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["29(1)"],"pubmed_abstract":["SKP1-CUL1-F-box (SCF) ubiquitin ligases play fundamental roles in cellular functions. Typically, substrate phosphorylation is required for SCF recognition and subsequent degradation. However, phospho-dependent substrates remain largely unidentified. Here, using quantitative phoshoproteome approach, we performed a system-wide investigation of phospho-dependent SCF substrates. This strategy identified diverse phospho-dependent candidates. Biochemical verification revealed a mechanism by which SCF<sup>FBXO22</sup> recognizes the motif XXPpSPXPXX as a conserved phosphodegron to target substrates for destruction. We further demonstrated BAG3, a HSP70 co-chaperone, is a bona fide substrate of SCF<sup>FBXO22</sup>. FBXO22 mediates BAG3 ubiquitination and degradation that requires ERK-dependent BA"],"journal":["Cell death and differentiation"],"pubmed_title":["Global identification of phospho-dependent SCF substrates reveals a FBXO22 phosphodegron and an ERK-FBXO22-BAG3 axis in tumorigenesis."],"pmcid":["PMC8738747"],"funding_grant_id":["81773018","32071432, 81872888, 91753203","71473074","81821005"],"pubmed_authors":["Tan M","Zhang J","Liu P","Dai W","Huang M","Ji J","Liu W","Liu Z","Zhao L","Cong X","Jia X","Zhai L","Ni D","Chen Y","Liu B","Liao S","Wang X","Pan L"],"additional_accession":[]},"is_claimable":false,"name":"Global identification of phospho-dependent SCF substrates reveals a FBXO22 phosphodegron and an ERK-FBXO22-BAG3 axis in tumorigenesis.","description":"SKP1-CUL1-F-box (SCF) ubiquitin ligases play fundamental roles in cellular functions. Typically, substrate phosphorylation is required for SCF recognition and subsequent degradation. However, phospho-dependent substrates remain largely unidentified. Here, using quantitative phoshoproteome approach, we performed a system-wide investigation of phospho-dependent SCF substrates. This strategy identified diverse phospho-dependent candidates. Biochemical verification revealed a mechanism by which SCF<sup>FBXO22</sup> recognizes the motif XXPpSPXPXX as a conserved phosphodegron to target substrates for destruction. We further demonstrated BAG3, a HSP70 co-chaperone, is a bona fide substrate of SCF<sup>FBXO22</sup>. FBXO22 mediates BAG3 ubiquitination and degradation that requires ERK-dependent BA","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2025-04-21T15:22:43.985Z","creation":"2025-02-19T03:30:49.172Z"},"accession":"S-EPMC8738747","cross_references":{"pubmed":["34215846"],"doi":["10.1038/s41418-021-00827-7"]}}