{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bagci H"],"funding":["National Science and Engineering Research Council of Canada","Swiss National Science Foundation","Swiss National Science Foundation Sinergia"],"pagination":["e202403046"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11467045"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(12)"],"pubmed_abstract":["The human CTLH/GID (hGID) complex emerged as an important E3 ligase regulating multiple cellular processes, including cell cycle progression and metabolism. However, the range of biological functions controlled by hGID remains unexplored. Here, we used proximity-dependent biotinylation (BioID2) to identify proteins interacting with the hGID complex, among them, substrate candidates that bind GID4 in a pocket-dependent manner. Biochemical and cellular assays revealed that the hGID<sup>GID4</sup> E3 ligase binds and ubiquitinates ARHGAP11A, thereby targeting this RhoGAP for proteasomal degradation. Indeed, GID4 depletion or impeding the GID4 substrate binding pocket with the PFI-7 inhibitor stabilizes ARHGAP11A protein amounts, although it carries no functional N-terminal degron. Interesting"],"journal":["Life science alliance"],"pubmed_title":["The hGID&lt;sup&gt;GID4&lt;/sup&gt; E3 ubiquitin ligase complex targets ARHGAP11A to regulate cell migration."],"pmcid":["PMC11467045"],"funding_grant_id":["310030_179283/1","CRSII5_183550","RGPIN-2024-04485"],"pubmed_authors":["Boulais J","Cote JF","Uliana F","Winkler M","Mohamed WI","Gradel B","Peter M","Pertz O","Bagci H","Park SL"],"additional_accession":[]},"is_claimable":false,"name":"The hGID&lt;sup&gt;GID4&lt;/sup&gt; E3 ubiquitin ligase complex targets ARHGAP11A to regulate cell migration.","description":"The human CTLH/GID (hGID) complex emerged as an important E3 ligase regulating multiple cellular processes, including cell cycle progression and metabolism. However, the range of biological functions controlled by hGID remains unexplored. Here, we used proximity-dependent biotinylation (BioID2) to identify proteins interacting with the hGID complex, among them, substrate candidates that bind GID4 in a pocket-dependent manner. Biochemical and cellular assays revealed that the hGID<sup>GID4</sup> E3 ligase binds and ubiquitinates ARHGAP11A, thereby targeting this RhoGAP for proteasomal degradation. Indeed, GID4 depletion or impeding the GID4 substrate binding pocket with the PFI-7 inhibitor stabilizes ARHGAP11A protein amounts, although it carries no functional N-terminal degron. Interesting","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2025-04-04T01:37:16.089Z","creation":"2025-04-04T01:37:16.089Z"},"accession":"S-EPMC11467045","cross_references":{"pubmed":["39389782"],"doi":["10.26508/lsa.202403046"]}}