{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Theophall GG"],"funding":["U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS)","NIDDK NIH HHS","NHLBI NIH HHS","U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (National Institute of Diabetes & Digestive & Kidney Diseases)","U.S. Department of Health & Human Services | NIH | National Heart, Lung, and Blood Institute (NHLBI)","NIGMS NIH HHS"],"pagination":["776"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12095592"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["DIAPH1 is a member of the family of Diaphanous Related Formins (DRFs) implicated in cell migration and cytokinesis. DRFs are maintained in an autoinhibited state by the intramolecular association between diaphanous inhibitory (DID) and diaphanous autoregulatory (DAD) domains. Actin polymerization requires the binding of activated RhoA to the GTPase binding domain (GBD) of DIAPH1 and the dissociation of DAD. In the presence of excess RhoA, actin polymerization is only partially activated. Using monomeric domain constructs of DIAPH1, the sequential binding affinities of RhoA and DAD to GBD-DID were characterized. Binding of RhoA and DAD were negatively cooperative requiring a 100-fold greater concentration of DAD to achieve saturation when RhoA binding site was occupied. The unimolecular arc"],"journal":["Communications biology"],"pubmed_title":["Negative cooperativity regulates ligand activation of DIAPH1 and other diaphanous related formins."],"pmcid":["PMC12095592"],"funding_grant_id":["R01 GM085006","R01 GM143749","R01 DK122456","5R01DK122456","P01 HL146367","5R01GM143749","1P01HL146367"],"pubmed_authors":["Omojowolo E","Schmidt AM","Burz DS","Shekhtman A","Nazarian P","Ramasamy R","Theophall GG","Reverdatto S","Premo A"],"additional_accession":[]},"is_claimable":false,"name":"Negative cooperativity regulates ligand activation of DIAPH1 and other diaphanous related formins.","description":"DIAPH1 is a member of the family of Diaphanous Related Formins (DRFs) implicated in cell migration and cytokinesis. DRFs are maintained in an autoinhibited state by the intramolecular association between diaphanous inhibitory (DID) and diaphanous autoregulatory (DAD) domains. Actin polymerization requires the binding of activated RhoA to the GTPase binding domain (GBD) of DIAPH1 and the dissociation of DAD. In the presence of excess RhoA, actin polymerization is only partially activated. Using monomeric domain constructs of DIAPH1, the sequential binding affinities of RhoA and DAD to GBD-DID were characterized. Binding of RhoA and DAD were negatively cooperative requiring a 100-fold greater concentration of DAD to achieve saturation when RhoA binding site was occupied. The unimolecular arc","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-03T02:44:25.515Z","creation":"2026-04-23T03:10:52.165Z"},"accession":"S-EPMC12095592","cross_references":{"pubmed":["40399622"],"doi":["10.1038/s42003-025-08222-5"]}}