{"doi":"10.64898/2026.04.25.720804","title":"Structural basis of dynein interaction with diverse activating adaptors","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>Cargo-specific activating adaptors enable dynein to assemble with dynactin into processive supercomplexes. Adaptors share a coiled-coil architecture, but are highly diverse in sequence and structure, raising the question of how they converge on a common activation mechanism. To address this, we determined near atomic cryo-EM structures of dynein-dynactin assembled with five adaptors: RAB11FIP3, NIN, TRAK1, BICD2 and HOOK3. Despite their heterogeneity, all complexes contain adaptor coiled coils which bridge two dynein dimers to the dynactin filament. Adaptors are defined by an N-terminal interaction at the HBS1 with the dynein heavy chain, additional contacts along the dynein-dynactin groove, and C-terminal binding to the dynactin pointed end. However, we also found distinct sequence features, coiled-coil breaks and pointed-end interfaces that tune complex stoichiometry and stability. Our results define shared principles of dynein activation while revealing unexpected plasticity in how adaptors recognise and organise the dynein-dynactin machinery.</jats:p>","journal":null,"year":null,"id":686623,"datarank":0.16479184330021646,"base_score":1.0986122886681096,"endowment":1.0986122886681096,"self_citation_contribution":0.16479184330021646,"citation_network_contribution":0.0,"self_endowment_contribution":0.16479184330021646,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":2,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1176851,"name":"Sami Chaaban","orcid":"0000-0003-1133-800X","position":1,"is_corresponding":false},{"id":1709239,"name":"Ferdos Abid Ali","orcid":null,"position":2,"is_corresponding":false},{"id":1793794,"name":"Leon Michalski","orcid":null,"position":3,"is_corresponding":false},{"id":201954,"name":"Andrew P. Carter","orcid":null,"position":4,"is_corresponding":false},{"id":862041,"name":"Ennio d’Amico","orcid":"0000-0002-1451-6273","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Structural basis of dynein interaction with diverse activating adaptors","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>Cargo-specific activating adaptors enable dynein to assemble with dynactin into processive supercomplexes. Adaptors share a coiled-coil architecture, but are highly diverse in sequence and structure, raising the question of how they converge on a common activation mechanism. To address this, we determined near atomic cryo-EM structures of dynein-dynactin assembled with five adaptors: RAB11FIP3, NIN, TRAK1, BICD2 and HOOK3. Despite their heterogeneity, all complexes contain adaptor coiled coils which bridge two dynein dimers to the dynactin filament. Adaptors are defined by an N-terminal interaction at the HBS1 with the dynein heavy chain, additional contacts along the dynein-dynactin groove, and C-terminal binding to the dynactin pointed end. However, we also found distinct sequence features, coiled-coil breaks and pointed-end interfaces that tune complex stoichiometry and stability. Our results define shared principles of dynein activation while revealing unexpected plasticity in how adaptors recognise and organise the dynein-dynactin machinery.</jats:p>","is_dataset_classified":null,"base_score":1.0986122886681096,"endowment":1.0986122886681096,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26207759","pmcid":null,"openalex_id":"https://openalex.org/W7159583979","authors":[],"funders":[{"funder_name":"","grant_id":"227434/Z/23/Z","title":null},{"funder_name":"","grant_id":"218653/Z/19/Z","title":null},{"funder_name":"","grant_id":"MC_UP_A025_1011","title":null},{"funder_name":"","grant_id":"101105484","title":null},{"funder_name":"","grant_id":"ALTF 334-2020","title":null}],"total_grants":5,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[{"year":2026,"count":2}],"oa_status":"green","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.64898/2026.04.25.720804","host_type":"repository"},{"url":"https://doi.org/10.64898/2026.04.25.720804","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.64898/2026.04.25.720804","host_type":"publisher"}],"fields_of_study":["Microtubule and mitosis dynamics","Bacteriophages and microbial interactions","Supramolecular Chemistry and Complexes"],"mesh_terms":[],"keywords":["Dynactin","Dynein","Signal transducing adaptor protein","Sequence (biology)","Bridge (graph theory)","Structural plasticity"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T20:00:16.327629Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}