{"doi":"10.1101/182576","title":"Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>A key player in the intracellular trafficking network is cytoplasmic dynein, a protein complex that transports molecular cargo along microtubule tracks. It has been shown that vertebrate dynein’s movement becomes strikingly enhanced upon interacting with a cofactor named dynactin and one of several cargo-adapters, such as BicaudalD2. However, the mechanisms responsible for this increase in transport efficiency are not well understood, largely due to a lack of structural information. We used cryo-electron tomography to visualize the first 3-dimensional structure of the intact dynein-dynactin complex bound to microtubules. Our structure reveals that the dynactin-cargo-adapter complex recruits and binds to two dimeric cytoplasmic dyneins. Interestingly, the dynein motor organization closely resembles that of axonemal dynein, suggesting that cytoplasmic dynein and axonemal dyneins may utilize similar mechanisms to coordinate multiple motors. We propose that grouping dyneins onto a single dynactin scaffold promotes collective force production as well as unidirectional processive motility. These findings provide a structural platform that facilitates a deeper biochemical and biophysical understanding of dynein regulation and cellular transport.</jats:p>","journal":null,"year":null,"id":648828,"datarank":0.6014549984364457,"base_score":2.1972245773362196,"endowment":2.1972245773362196,"self_citation_contribution":0.32958368660043297,"citation_network_contribution":0.27187131183601276,"self_endowment_contribution":0.32958368660043297,"citer_contribution":0.27187131183601276,"corpus_percentile":null,"corpus_rank":null,"citation_count":8,"citer_count":7,"citers_with_citation_signal":6,"citers_with_endowment":6,"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":314359,"name":"Saikat Chowdhury","orcid":"0000-0001-8043-5028","position":1,"is_corresponding":false},{"id":1392440,"name":"Yiru Xu","orcid":null,"position":2,"is_corresponding":false},{"id":202406,"name":"Richard J. McKenney","orcid":"0000-0002-8423-0852","position":3,"is_corresponding":false},{"id":1691147,"name":"Trina A. Schroer","orcid":"0000-0002-5065-1835","position":4,"is_corresponding":false},{"id":287919,"name":"Gabriel C. Lander","orcid":"0000-0003-4921-1135","position":5,"is_corresponding":false},{"id":514884,"name":"Danielle A. Grotjahn","orcid":"0000-0001-5908-7882","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>A key player in the intracellular trafficking network is cytoplasmic dynein, a protein complex that transports molecular cargo along microtubule tracks. It has been shown that vertebrate dynein’s movement becomes strikingly enhanced upon interacting with a cofactor named dynactin and one of several cargo-adapters, such as BicaudalD2. However, the mechanisms responsible for this increase in transport efficiency are not well understood, largely due to a lack of structural information. We used cryo-electron tomography to visualize the first 3-dimensional structure of the intact dynein-dynactin complex bound to microtubules. Our structure reveals that the dynactin-cargo-adapter complex recruits and binds to two dimeric cytoplasmic dyneins. Interestingly, the dynein motor organization closely resembles that of axonemal dynein, suggesting that cytoplasmic dynein and axonemal dyneins may utilize similar mechanisms to coordinate multiple motors. We propose that grouping dyneins onto a single dynactin scaffold promotes collective force production as well as unidirectional processive motility. These findings provide a structural platform that facilitates a deeper biochemical and biophysical understanding of dynein regulation and cellular transport.</jats:p>","is_dataset_classified":null,"base_score":2.1972245773362196,"endowment":2.1972245773362196,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19162232","pmcid":null,"openalex_id":"https://openalex.org/W2750867488","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"1S10OD021634-01","title":"COMPUTING AND DATA STORAGE CLUSTER FOR ELECTRON MICROSCOPY"},{"funder_name":"National Institutes of Health","grant_id":"1R35GM124889-01","title":"Coordination of molecular motor activity in intracellular transport and assembly of cytoskeletal architecture."},{"funder_name":"National Institutes of Health","grant_id":"1DP2EB020402-01","title":"Molecular basis of axonal transport described by high-resolution 3D imaging"},{"funder_name":"National Institutes of Health","grant_id":"5R00NS089428-05","title":"Regulation of Cytoplasmic Dynein Motility in Neuronal Transport"}],"total_grants":4,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[{"year":2018,"count":2},{"year":2020,"count":2},{"year":2022,"count":2},{"year":2023,"count":2}],"oa_status":"green","license":"cc-by","oa_locations":[{"url":"https://www.biorxiv.org/content/biorxiv/early/2017/08/31/182576.full.pdf","host_type":"repository"},{"url":"https://www.biorxiv.org/content/biorxiv/early/2017/08/31/182576.full.pdf","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.1101/182576","host_type":"publisher"},{"url":"https://doi.org/10.1101/182576","host_type":"repository"},{"url":"https://doi.org/10.1016/j.bpj.2017.11.1086","host_type":""},{"url":"http://www.cell.com/article/S0006349517323184/pdf","host_type":""},{"url":"https://europepmc.org/articles/pmc5969528?pdf=render","host_type":""},{"url":"https://doi.org/10.1038/s41594-018-0027-7","host_type":""},{"url":"https://pubmed.ncbi.nlm.nih.gov/29416113","host_type":""},{"url":"http://dx.doi.org/10.1038/s41594-018-0027-7","host_type":""},{"url":"https://dx.doi.org/10.1038/s41594-018-0027-7","host_type":""},{"url":"https://dx.doi.org/10.1101/182576","host_type":""},{"url":"https://dx.doi.org/10.1016/j.bpj.2017.11.1086","host_type":""},{"url":"https://escholarship.org/uc/item/68x8m31s","host_type":""},{"url":"https://escholarship.org/content/qt68x8m31s/qt68x8m31s.pdf","host_type":""},{"url":"http://dx.doi.org/10.1101/182576","host_type":""},{"url":"https://doi.org/https://doi.org/10.1038/s41594-018-0027-7","host_type":""}],"fields_of_study":["Microtubule and mitosis dynamics","Photosynthetic Processes and Mechanisms","Advanced Electron Microscopy Techniques and Applications","0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":[],"keywords":["Dynein","Dynactin","Microtubule","Cell biology","Motor protein","Biology","Organelle","Cytoplasm","Motility","Biophysics","Models, Molecular","Electron Microscope Tomography","Biomedical and clinical sciences","Microtubules (mesh)","11 Medical and Health Sciences (for)","Medical and Health Sciences","Microtubules","Mice","34 Chemical sciences (for-2020)","Models","31 Biological sciences (for-2020)","2.1 Biological and endogenous factors","Animals (mesh)","Dynactin Complex (mesh)","Developmental Biology (science-metrix)","Generic health relevance (hrcs-hc)","03 Chemical Sciences (for)","Mice (mesh)","Dynactin Complex","Biological Sciences","06 Biological Sciences (for)","Molecular (mesh)","Biological Transport (mesh)","Neurological","Dyneins 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