EMD-7000

Subtomogram averaging
38.0 Å
EMD-7000 Deposition: 23/08/2017
Map released: 20/09/2017
Last modified: 21/03/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-7000

Subtomogram average of microtubule-bound dynein-dynactin-BICD2N complex

EMD-7000

Subtomogram averaging
38.0 Å
EMD-7000 Deposition: 23/08/2017
Map released: 20/09/2017
Last modified: 21/03/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Mus musculus
Sample: microtubule-bound dynein-dynactin-BICD2N complex
Raw data: EMPIAR-10520

Deposition Authors: Grotjahn DA, Chowdhury S, Xu Y, McKenney RJ, Schroer TA, Lander GC
Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility.
Grotjahn DA, Chowdhury S , Xu Y, McKenney RJ, Schroer TA, Lander GC
(2018) Nat. Struct. Mol. Biol. , 25 , 203 - 207
PUBMED: 29416113
DOI: doi:10.1038/s41594-018-0027-7
ISSN: 1545-9985
Abstract:
Cytoplasmic dynein is a protein complex that transports molecular cargo along microtubules (MTs), playing a key role in the intracellular trafficking network. Vertebrate dynein's movement becomes strikingly enhanced upon interacting with dynactin and a cargo adaptor such as BicaudalD2. However, the mechanisms responsible for increased transport activity are not well understood, largely owing to limited structural information. We used cryo-electron tomography (cryo-ET) to visualize the 3D structure of the MT-bound dynein-dynactin complex from Mus musculus and show that the dynactin-cargo adaptor complex binds two dimeric dyneins. This configuration imposes spatial and conformational constraints on both dynein dimers, positioning the four motor domains in proximity to one another and oriented toward the MT minus end. We propose that grouping multiple dyneins onto a single dynactin scaffold promotes collective force production, increased processivity, and unidirectional movement, suggesting mechanistic parallels to axonemal dynein. These findings provide structural insights into a previously unknown mechanism for dynein regulation.