Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end
| العنوان: | Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end |
|---|---|
| المؤلفون: | Clinton K. Lau, Francis J. O’Reilly, Balaji Santhanam, Andrew P. Carter, Samuel E Lacey, Juri Rappsilber |
| المساهمون: | Lau, Clinton K [0000-0003-1083-2989], O'Reilly, Francis J [0000-0001-9258-0150], Santhanam, Balaji [0000-0001-8523-4145], Lacey, Samuel E [0000-0002-3807-8888], Rappsilber, Juri [0000-0001-5999-1310], Carter, Andrew P [0000-0001-7292-5430], Apollo - University of Cambridge Repository |
| المصدر: | The EMBO Journal Lau, C K, O’Reilly, F J, Santhanam, B, Lacey, S E, Rappsilber, J & Carter, A P 2021, ' Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end ', EMBO Journal, vol. 40, no. 8, e106164 . https://doi.org/10.15252/embj.2020106164Test |
| بيانات النشر: | EMBO, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | cryo‐electron microscopy, Cryo-electron microscopy, Protein subunit, Dynein, cryo-electron microscopy, macromolecular substances, Biology, Molecular Dynamics Simulation, Topology, Article, General Biochemistry, Genetics and Molecular Biology, Protein filament, 03 medical and health sciences, 0302 clinical medicine, cargo adaptors, Protein Domains, Structural Biology, Microtubule, dynactin, Molecular motor, Humans, Molecular Biology, 030304 developmental biology, 0303 health sciences, General Immunology and Microbiology, General Neuroscience, protein complex, Cryoelectron Microscopy, conservation, Articles, Dynactin Complex, Protein Subunits, Shoulder region, Dynactin, Cell Adhesion, Polarity & Cytoskeleton, Protein Multimerization, 030217 neurology & neurosurgery |
| الوصف: | Dynactin is a 1.1 MDa complex that activates the molecular motor dynein for ultra‐processive transport along microtubules. In order to do this, it forms a tripartite complex with dynein and a coiled‐coil adaptor. Dynactin consists of an actin‐related filament whose length is defined by its flexible shoulder domain. Despite previous cryo‐EM structures, the molecular architecture of the shoulder and pointed end of the filament is still poorly understood due to the lack of high‐resolution information in these regions. Here we combine multiple cryo‐EM datasets and define precise masking strategies for particle signal subtraction and 3D classification. This overcomes domain flexibility and results in high‐resolution maps into which we can build the shoulder and pointed end. The unique architecture of the shoulder securely houses the p150 subunit and positions the four identical p50 subunits in different conformations to bind dynactin’s filament. The pointed end map allows us to build the first structure of p62 and reveals the molecular basis for cargo adaptor binding to different sites at the pointed end. Refinement of dynactin cryo‐EM structures offers insights into dynactin subunit organization in the shoulder region and adaptor binding to its pointed end. |
| وصف الملف: | application/pdf; text/xml |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cb9e9a382ded0313e7868040af40dc2Test https://www.repository.cam.ac.uk/handle/1810/321083Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....6cb9e9a382ded0313e7868040af40dc2 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |