|Entry||Database: EMDB / ID: 4191|
|Title||In situ cryo-electron tomogram from Rat neuron with C9ORF72 Poly-GA aggregates|
|Map data||Tomogram of Rat neuron cell|
|Sample||in situ tomogram from Rat neuron:|
|Source||Rattus norvegicus (Norway rat)|
|Method||electron tomography / cryo EM|
|Authors||Guo Q / Lehmer C / Martinez-Sanchez A / Rudack T / Beck F / Hartmann H / Hipp MS / Hartl FU / Edbauer D / Baumeister W / Fernandez-Busnadiego F|
|Citation||Journal: Cell / Year: 2018|
Title: In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
Authors: Qiang Guo / Carina Lehmer / Antonio Martínez-Sánchez / Till Rudack / Florian Beck / Hannelore Hartmann / Manuela Pérez-Berlanga / Frédéric Frottin / Mark S Hipp / F Ulrich Hartl / Dieter Edbauer / Wolfgang Baumeister / Rubén Fernández-Busnadiego
Abstract: Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of many neurodegenerative diseases. Here, we address the elusive link between these phenomena by employing ...Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of many neurodegenerative diseases. Here, we address the elusive link between these phenomena by employing cryo-electron tomography to dissect the molecular architecture of protein aggregates within intact neurons at high resolution. We focus on the poly-Gly-Ala (poly-GA) aggregates resulting from aberrant translation of an expanded GGGGCC repeat in C9orf72, the most common genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia. We find that poly-GA aggregates consist of densely packed twisted ribbons that recruit numerous 26S proteasome complexes, while other macromolecules are largely excluded. Proximity to poly-GA ribbons stabilizes a transient substrate-processing conformation of the 26S proteasome, suggesting stalled degradation. Thus, poly-GA aggregates may compromise neuronal proteostasis by driving the accumulation and functional impairment of a large fraction of cellular proteasomes.
|Date||Deposition: Dec 5, 2017 / Header (metadata) release: Jan 17, 2018 / Map release: Feb 7, 2018 / Last update: Feb 21, 2018|
Downloads & links
|File||emd_4191.map.gz (map file in CCP4 format, 243524 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 13.68 Å|
CCP4 map header:
-Entire in situ tomogram from Rat neuron
|Entire||Name: in situ tomogram from Rat neuron / Number of components: 1|
-Component #1: cellular-component, in situ tomogram from Rat neuron
|Cellular-component||Name: in situ tomogram from Rat neuron / Recombinant expression: No|
|Source||Species: Rattus norvegicus (Norway rat)|
|Specimen||Specimen state: cell / Method: cryo EM|
|Sample solution||pH: 7|
|Support film||The grid was coated with C prior to use|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: OTHER / Temperature: 298 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 1.8 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 42000.0 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 5000.0 - 7000.0 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: electron tomography / Number of sections: 59|
|3D reconstruction||Software: eTomo / Resolution method: OTHER|
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