[English] 日本語
Yorodumi- EMDB-47935: mTORC1-Rag-Ragulator-4EBP1 on membrane with one extra Rag-Ragulator -
+
Open data
-
Basic information
| Entry | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | mTORC1-Rag-Ragulator-4EBP1 on membrane with one extra Rag-Ragulator | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | mTORC1 / 4EBP1 / cell growth / singaling protein / membrane / SIGNALING PROTEIN | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.47 Å | |||||||||
Authors | Cui Z / Hurley J | |||||||||
| Funding support | United States, 1 items
| |||||||||
Citation | Journal: Nature / Year: 2025Title: Structural basis for mTORC1 activation on the lysosomal membrane. Authors: Zhicheng Cui / Alessandra Esposito / Gennaro Napolitano / Andrea Ballabio / James H Hurley / ![]() Abstract: The mechanistic target of rapamycin complex 1 (mTORC1) integrates growth factor (GF) and nutrient signals to stimulate anabolic processes connected to cell growth and inhibit catabolic processes such ...The mechanistic target of rapamycin complex 1 (mTORC1) integrates growth factor (GF) and nutrient signals to stimulate anabolic processes connected to cell growth and inhibit catabolic processes such as autophagy. GF signalling through the tuberous sclerosis complex regulates the lysosomally localized small GTPase RAS homologue enriched in brain (RHEB). Direct binding of RHEB-GTP to the mTOR kinase subunit of mTORC1 allosterically activates the kinase by inducing a large-scale conformational change. Here we reconstituted mTORC1 activation on membranes by RHEB, RAGs and Ragulator. Cryo-electron microscopy showed that RAPTOR and mTOR interact directly with the membrane. Full engagement of the membrane anchors is required for optimal alignment of the catalytic residues in the mTOR kinase active site. Converging signals from GFs and nutrients drive mTORC1 recruitment to and activation on lysosomal membrane in a four-step process, consisting of (1) RAG-Ragulator-driven recruitment to within ~100 Å of the lysosomal membrane; (2) RHEB-driven recruitment to within ~40 Å; (3) RAPTOR-membrane engagement and intermediate enzyme activation; and (4) mTOR-membrane engagement and full enzyme activation. RHEB and membrane engagement combined leads to full catalytic activation and structurally explains GF and nutrient signal integration at the lysosome. | |||||||||
| History |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_47935.map.gz | 323.5 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-47935-v30.xml emd-47935.xml | 13.7 KB 13.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_47935_fsc.xml | 14.8 KB | Display | FSC data file |
| Images | emd_47935.png | 91.9 KB | ||
| Filedesc metadata | emd-47935.cif.gz | 4.1 KB | ||
| Others | emd_47935_half_map_1.map.gz emd_47935_half_map_2.map.gz | 317.9 MB 317.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-47935 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-47935 | HTTPS FTP |
-Validation report
| Summary document | emd_47935_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
|---|---|---|---|---|
| Full document | emd_47935_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_47935_validation.xml.gz | 24 KB | Display | |
| Data in CIF | emd_47935_validation.cif.gz | 31.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-47935 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-47935 | HTTPS FTP |
-Related structure data
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|
-
Map
| File | Download / File: emd_47935.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Half map: #1
| File | emd_47935_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #2
| File | emd_47935_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : The mTORC1-Rag-Ragulator-4EBP1 complex on membrane
| Entire | Name: The mTORC1-Rag-Ragulator-4EBP1 complex on membrane |
|---|---|
| Components |
|
-Supramolecule #1: The mTORC1-Rag-Ragulator-4EBP1 complex on membrane
| Supramolecule | Name: The mTORC1-Rag-Ragulator-4EBP1 complex on membrane / type: complex / ID: 1 / Parent: 0 |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Buffer | pH: 7.4 |
|---|---|
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.9 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
Movie
Controller
About Yorodumi



Keywords
Homo sapiens (human)
Authors
United States, 1 items
Citation












Z (Sec.)
Y (Row.)
X (Col.)




































Processing
FIELD EMISSION GUN

