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Open data
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Basic information
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Title | Architecture of the ESCPE-1 membrane coat | |||||||||
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![]() | sorting nexins / PX domain / BAR domain / endosomes / retrograde transport / endocytic recycling / cargo recognition / protein coat / membrane recruitment / membrane deformation / membrane tubules. / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() retromer, tubulation complex / lamellipodium morphogenesis / epidermal growth factor catabolic process / pinocytosis / cytoplasmic side of early endosome membrane / leptin receptor binding / tubular endosome / macropinocytic cup / early endosome to Golgi transport / Retrograde transport at the Trans-Golgi-Network ...retromer, tubulation complex / lamellipodium morphogenesis / epidermal growth factor catabolic process / pinocytosis / cytoplasmic side of early endosome membrane / leptin receptor binding / tubular endosome / macropinocytic cup / early endosome to Golgi transport / Retrograde transport at the Trans-Golgi-Network / clathrin coat / retromer complex binding / response to tetrachloromethane / insulin-like growth factor receptor activity / retromer complex / insulin-like growth factor binding / phosphatidylinositol-5-phosphate binding / transferrin receptor binding / insulin-like growth factor II binding / trans-Golgi network transport vesicle / positive regulation by host of viral process / retinoic acid binding / retrograde transport, endosome to Golgi / phosphatidylinositol-4-phosphate binding / phosphatidylinositol-3,5-bisphosphate binding / lysosomal transport / epidermal growth factor receptor binding / Golgi Associated Vesicle Biogenesis / nuclear envelope lumen / D-mannose binding / brush border / dynactin binding / phagocytic cup / endocytic vesicle / G-protein alpha-subunit binding / D1 dopamine receptor binding / regulation of macroautophagy / animal organ regeneration / response to retinoic acid / positive regulation of insulin receptor signaling pathway / transport vesicle / ruffle / negative regulation of blood pressure / phosphatidylinositol binding / receptor-mediated endocytosis / secretory granule membrane / post-embryonic development / trans-Golgi network membrane / liver development / phosphoprotein binding / intracellular protein transport / insulin receptor binding / clathrin-coated endocytic vesicle membrane / trans-Golgi network / receptor internalization / cytoplasmic side of plasma membrane / late endosome / Cargo recognition for clathrin-mediated endocytosis / lamellipodium / Clathrin-mediated endocytosis / signaling receptor activity / early endosome membrane / spermatogenesis / vesicle / early endosome / lysosome / endosome membrane / endosome / cadherin binding / positive regulation of apoptotic process / G protein-coupled receptor signaling pathway / protein heterodimerization activity / Golgi membrane / intracellular membrane-bounded organelle / focal adhesion / Neutrophil degranulation / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / Golgi apparatus / enzyme binding / cell surface / signal transduction / protein homodimerization activity / protein-containing complex / extracellular exosome / identical protein binding / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | subtomogram averaging / cryo EM / Resolution: 10.0 Å | |||||||||
![]() | Lopez-Robles C / Scaramuzza S / Astorga-Simon E / Ishida M / Williamsom CD / Banos-Mateos S / Gil-Carton D / Romero M / Vidaurrazaga A / Fernandez-Recio J ...Lopez-Robles C / Scaramuzza S / Astorga-Simon E / Ishida M / Williamsom CD / Banos-Mateos S / Gil-Carton D / Romero M / Vidaurrazaga A / Fernandez-Recio J / Rojas AL / Bonifacino JS / Castano-Diez D / Hierro A | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Architecture of the ESCPE-1 membrane coat. Authors: Carlos Lopez-Robles / Stefano Scaramuzza / Elsa N Astorga-Simon / Morié Ishida / Chad D Williamson / Soledad Baños-Mateos / David Gil-Carton / Miguel Romero-Durana / Ander Vidaurrazaga / ...Authors: Carlos Lopez-Robles / Stefano Scaramuzza / Elsa N Astorga-Simon / Morié Ishida / Chad D Williamson / Soledad Baños-Mateos / David Gil-Carton / Miguel Romero-Durana / Ander Vidaurrazaga / Juan Fernandez-Recio / Adriana L Rojas / Juan S Bonifacino / Daniel Castaño-Díez / Aitor Hierro / ![]() ![]() ![]() Abstract: Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1) ...Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 3.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.2 KB 18.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 3.7 KB | Display | ![]() |
Images | ![]() | 161.3 KB | ||
Filedesc metadata | ![]() | 6.5 KB | ||
Others | ![]() ![]() | 3.1 MB 3.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8afzMC ![]() 8a1gC ![]() 8abqC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 2.73 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_15413_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #1
File | emd_15413_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1)
Entire | Name: Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1) |
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Components |
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-Supramolecule #1: Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1)
Supramolecule | Name: Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1) type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 110 KDa |
-Macromolecule #1: Sorting nexin-1
Macromolecule | Name: Sorting nexin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 59.14434 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLF ADATVELSLD STQNNQKKVL AKTLISLPPQ EATNSSKPQP TYEELEEEEQ EDQFDLTVGI TDPEKIGDGM N AYVAYKVT ...String: MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLF ADATVELSLD STQNNQKKVL AKTLISLPPQ EATNSSKPQP TYEELEEEEQ EDQFDLTVGI TDPEKIGDGM N AYVAYKVT TQTSLPLFRS KQFAVKRRFS DFLGLYEKLS EKHSQNGFIV PPPPEKSLIG MTKVKVGKED SSSAEFLEKR RA ALERYLQ RIVNHPTMLQ DPDVREFLEK EELPRAVGTQ TLSGAGLLKM FNKATDAVSK MTIKMNESDI WFEEKLQEVE CEE QRLRKL HAVVETLVNH RKELALNTAQ FAKSLAMLGS SEDNTALSRA LSQLAEVEEK IEQLHQEQAN NDFFLLAELL SDYI RLLAI VRAAFDQRMK TWQRWQDAQA TLQKKREAEA RLLWANKPDK LQQAKDEILE WESRVTQYER DFERISTVVR KEVIR FEKE KSKDFKNHVI KYLETLLYSQ QQLAKYWEAF LPEAKAIS UniProtKB: Sorting nexin-1 |
-Macromolecule #2: Sorting nexin-5
Macromolecule | Name: Sorting nexin-5 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 46.891504 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLI IPPAPTKPDF DGPREKMQKL GEGEGSMTKE EFAKMKQELE AEYLAVFKKT VSSHEVFLQR LSSHPVLSKD R NFHVFLEY ...String: MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLI IPPAPTKPDF DGPREKMQKL GEGEGSMTKE EFAKMKQELE AEYLAVFKKT VSSHEVFLQR LSSHPVLSKD R NFHVFLEY DQDLSVRRKN TKEMFGGFFK SVVKSADEVL FTGVKEVDDF FEQEKNFLIN YYNRIKDSCV KADKMTRSHK NV ADDYIHT AACLHSLALE EPTVIKKYLL KVAELFEKLR KVEGRVSSDE DLKLTELLRY YMLNIEAAKD LLYRRTKALI DYE NSNKAL DKARLKSKDV KLAEAHQQEC CQKFEQLSES AKEELINFKR KRVAAFRKNL IEMSELEIKH ARNNVSLLQS CIDL FKNN UniProtKB: Sorting nexin-5 |
-Macromolecule #3: Cation-independent mannose-6-phosphate receptor
Macromolecule | Name: Cation-independent mannose-6-phosphate receptor / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 3.766033 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SNVSYKYSKV NKEEETDENE TEWLMEEIQL P UniProtKB: Cation-independent mannose-6-phosphate receptor |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | subtomogram averaging |
Aggregation state | particle |
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Sample preparation
Concentration | 3.0 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 282 K / Instrument: FEI VITROBOT MARK II / Details: Incubation time 30s Blotting time 2s. |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average electron dose: 2.8 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 5.0 µm / Nominal defocus min: 2.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |