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| Entry | Database: PDB / ID: 23as | ||||||||||||||||||||||||
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| Title | Structure of Arabidopsis SNX1 (Class l, 7-fold) | ||||||||||||||||||||||||
Components | Sorting nexin 1 | ||||||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / SNX protein / Arabidopsis thaliana / tube | ||||||||||||||||||||||||
| Function / homology | Function and homology informationpositive gravitropism / root development / Golgi to vacuole transport / retromer complex / protein targeting to vacuole / endosome to lysosome transport / multivesicular body / phosphatidylinositol binding / protein localization to plasma membrane / endosome ...positive gravitropism / root development / Golgi to vacuole transport / retromer complex / protein targeting to vacuole / endosome to lysosome transport / multivesicular body / phosphatidylinositol binding / protein localization to plasma membrane / endosome / endosome membrane / Golgi apparatus / membrane / plasma membrane Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 7.2 Å | ||||||||||||||||||||||||
Authors | Li, Y.B. / Tao, R. / Zhang, H. / Wen, X.K. / Leung, S.K.P. / Lau, W.C.Y. / Jiang, L.W. / Cui, Y. | ||||||||||||||||||||||||
| Funding support | China, Hong Kong, 4items
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Citation | Journal: Nat Commun / Year: 2026Title: SNX-mediated biogenesis of a plant-unique vesicle derived from the multivesicular body. Authors: Yanbin Li / Ran Tao / Hai Zhang / Xiaokang Wen / Stephen King Pong Leung / Qing Qi / Xiaohui Zheng / Haoxuan Guo / Congxian Wu / Zhifei Fu / Xiaorong Huang / Wilson Chun Yu Lau / Liwen Jiang / Yong Cui / ![]() Abstract: Retrograde transport is central to endomembrane homeostasis, yet the identity and origin of plant retrograde carriers remain unresolved. Prevailing models propose that plant vacuolar sorting ...Retrograde transport is central to endomembrane homeostasis, yet the identity and origin of plant retrograde carriers remain unresolved. Prevailing models propose that plant vacuolar sorting receptors (VSRs) recycle either from multivesicular bodies (MVBs) to the trans-Golgi network (TGN) or from the TGN to the Golgi apparatus and/or endoplasmic reticulum (ER). However, the ultrastructural features of plant retrograde transport carriers remain largely unresolved. Here, we show that plant retrograde transport is likely mediated by a previously unrecognized class of MVB-derived spherical vesicles. Using correlative light and electron microscopy and three-dimensional electron tomography, we identify a distinct population of ~30-50 nm spherical vesicles adjacent to MVBs, including nascent vesicles budding from the MVB limiting membrane in Arabidopsis root cells. Immunogold labeling shows that these vesicles are enriched in retromer components and VSRs, suggesting that they possibly function as retrograde transport carriers. To investigate their biogenesis, we perform cryo-electron microscopy and liposome tubulation assays, showing that Arabidopsis SNX1 generates shorter membrane tubules than its mammalian counterpart, consistent with reduced membrane affinity linked to differences in the amphipathic helix. Notably, the SNX1-SNX2 heterodimer produces heterogeneous structures, including spherical vesicles, recapitulating in vivo observations. Lastly, knockdown of SNX1 or SNX2 results in vacuolar mislocalization and increased degradation of GFP-VSR2, and defects in SNX1 and VPS29 inhibit formation of spherical vesicles adjacent to MVBs, resulting in embryonic lethality before the globular stage. Together, these findings establish MVB-derived spherical vesicles as plant retrograde carriers and reveal a distinct SNX-mediated mechanism underlying their formation. | ||||||||||||||||||||||||
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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| PDBx/mmCIF format | 23as.cif.gz | 5.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb23as.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 23as.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/3a/23as ftp://data.pdbj.org/pub/pdb/validation_reports/3a/23as | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 68805MC ![]() 23atC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Assembly
| Deposited unit | ![]()
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| Noncrystallographic symmetry (NCS) | NCS domain:
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