Components of coated vesicles and nuclear pore complexes share a common molecular architecture.
Numerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the chromatin within the nuclear envelope. The nuclear...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2004-12-01
|
| Series: | PLoS Biology |
| Online Access: | https://doi.org/10.1371/journal.pbio.0020380 |
| _version_ | 1819124332114214912 |
|---|---|
| author | Damien Devos Svetlana Dokudovskaya Frank Alber Rosemary Williams Brian T Chait Andrej Sali Michael P Rout |
| author_facet | Damien Devos Svetlana Dokudovskaya Frank Alber Rosemary Williams Brian T Chait Andrej Sali Michael P Rout |
| author_sort | Damien Devos |
| collection | DOAJ |
| description | Numerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the chromatin within the nuclear envelope. The nuclear pore complex is the portal that specifically mediates macromolecular trafficking across the nuclear envelope. Although it is generally understood that these internal membrane systems evolved from specialized invaginations of the prokaryotic plasma membrane, it is not clear how the nuclear pore complex could have evolved from organisms with no analogous transport system. Here we use computational and biochemical methods to perform a structural analysis of the seven proteins comprising the yNup84/vNup107-160 subcomplex, a core building block of the nuclear pore complex. Our analysis indicates that all seven proteins contain either a beta-propeller fold, an alpha-solenoid fold, or a distinctive arrangement of both, revealing close similarities between the structures comprising the yNup84/vNup107-160 subcomplex and those comprising the major types of vesicle coating complexes that maintain vesicular trafficking pathways. These similarities suggest a common evolutionary origin for nuclear pore complexes and coated vesicles in an early membrane-curving module that led to the formation of the internal membrane systems in modern eukaryotes. |
| first_indexed | 2024-12-22T07:22:33Z |
| format | Article |
| id | doaj.art-b8d5248674d543b188ad4c177bc0a6c0 |
| institution | Directory Open Access Journal |
| issn | 1544-9173 1545-7885 |
| language | English |
| last_indexed | 2024-12-22T07:22:33Z |
| publishDate | 2004-12-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj.art-b8d5248674d543b188ad4c177bc0a6c02022-12-21T18:34:13ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852004-12-01212e38010.1371/journal.pbio.0020380Components of coated vesicles and nuclear pore complexes share a common molecular architecture.Damien DevosSvetlana DokudovskayaFrank AlberRosemary WilliamsBrian T ChaitAndrej SaliMichael P RoutNumerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the chromatin within the nuclear envelope. The nuclear pore complex is the portal that specifically mediates macromolecular trafficking across the nuclear envelope. Although it is generally understood that these internal membrane systems evolved from specialized invaginations of the prokaryotic plasma membrane, it is not clear how the nuclear pore complex could have evolved from organisms with no analogous transport system. Here we use computational and biochemical methods to perform a structural analysis of the seven proteins comprising the yNup84/vNup107-160 subcomplex, a core building block of the nuclear pore complex. Our analysis indicates that all seven proteins contain either a beta-propeller fold, an alpha-solenoid fold, or a distinctive arrangement of both, revealing close similarities between the structures comprising the yNup84/vNup107-160 subcomplex and those comprising the major types of vesicle coating complexes that maintain vesicular trafficking pathways. These similarities suggest a common evolutionary origin for nuclear pore complexes and coated vesicles in an early membrane-curving module that led to the formation of the internal membrane systems in modern eukaryotes.https://doi.org/10.1371/journal.pbio.0020380 |
| spellingShingle | Damien Devos Svetlana Dokudovskaya Frank Alber Rosemary Williams Brian T Chait Andrej Sali Michael P Rout Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biology |
| title | Components of coated vesicles and nuclear pore complexes share a common molecular architecture. |
| title_full | Components of coated vesicles and nuclear pore complexes share a common molecular architecture. |
| title_fullStr | Components of coated vesicles and nuclear pore complexes share a common molecular architecture. |
| title_full_unstemmed | Components of coated vesicles and nuclear pore complexes share a common molecular architecture. |
| title_short | Components of coated vesicles and nuclear pore complexes share a common molecular architecture. |
| title_sort | components of coated vesicles and nuclear pore complexes share a common molecular architecture |
| url | https://doi.org/10.1371/journal.pbio.0020380 |
| work_keys_str_mv | AT damiendevos componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture AT svetlanadokudovskaya componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture AT frankalber componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture AT rosemarywilliams componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture AT briantchait componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture AT andrejsali componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture AT michaelprout componentsofcoatedvesiclesandnuclearporecomplexesshareacommonmoleculararchitecture |