Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges
The nuclear pore complex (NPC) regulates all traffic between the cytoplasm and the nucleus. It is a large protein assembly composed of multiple copies of ~30 nucleoporins (nups). Structural studies of the NPC have been limited by its considerable size and complexity. Progress toward understanding t...
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| Format: | Article |
| Language: | en_US |
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Landes Bioscience
2014
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| Online Access: | http://hdl.handle.net/1721.1/85064 https://orcid.org/0000-0001-8012-1512 |
| _version_ | 1811095143669825536 |
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| author | Leksa, Nina Carolina Schwartz, Thomas |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Leksa, Nina Carolina Schwartz, Thomas |
| author_sort | Leksa, Nina Carolina |
| collection | MIT |
| description | The nuclear pore complex (NPC) regulates all traffic between the cytoplasm and the nucleus. It is a large protein assembly composed of multiple copies of ~30 nucleoporins (nups). Structural studies of the NPC have been limited by its considerable size and complexity. Progress toward understanding the structure of this nanomachine has benefited from its modular nature, which allows for this 40-60 MDa assembly to be broken down into subcomplexes that can be studied individually. While recent work by both crystallographers and electron microscopists has greatly enhanced our model of the NPC, the resolution gap between crystal and EM structures remains too large to confidently place individual proteins within the context of the fully assembled NPC. In an effort to arrive at a veritable model of the NPC, we solved the structure of several scaffold nups and defined the ancestral coatomer element (ACE1) common to a set of nucleoporins and COPII vesicle coat proteins. Subsequently, we proposed a lattice-like model of the NPC, analogous to the COPII lattice, in which ACE1 proteins form the edge elements and β-propellers form the vertex elements. Here, we review our recent studies, speculate on how interactions between subcomplexes of the NPC are mediated, and outline the steps and challenges that lay ahead on the path to understanding this enormous assembly in molecular detail. |
| first_indexed | 2024-09-23T16:11:03Z |
| format | Article |
| id | mit-1721.1/85064 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T16:11:03Z |
| publishDate | 2014 |
| publisher | Landes Bioscience |
| record_format | dspace |
| spelling | mit-1721.1/850642022-10-02T06:54:35Z Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges Leksa, Nina Carolina Schwartz, Thomas Massachusetts Institute of Technology. Department of Biology Leksa, Nina Carolina Schwartz, Thomas The nuclear pore complex (NPC) regulates all traffic between the cytoplasm and the nucleus. It is a large protein assembly composed of multiple copies of ~30 nucleoporins (nups). Structural studies of the NPC have been limited by its considerable size and complexity. Progress toward understanding the structure of this nanomachine has benefited from its modular nature, which allows for this 40-60 MDa assembly to be broken down into subcomplexes that can be studied individually. While recent work by both crystallographers and electron microscopists has greatly enhanced our model of the NPC, the resolution gap between crystal and EM structures remains too large to confidently place individual proteins within the context of the fully assembled NPC. In an effort to arrive at a veritable model of the NPC, we solved the structure of several scaffold nups and defined the ancestral coatomer element (ACE1) common to a set of nucleoporins and COPII vesicle coat proteins. Subsequently, we proposed a lattice-like model of the NPC, analogous to the COPII lattice, in which ACE1 proteins form the edge elements and β-propellers form the vertex elements. Here, we review our recent studies, speculate on how interactions between subcomplexes of the NPC are mediated, and outline the steps and challenges that lay ahead on the path to understanding this enormous assembly in molecular detail. National Institutes of Health (U.S.) (grant GM77537) Massachusetts Institute of Technology (Poitras Fellowship) Pew Charitable Trusts (Pew Scholar of the Biomedical Sciences) 2014-02-21T15:55:37Z 2014-02-21T15:55:37Z 2010-07 2011-03 Article http://purl.org/eprint/type/JournalArticle 1949-1034 http://hdl.handle.net/1721.1/85064 Leksa, Nina C., and Thomas U. Schwartz. “Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges.” Nucleus 1, no. 4 (July 1, 2010): 314-318. https://orcid.org/0000-0001-8012-1512 en_US http://dx.doi.org/10.4161/nucl.1.4.11798 Nucleus Creative Commons Attribution http://creativecommons.org/ application/pdf Landes Bioscience Landes Bioscience |
| spellingShingle | Leksa, Nina Carolina Schwartz, Thomas Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges |
| title | Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges |
| title_full | Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges |
| title_fullStr | Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges |
| title_full_unstemmed | Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges |
| title_short | Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges |
| title_sort | membrane coating lattice scaffolds in the nuclear pore and vesicle coats commonalities differences challenges |
| url | http://hdl.handle.net/1721.1/85064 https://orcid.org/0000-0001-8012-1512 |
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