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- Bernhard Hampoelz
- Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany;, ,
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- Amparo Andres-Pons
- Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany;, ,
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- Panagiotis Kastritis
- Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany;, ,
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- Martin Beck
- Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany;, ,
説明
<jats:p> Nuclear pore complexes (NPCs) mediate nucleocytoplasmic exchange. They are exceptionally large protein complexes that fuse the inner and outer nuclear membranes to form channels across the nuclear envelope. About 30 different protein components, termed nucleoporins, assemble in multiple copies into an intricate cylindrical architecture. Here, we review our current knowledge of the structure of nucleoporins and how those come together in situ. We delineate architectural principles on several hierarchical organization levels, including isoforms, posttranslational modifications, nucleoporins, and higher-order oligomerization of nucleoporin subcomplexes. We discuss how cells exploit this modularity to faithfully assemble NPCs. </jats:p>
収録刊行物
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- Annual Review of Biophysics
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Annual Review of Biophysics 48 (1), 515-536, 2019-05-06
Annual Reviews