Functional Insights from Studies on the Structure of the Nuclear Pore and Coat Protein Complexes
Author(s) -
Thomas Schwartz
Publication year - 2013
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a013375
Subject(s) - nuclear pore , biology , endoplasmic reticulum , inner membrane , nucleus , microbiology and biotechnology , membrane , nuclear lamina , biophysics , lipid bilayer , nuclear protein , transcription factor , mitochondrion , gene , biochemistry
The nuclear envelope (NE) is a specific extension of the endoplasmic reticulum (ER) that wraps around the nucleus and enables the spatial separation of gene transcription and protein translation, one of the signature features of eukaryotes. Rather than being completely closed, the double lipid bilayer of the NE is perforated at sites where the inner and outer nuclear membranes fuse, resulting in circular openings lined with sharply bent membranes. These openings are filled with nuclear pore complexes (NPCs), enormous protein assemblies that facilitate nuclear transport. The scaffold components of the NPC surprisingly share interesting similarities with elements of coat protein complexes, which have general implications for function and evolution of these membrane-coating complexes. Here I discuss, from a structural perspective, what these findings might teach us.
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