Andrej Sali Lab

This page lists some of the commentaries on our recent papers about a method to determine the structures of macromolecular assemblies and its application to the nuclear pore complex.

1. Frank Alber, Svetlana Dokudovskaya, Liesbeth M. Veenhoff, Wenzhu Zhang, Julia Kipper, Damien Devos, Adisetyantari Suprapto, Orit Karni-Schmidt, Rosemary Williams, Brian T. Chait, Michael P. Rout & Andrej Sali. Determining the architectures of macromolecular assemblies. Nature 450, 683-694, 2007.

Nuclear pore complexes (NPCs) are proteinaceous assemblies of approximately 50 MDa that selectively transport cargoes across the nuclear envelope. To determine the molecular architecture of the yeast NPC, we collected a diverse set of biophysical and proteomic data, and developed a method for using these data to localize the NPCs 456 constituent proteins (see the accompanying paper). Our structure reveals that half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. This scaffold forms an interlaced network that coats the entire curved surface of the nuclear envelope membrane within which the NPC is embedded. The selective barrier for transport is formed by large numbers of proteins with disordered regions that line the inner face of the scaffold. The NPC consists of only a few structural modules that resemble each other in terms of the configuration of their homologous constituents, the most striking of these being a 16-fold repetition of 'columns'. These findings provide clues to the evolutionary origins of the NPC.

2. Frank Alber, Svetlana Dokudovskaya, Liesbeth M. Veenhoff, Wenzhu Zhang, Julia Kipper, Damien Devos, Adisetyantari Suprapto, Orit Karni-Schmidt, Rosemary Williams, Brian T. Chait, Andrej Sali & Michael P. Rout. The molecular architecture of the nuclear pore complex. Nature 450, 695-701, 2007.

Nuclear pore complexes (NPCs) are proteinaceous assemblies of approximately 50 MDa that selectively transport cargoes across the nuclear envelope. To determine the molecular architecture of the yeast NPC, we collected a diverse set of biophysical and proteomic data, and developed a method for using these data to localize the NPCs 456 constituent proteins (see the accompanying paper). Our structure reveals that half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. This scaffold forms an interlaced network that coats the entire curved surface of the nuclear envelope membrane within which the NPC is embedded. The selective barrier for transport is formed by large numbers of proteins with disordered regions that line the inner face of the scaffold. The NPC consists of only a few structural modules that resemble each other in terms of the configuration of their homologous constituents, the most striking of these being a 16-fold repetition of columns. These findings provide clues to the evolutionary origins of the NPC.

These two NPC papers where highlighted in:

The favorite cell biology paper in 2007, selected by Nature editors, This year in Nature

Highlighted in Methods to Watch, in Nature Methods

Highlighted in Editor's Summary, Nature

Highlighted in News and Views, Nature

Among the top two dozen examples of important advances in chemistry-based research in 2007; 2007 Chemistry Highlights, Chemical & Engineering News

Highlighted in Latest News, Probing Large Proteins, Chemical & Engineering News:

Voted the top two most interesting recent papers in biology by Faculty of 1000