Literature DB >> 21326946

Characterization of the membrane-coating Nup84 complex: paradigm for the nuclear pore complex structure.

Erik W Debler1, Kuo-Chiang Hsia, Vivien Nagy, Hyuk-Soo Seo, André Hoelz.   

Abstract

Nuclear pore complexes (NPCs) function as selective gates for nucleocytoplasmic transport. Although the NPC was discovered more than half a century ago, our knowledge of NPC components in atomic detail has exploded only over the past few years. Recent structural, biochemical, and in vivo studies of NPC components, in particular the membrane-coating heptameric Nup84 complex, have shed light onto the NPC architecture as well as onto its dynamic nature. Striking similarities were revealed between the components of the NPC and of coat protein complexes in the endocytic and secretory pathways, supporting their common evolutionary origin in a progenitor protocoatomer. Here, we summarize these findings and discuss emerging concepts that underlie the molecular architecture and the dynamics of the NPC. We conclude that the uncovered principles are not limited to the NPC, but are likely to extend to other macromolecular assemblies.

Entities:  

Keywords:  binding promiscuity; coat protein complex; coatomer; crystallography; dynamic interaction; electron microscopy; macromolecular assembly; nucleocytoplasmic transport; nucleoporin; vesicle coats

Mesh:

Substances:

Year:  2010        PMID: 21326946      PMCID: PMC3030690          DOI: 10.4161/nucl.1.2.11120

Source DB:  PubMed          Journal:  Nucleus        ISSN: 1949-1034            Impact factor:   4.197


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Journal:  Proc Natl Acad Sci U S A       Date:  2009-08-11       Impact factor: 11.205

6.  Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.

Authors:  Vivien Nagy; Kuo-Chiang Hsia; Erik W Debler; Martin Kampmann; Andrew M Davenport; Günter Blobel; André Hoelz
Journal:  Proc Natl Acad Sci U S A       Date:  2009-10-01       Impact factor: 11.205

7.  The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.

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4.  Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex.

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6.  Crystal structure of the N-terminal domain of Nup358/RanBP2.

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  6 in total

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