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The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes.

ABSTRACT: Nuclear pore complexes (NPCs) are large macromolecular assemblies that control all transport across the nuclear envelope. They are formed by about 30 nucleoporins (Nups), which can be roughly categorized into those forming the structural skeleton of the pore and those creating the central channel and thus providing the transport and gating properties of the NPC. Here we show that the conserved nucleoporin Nup93 is essential for NPC assembly and connects both portions of the NPC. Although the C-terminal domain of the protein is necessary and sufficient for the assembly of a minimal structural backbone, full-length Nup93 is required for the additional recruitment of the Nup62 complex and the establishment of transport-competent NPCs.

SUBMITTER: Sachdev R

PROVIDER: S-EPMC3279400 | biostudies-other | 2012 Feb

REPOSITORIES: biostudies-other

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The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes.

Sachdev Ruchika R Sieverding Cornelia C Flötenmeyer Matthias M Antonin Wolfram W

Molecular biology of the cell 20111214 4

Nuclear pore complexes (NPCs) are large macromolecular assemblies that control all transport across the nuclear envelope. They are formed by about 30 nucleoporins (Nups), which can be roughly categorized into those forming the structural skeleton of the pore and those creating the central channel and thus providing the transport and gating properties of the NPC. Here we show that the conserved nucleoporin Nup93 is essential for NPC assembly and connects both portions of the NPC. Although the C-t ...[more]

PMID: 22171326

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