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The Conserved Transmembrane Nucleoporin NDC1 Is Required for Nuclear Pore Complex Assembly in Vertebrate Cells

Authors
Journal
Molecular Cell
1097-2765
Publisher
Elsevier
Publication Date
Volume
22
Issue
1
Identifiers
DOI: 10.1016/j.molcel.2006.02.015
Disciplines
  • Biology
  • Chemistry
  • Medicine

Abstract

Summary Nuclear pore complexes (NPCs) are large proteinaceous channels embedded in the nuclear envelope (NE), through which exchange of molecules between the nucleus and cytosol occurs. Biogenesis of NPCs is complex and poorly understood. In particular, almost nothing is known about how NPCs are anchored in the NE. Here, we characterize vertebrate NDC1—a transmembrane nucleoporin conserved between yeast and metazoans. We show by RNA interference (RNAi) and biochemical depletion that NDC1 plays an important role in NPC and NE assembly in vivo and in vitro. RNAi experiments suggest a functional link between NDC1 and the soluble nucleoporins Nup93, Nup53, and Nup205. Importantly, NDC1 interacts with Nup53 in vitro. This suggests that NDC1 function involves forming a link between the NE membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane.

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