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

• Published in: Molecular cell Vol. 22; no. 1; pp. 93 - 103
• Main Authors: Mansfeld, Jörg, Güttinger, Stephan, Hawryluk-Gara, Lisa A., Panté, Nelly, Mall, Moritz, Galy, Vincent, Haselmann, Uta, Mühlhäusser, Petra, Wozniak, Richard W., Mattaj, Iain W., Kutay, Ulrike, Antonin, Wolfram
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07-04-2006; Cell Press
• Subjects: Amino Acid Sequence; Animals; Cell Membrane - metabolism; Cellular Biology; Cloning, Molecular; Conserved Sequence; HeLa Cells; Humans; Life Sciences; Metazoa; Molecular Sequence Data; Nuclear Envelope - metabolism; Nuclear Pore - physiology; Nuclear Pore Complex Proteins - chemistry; Nuclear Pore Complex Proteins - genetics; Nuclear Pore Complex Proteins - metabolism; Osteosarcoma - metabolism; Peptide Fragments - immunology; Proteolipids; Rabbits; RNA, Small Interfering - pharmacology; Sequence Homology, Amino Acid; Subcellular Processes; Xenopus laevis - metabolism; Xenopus Proteins - chemistry; Xenopus Proteins - genetics; Xenopus Proteins - metabolism
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/j.molcel.2006.02.015

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.