Nuclear Envelope: Nuclear Pore Complexity

Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly

During mitosis, the nuclear envelope merges with the endoplasmic reticulum (ER), and nuclear pore complexes are disassembled. In a current model for reassembly after mitosis, the nuclear envelope forms by a reshaping of ER tubules. For the assembly of pores, two major models have been proposed. In the insertion model, nuclear pore complexes are embedded in the nuclear envelope after their forma...

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Correspondence to Ulrike Kutay: [email protected] Y. Turgay’s present address is Dept. of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland. D.W. Gerlich’s present address is Institute of Molecular Biotechnology, 1030 Vienna, Austria. P. Meraldi’s present address is Centre Médical Universitaire, Université de Genève, CH-1211 Geneva, Switzerland. Abbreviations used in th...

Nuclear pores form de novo from both sides of the nuclear envelope.

Nuclear pore complexes are multiprotein channels that span the double lipid bilayer of the nuclear envelope. How new pores are inserted into the intact nuclear envelope of proliferating and differentiating eukaryotic cells is unknown. We found that the Nup107-160 complex was incorporated into assembly sites in the nuclear envelope from both the nucleoplasmic and the cytoplasmic sides. Nuclear p...

Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution

The biogenesis of nuclear pore complexes (NPCs) represents a paradigm for the assembly of high-complexity macromolecular structures. So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope. Here, we describe the identification and functional characterization of Pom33, a novel transmembrane protein dynamically associated w...

Chm7 and Heh1 form a nuclear envelope subdomain for nuclear pore complex quality control