Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
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| Authors: | Anne Chadrin Barbara Hess Mabel San Roman Xavier Gatti Bérangère Lombard Damarys Loew Yves Barral Benoit Palancade Valérie Doye |
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| Affiliation: | 1.Institut Jacques Monod, UMR 7592, Centre National de la Recherche Scientifique/Université Paris Diderot, 75013 Paris, France;2.Institute of Biochemistry, Department of Biology, Eidgenössische Technische Hochschule Zürich, CH-8093 Zürich, Switzerland;3.Institut Curie, Centre de Recherche, Laboratory of Proteomic Mass Spectrometry, 75248 Paris, France |
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| Abstract: | 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 with budding yeast NPCs. Pom33 becomes critical for yeast viability in the absence of a functional Nup84 complex or Ndc1 interaction network, which are two core NPC subcomplexes, and associates with the reticulon Rtn1. Moreover, POM33 loss of function impairs NPC distribution, a readout for a subset of genes required for pore biogenesis, including members of the Nup84 complex and RTN1. Consistently, we show that Pom33 is required for normal NPC density in the daughter nucleus and for proper NPC biogenesis and/or stability in the absence of Nup170. We hypothesize that, by modifying or stabilizing the nuclear envelope–NPC interface, Pom33 may contribute to proper distribution and/or efficient assembly of nuclear pores. |
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