期刊
JOURNAL OF CELL BIOLOGY
卷 189, 期 5, 页码 795-811出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200910043
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- Centre National de la Recherche Scientifique
- Institut Curie
- Ligue Nationale contre le Cancer (Equipe Labelisee) [2006, 2009]
- Agence Nationale de la Recherche [ANR 07-BLAN-0063-01]
- Eidgenossische Technische Hochschule Zurich
- Ministere de l'Enseignement Superieur et de la recherche
- Association pour la Recherche contre le Cancer
- Agence Nationale de la Recherche (ANR) [ANR-07-BLAN-0063] Funding Source: Agence Nationale de la Recherche (ANR)
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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