ArticleGenetics2006
The integral membrane protein Pom34p functionally links nucleoporin subcomplexes.
Article in Genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 56 citations in OpenAlex.
- The nuclear envelope protein TMEM209 is an integral component of the nuclear pore complex and interacts with Nup210.Journal of cell science · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane.The Journal of cell biology · 2023Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- The ESCRT-III complex is required for nuclear pore complex sequestration and regulates gamete replicative lifespan in budding yeast meiosis.Nucleus (Austin, Tex.) · 2020Article
- Review
- Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis.The Journal of cell biology · 2018Article
- Compositionally distinct nuclear pore complexes of functionally distinct dimorphic nuclei in the ciliateJournal of cell science · 2017Article
- Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.Structure (London, England : 1993) · 2017Article
- The nuclear pore complex: understanding its function through structural insight.Nature reviews. Molecular cell biology · 2017Review
- Article
- Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum.Molecular biology of the cell · 2015Article
- Nuclear pore basket proteins are tethered to the nuclear envelope and can regulate membrane curvature.Developmental cell · 2015Article
- Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.The EMBO journal · 2012Article
- The yeast nuclear pore complex and transport through it.Genetics · 2012Article
- Brr6 drives the Schizosaccharomyces pombe spindle pole body nuclear envelope insertion/extrusion cycle.The Journal of cell biology · 2011Article
- Nuclear pore complex-a coat specifically tailored for the nuclear envelope.Current opinion in cell biology · 2011Review
- Lumenal interactions in nuclear pore complex assembly and stability.Molecular biology of the cell · 2011Article
- Changes in the nuclear envelope environment affect spindle pole body duplication in Saccharomyces cerevisiae.Genetics · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Here we have examined the function of Pom34p, a novel membrane protein in Saccharomyces cerevisiae, localized to nuclear pore complexes (NPCs). Membrane topology analysis revealed that Pom34p is a double-pass transmembrane protein with both the amino (N) and carboxy (C) termini positioned on the cytosolic/pore face. The network of genetic interactions between POM34 and genes encoding other nucleoporins was established and showed specific links between Pom34p function and Nup170p, Nup188p, Nup59p, Gle2p, Nup159p, and Nup82p. The transmembrane domains of Pom34p in addition to either the N- or C-terminal region were necessary for its function in different double mutants. We further characterized the pom34deltaN nup188delta mutant and found it to be perturbed in both NPC structure and function. Mislocalization of a subset of nucleoporins harboring phenylalanine-glycine repeats was observed, and nuclear import capacity for the Kap104p and Kap121p pathways was inhibited. In contrast, the pom34delta pom152delta double mutant was viable at all temperatures and showed no such defects. Interestingly, POM152 overexpression suppressed the synthetic lethality of pom34delta nup170delta and pom34delta nup59delta mutants. We speculate that multiple integral membrane proteins, either within the nuclear pore domain or in the nuclear envelope, execute coordinated roles in NPC structure and function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.