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Article

The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function.

Molecular biology of the cell - 1 Feb 1998

Ho A K, Raczniak G A, Ives E B, Wente S R

Abstract excerpt

Integral membrane proteins are predicted to play key roles in the biogenesis and function of nuclear pore complexes (NPCs). Revealing how the transport apparatus is assembled will be critical for understanding the mechanism of nucleocytoplasmic transport. We observed that expression of the carboxyl-terminal 200 amino acids of the nucleoporin Nup116p had no effect on wild-type yeast cells, but it rendered the...

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Identifiers

PMID: 9450961
DOI: 10.1091/mbc.9.2.355
PMCID: PMC25263

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Source receipt: pubmed, retrieved 7 Sept 2026.

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The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function.PMID 9450961Read ↗

The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor.Semantic proximity Read ↗

A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic.Semantic proximity Read ↗

Topology and functional domains of the yeast pore membrane protein Pom152p.Semantic proximity Read ↗

Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.Semantic proximity Read ↗

The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function.Semantic proximity Read ↗

The integral membrane protein Pom34p functionally links nucleoporin subcomplexes.Semantic proximity Read ↗

Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.Semantic proximity Read ↗

Mutations affecting spindle pole body and mitotic exit network function are synthetically lethal with a deletion of the nucleoporin NUP1 in S. cerevisiae.Semantic proximity Read ↗

The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex.Semantic proximity Read ↗

Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif.Semantic proximity Read ↗

nup1 mutants exhibit pleiotropic defects in nuclear pore complex function.Semantic proximity Read ↗

A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly.Semantic proximity Read ↗

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