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Article

Topology and functional domains of the yeast pore membrane protein Pom152p.

The Journal of biological chemistry - 19 Feb 1999

Tcheperegine S E, Marelli M, Wozniak R W

Abstract excerpt

Integral membrane proteins associated with the nuclear pore complex (NPC) are likely to play an important role in the biogenesis of this structure. Here we have examined the functional roles of domains of the yeast pore membrane protein Pom152p in establishing its topology and its interactions with other NPC proteins. The topology of Pom152p was evaluated by alkaline extraction, protease protection, and...

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Identifiers

PMID: 9988776
DOI: 10.1074/jbc.274.8.5252

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Topology and functional domains of the yeast pore membrane protein Pom152p.PMID 9988776Read ↗

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

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

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

The Ran GTPase cycle is required for yeast nuclear pore complex assembly.Semantic proximity Read ↗

The Nup155-mediated organisation of inner nuclear membrane proteins is independent of Nup155 anchoring to the metazoan nuclear pore complex.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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The fission yeast Schizosaccharomyces pombe has two importin-alpha proteins, Imp1p and Cut15p, which have common and unique functions in nucleocytoplasmic transport and cell cycle progression.Semantic proximity Read ↗

A dominant-negative form of POM121 binds chromatin and disrupts the two separate modes of nuclear pore assembly.Semantic proximity Read ↗

Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly.Semantic proximity Read ↗

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