Topology and Functional Domains of the Yeast Pore Membrane Protein Pom152p

Tcheperegine, Serguei E.; Marelli, Marcello; Wozniak, Richard W.

doi:10.1074/jbc.274.8.5252

Cited by 36 publications

(54 citation statements)

References 24 publications

(34 reference statements)

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“…As controls, the glycosylation states of a Pom152p-Suc2p myc fusion in pom152D cells and a Snl1p-Suc2p fusion in snl1D cells were monitored. Pom152p and Snl1p have opposite topologies with the C terminus sequestered in the ER/NE lumen and cytosol, respectively (Ho et al 1998;Tcheperegine et al 1999). The Pom152p-Suc2p myc fusion was sensitive to Endo H digestion as reflected by the migration shift ( Figure 1C, lanes 3 and 4).…”

Section: Resultsmentioning

confidence: 93%

“…lethality whereas a pom152D nic96-7 mutant is synthetically lethal Tcheperegine et al 1999). This might reflect allele specificity for the nic96 mutants, and/or these results might be further evidence of distinct roles for Pom152p and Pom34p.…”

Section: Discussionmentioning

confidence: 94%

“…Unlike Ndc1p, both Pom152p and Pom34p reside exclusively within the NPC (Wozniak et al 1994;Rout et al 2000). Pom152p is a type II integral membrane protein with a single transmembrane segment and the majority of the protein positioned in the NE lumen (Tcheperegine et al 1999). Several studies have revealed roles for Ndc1p and Pom152p in NPC molecular organization.…”

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confidence: 99%

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The Integral Membrane Protein Pom34p Functionally Links Nucleoporin Subcomplexes

2006

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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 pom34DN nup188D 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 pom34D pom152D double mutant was viable at all temperatures and showed no such defects. Interestingly, POM152 overexpression suppressed the synthetic lethality of pom34D nup170D and pom34D nup59D 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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Section: Resultsmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 94%

mentioning

confidence: 99%

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The Integral Membrane Protein Pom34p Functionally Links Nucleoporin Subcomplexes

2006

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“…4A). Ndc1 is an integral membrane protein that has overlapping functions with Pom152 and Pom34 in NPC biogenesis (Chial et al 1998;Tcheperegine et al 1999;Madrid et al 2006). The myosin like Mlp1 and Mlp2 are associated with the nuclear side of the NPC and have diverse roles in the retention of nonspliced mRNAs, nuclear transport, and SPB duplication (Strambio-de-Castillia et al 1999;Galy et al 2004;Niepel et al 2005).…”

Section: Eap1 Allows Bypass Of Mps2 Function By Inhibiting Translatiomentioning

confidence: 99%

The SESA network links duplication of the yeast centrosome with the protein translation machinery

Sezen¹,

Seedorf²,

Schiebel³

2009

Genes Dev.

134

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The yeast spindle pole body (SPB), the functional equivalent of mammalian centrosome, duplicates in G1/S phase of the cell cycle and then becomes inserted into the nuclear envelope. Here we describe a link between SPB duplication and targeted translation control. When insertion of the newly formed SPB into the nuclear envelope fails, the SESA network comprising the GYF domain protein Smy2, the translation inhibitor Eap1, the mRNAbinding protein Scp160 and the Asc1 protein, specifically inhibits initiation of translation of POM34 mRNA that encodes an integral membrane protein of the nuclear pore complex, while having no impact on other mRNAs. In response to SESA, POM34 mRNA accumulates in the cytoplasm and is not targeted to the ER for cotranslational translocation of the protein. Reduced level of Pom34 is sufficient to restore viability of mutants with defects in SPB duplication. We suggest that the SESA network provides a mechanism by which cells can regulate the translation of specific mRNAs. This regulation is used to coordinate competing events in the nuclear envelope.[Keywords: Regulation of translation; spindle pole body; nuclear pore complex; Smy2; Eap1; Scp160] Supplemental material is available at http://www.genesdev.org.

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“…Pom34p is a small, transmembrane NPC protein of unknown function (Rout et al 2000). Pom152p, like gp210 in mammalian cells, is a large, transmembrane glycoprotein with the majority of its mass in the NE lumen (Wozniak et al 1994;Tcheperegine et al 1999). Despite encoding the only large integral membrane protein in the yeast NPC, POM152 is not essential (Wozniak et al 1994).…”

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confidence: 99%

Nuclear Pore Complex Function in Saccharomyces cerevisiae Is Influenced by Glycosylation of the Transmembrane Nucleoporin Pom152p

et al. 2005

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The regulated transport of proteins across the nuclear envelope occurs through nuclear pore complexes (NPCs), which are composed of .30 different protein subunits termed nucleoporins. While some nucleoporins are glycosylated, little about the role of glycosylation in NPC activity is understood. We have identified loss-of-function alleles of ALG12, encoding a mannosyltransferase, as suppressors of a temperature-sensitive mutation in the gene encoding the FXFG-nucleoporin NUP1. We observe that nup1D cells import nucleophilic proteins more efficiently when ALG12 is absent, suggesting that glycosylation may influence nuclear transport. Conditional nup1 and nup82 mutations are partially suppressed by the glycosylation inhibitor tunicamycin, while nic96 and nup116 alleles are hypersensitive to tunicamycin treatment, further implicating glycosylation in NPC function. Because Pom152p is a glycosylated, transmembrane nucleoporin, we examined genetic interactions between pom152 mutants and nup1D. A nup1 deletion is lethal in combination with pom152D, as well as with truncations of the Nterminal and transmembrane regions of Pom152p. However, truncations of the N-glycosylated, lumenal domain of Pom152p and pom152 mutants lacking N-linked glycosylation sites are viable in combination with nup1D, suppress nup1D temperature sensitivity, and partially suppress the nuclear protein import defects associated with the deletion of NUP1. These data provide compelling evidence for a role for glycosylation in influencing NPC function.

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Topology and Functional Domains of the Yeast Pore Membrane Protein Pom152p

Cited by 36 publications

References 24 publications

The Integral Membrane Protein Pom34p Functionally Links Nucleoporin Subcomplexes

The Integral Membrane Protein Pom34p Functionally Links Nucleoporin Subcomplexes

The SESA network links duplication of the yeast centrosome with the protein translation machinery

Nuclear Pore Complex Function in Saccharomyces cerevisiae Is Influenced by Glycosylation of the Transmembrane Nucleoporin Pom152p

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