The Integral Membrane Protein Pom34p Functionally Links Nucleoporin Subcomplexes

Miao, Mi; Ryan, Kathryn J.; Wente, Susan R.

doi:10.1534/genetics.105.052068

Cited by 52 publications

(75 citation statements)

References 90 publications

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“…This raises the possibility that nuclear pore complexes may cause an additional type of nuclear envelope alteration that affects SPB function. Several of the nucleoporin genes that upon deletion suppress mps3 mutants code for proteins implicated in nuclear pore complex insertion or assembly, including Nup157p, Nic96p, Nup188p, Pom152p, and Pom34p (Nehrbass et al 1996;Zabel et al 1996;Gomez-Ospina et al 2000;Madrid et al 2006;Miao et al 2006;Dawson et al 2009;Flemming et al 2009;Makio et al 2009;Onischenko et al 2009). Since many of these genes are not essential for viability, while nuclear pore complexes are essential, these gene deletions are unlikely to suppress the mps3-1 defect by eliminating nuclear pore complexes or drastically reducing their number.…”

Section: Discussionmentioning

confidence: 99%

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

et al. 2010

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The Saccharomyces cerevisiae nuclear membrane is part of a complex nuclear envelope environment also containing chromatin, integral and peripheral membrane proteins, and large structures such as nuclear pore complexes (NPCs) and the spindle pole body. To study how properties of the nuclear membrane affect nuclear envelope processes, we altered the nuclear membrane by deleting the SPO7 gene. We found that spo7D cells were sickened by the mutation of genes coding for spindle pole body components and that spo7D was synthetically lethal with mutations in the SUN domain gene MPS3. Mps3p is required for spindle pole body duplication and for a variety of other nuclear envelope processes. In spo7D cells, the spindle pole body defect of mps3 mutants was exacerbated, suggesting that nuclear membrane composition affects spindle pole body function. The synthetic lethality between spo7D and mps3 mutants was suppressed by deletion of specific nucleoporin genes. In fact, these gene deletions bypassed the requirement for Mps3p entirely, suggesting that under certain conditions spindle pole body duplication can occur via an Mps3p-independent pathway. These data point to an antagonistic relationship between nuclear pore complexes and the spindle pole body. We propose a model whereby nuclear pore complexes either compete with the spindle pole body for insertion into the nuclear membrane or affect spindle pole body duplication by altering the nuclear envelope environment. T HE nuclear envelope is composed of distinct outer and inner nuclear membranes. The outer nuclear membrane is continuous with the endoplasmic reticulum. The inner nuclear membrane is associated with a unique set of proteins, some of which mediate interactions between the nuclear envelope and chromatin (reviewed in Zhao et al. 2009). Nuclear pore complexes traverse both membranes and allow transport of proteins and solutes between the cytoplasm and the nucleus. The inner and outer nuclear membranes fuse in the region surrounding each nuclear pore complex.In animal cells, the nuclear envelope disassembles as cells enter mitosis and reassembles upon mitotic exit. Nuclear envelope breakdown allows the association of chromosomes with spindle microtubules, which are nucleated from centrosomes that reside in the cytoplasm. In contrast, certain types of fungi, such as the budding yeast Saccharomyces cerevisiae, undergo closed mitosis, where the nuclear envelope remains intact throughout the entire cell cycle. Closed mitosis is possible because the yeast centrosome-equivalent, the spindle pole body (SPB), is embedded in the nuclear envelope, allowing the SPB to nucleate both cytoplasmic and nuclear microtubules. SPB duplication requires a mechanism for inserting the new SPB into the nuclear envelope (reviewed in Jaspersen and Winey 2004). The new SPB begins to form in late G 1 /early S phase as satellite material deposited on the cytoplasmic face of an electron-dense region of the nuclear envelope, called the half-bridge. The satellite material matures into a dupl...

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Section: Discussionmentioning

confidence: 99%

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

et al. 2010

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“…They are part of the membrane ring of the NPC and as such important for NPC biogenesis (Fig. 9, step 1; Wozniak et al 1994;Chial et al 1998;Madrid et al 2006;Miao et al 2006;Alber et al 2007a,b;Onischenko et al 2009). A functional link between SPB insertion and NPCs, which are frequently observed near duplicating SPBs, was already proposed (Adams and Kilmartin 1999;Jaspersen and Winey 2004).…”

Section: Sesa Inhibits Initiation Of Translation Of Pom34 Mrnamentioning

confidence: 94%

“…Membrane localization of POM34 mRNA requires initiation of translation POM34 encodes an integral protein of the nuclear envelope (Miao et al 2006). Its translation should therefore occur at the ER (Rapoport 1990).…”

Section: Sesa Inhibits Translation Of Pom34 Mrnamentioning

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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“…The core scaffold is linked to the pore membrane through integral membrane proteins. So far, four membrane nucleoporins have been identified in different organisms: Pom34, Pom152, Pom33 and Ndc1 in yeast (Chadrin et al, 2010;Lau et al, 2004;Miao et al, 2006;Wozniak et al, 1994) and Gp210, Pom121 and Ndc1, which is the only one conserved as an integral pore membrane protein, in vertebrates (Gerace et al, 1982;Hallberg et al, 1993;Mans et al, 2004;Mansfeld et al, 2006;Stavru et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Nup53 interaction with Ndc1 and Nup155 are required for nuclear pore complex assembly

Eisenhardt

Redolfi

Antonin

2013

Journal of Cell Science

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Nuclear pore complexes (NPCs) are the gateways for nucleocytoplasmic exchange. The ordered assembly of these huge complexes from several hundred individual components into an intricate protein interaction network which deforms the two membranes of the nuclear envelope into a pore is only rudimentarily understood. Here, we show that the interaction between Nup53 and the integral pore membrane protein Ndc1 is essential for vertebrate NPC assembly. The Ndc1 binding site on Nup53 overlaps with a region that induces membrane bending and is specifically required to modulate this activity, suggesting that the membrane-deforming capability of Nup53 is adjusted during the NPC assembly process. We further demonstrate that the interaction of Nup53 and Nup155 has a crucial role in NPC formation as the main determinant of recruitment of Nup155 to the assembling pore. Overall, our results pinpoint the diversity of interaction modes accomplished by Nup53, highlighting this protein as an essential link between the pore membrane and the NPC, and as a crucial factor in the formation of the pore membrane.

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The Integral Membrane Protein Pom34p Functionally Links Nucleoporin Subcomplexes

Cited by 52 publications

References 90 publications

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

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

Nup53 interaction with Ndc1 and Nup155 are required for nuclear pore complex assembly

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