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

Sezen, Bengii; Seedorf, Matthias; Schiebel, Elmar

doi:10.1101/gad.524209

Cited by 75 publications

(145 citation statements)

References 68 publications

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“…For example, the expression of STE12, GPA2, and CLN1 was shown to be translationally upregulated in caf20D cells during filamentous growth, and STE12 regulation was dependent on Caf20 (Park et al 2006b). Eap1 (together with Scp160, Asc1, and Smy2) is involved in translational repression of the POM34 mRNA (Sezen et al 2009). These data support the idea that the 4E-BPs can interact with and repress the translation of particular mRNA targets, possibly via interactions with other sequencespecific mRNA binding proteins, similar to examples from higher eukaryotes (Kong and Lasko 2012).…”

Section: Regulating Eif4e-eif4g Interactions By 4e-bpsmentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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In this review, we provide an overview of protein synthesis in the yeast Saccharomyces cerevisiae. The mechanism of protein synthesis is well conserved between yeast and other eukaryotes, and molecular genetic studies in budding yeast have provided critical insights into the fundamental process of translation as well as its regulation. The review focuses on the initiation and elongation phases of protein synthesis with descriptions of the roles of translation initiation and elongation factors that assist the ribosome in binding the messenger RNA (mRNA), selecting the start codon, and synthesizing the polypeptide. We also examine mechanisms of translational control highlighting the mRNA cap-binding proteins and the regulation of GCN4 and CPA1 mRNAs.

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Section: Regulating Eif4e-eif4g Interactions By 4e-bpsmentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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“…The C. elegans genome contains three additional genes that encode well-conserved GYF domains, but none show any sequence similarity with SAO-1 outside of the GYF domain (Kofler and Freund 2006). In yeast, GYFdomain proteins have been associated with a variety of cellular functions, such as COPII vesicle formation (Higashio et al 2008), membrane traffic (Georgiev et al 2008), genespecific inhibition of translation initiation (Sezen et al 2009), and mRNA splicing (Bialkowska and Kurlandzka 2002). Identification of binding partners for human GYF domains also supports involvement in vesicle transport and mRNA processing (Kofler et al 2009;Ash et al 2010).…”

Section: Genotype Of Mothermentioning

confidence: 99%

Notch Signaling Is Antagonized by SAO-1, a Novel GYF-Domain Protein That Interacts with the E3 Ubiquitin Ligase SEL-10 in Caenorhabditis elegans

et al. 2012

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Notch signaling pathways can be regulated through a variety of cellular mechanisms, and genetically compromised systems provide useful platforms from which to search for the responsible modulators. The Caenorhabditis elegans gene aph-1 encodes a component of g-secretase, which is essential for Notch signaling events throughout development. By looking for suppressors of the incompletely penetrant aph-1(zu147) mutation, we identify a new gene, sao-1 (suppressor of aph-one), that negatively regulates aph-1(zu147) activity in the early embryo. The sao-1 gene encodes a novel protein that contains a GYF protein-protein interaction domain and interacts specifically with SEL-10, an Fbw7 component of SCF E3 ubiquitin ligases. We demonstrate that the embryonic lethality of aph-1(zu147) mutants can be suppressed by removing sao-1 activity or by mutations that disrupt the SAO-1-SEL-10 protein interaction. Decreased sao-1 activity also influences Notch signaling events when they are compromised at different molecular steps of the pathway, such as at the level of the Notch receptor GLP-1 or the downstream transcription factor LAG-1. Combined analysis of the SAO-1-SEL-10 protein interaction and comparisons of sao-1 and sel-10 genetic interactions suggest a possible role for SAO-1 as an accessory protein that participates with SEL-10 in downregulation of Notch signaling. This work provides the first mutant analysis of a GYF-domain protein in either C. elegans or Drosophila and introduces a new type of Fbw7-interacting protein that acts in a subset of Fbw7 functions.

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“…Specific nucleoporin deletions suppress the growth defects of mps3 mutants: It was previously reported that deletion of genes coding for the POM nucleoporins Pom152p or Pom34p can rescue defects seen in certain mutants that disrupt SPB insertion, including ndc1, bbp1, and mps2 mutants (Chial et al 1998;Sezen et al 2009). To test whether POM gene deletions could also relieve defects associated with MPS3 mutation, POM152 and POM34 were individually deleted in haploid strains containing either wild-type MPS3 or mps3-1 alleles.…”

Section: Spb Mutant Allelementioning

confidence: 99%

“…Moreover, while there is considerable overlap between the nucleoporin deletions that suppress mps2D and mps3-1, the spectrum of suppressing mutants is not identical: nup188D could partially suppress mps3-1 but not mps2D (Sezen et al 2009), and nup157D suppressed mps3-1 but not mps2-1 (see below).…”

Section: Spb Mutant Allelementioning

confidence: 99%

“…To test this, POM152 and POM34 were individually deleted in haploid strains containing spc42-11 or mps2-1 and assayed for growth on rich media at 23°and 37°. The mps2-1 allele was used as a control because POM deletions are known to rescue this mutant (Sezen et al 2009). Neither POM gene deletion rescued the temperature sensitivity of the spc42-11 allele ( Figure 6B; data not shown).…”

Section: Spb Mutant Allelementioning

confidence: 99%

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

Cited by 75 publications

References 68 publications

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Notch Signaling Is Antagonized by SAO-1, a Novel GYF-Domain Protein That Interacts with the E3 Ubiquitin Ligase SEL-10 in Caenorhabditis elegans

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

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