Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner

Frey, Steffen; Pool, Martin; Seedorf, Matthias

doi:10.1074/jbc.m009430200

Cited by 102 publications

(126 citation statements)

References 50 publications

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“…The latter distributions were as expected, since most ribosomes are present in cytoplasm while Scp160 is enriched with ribosomes at the ER (Supplemental Fig. S9A; Frey et al 2001). Together, the cellular distributions of Scp160, Sec61, Pgk1, and Rpl35 proteins demonstrate that the fractionation into membrane and cytoplasmic fractions was successful.…”

Section: Sesa Inhibits Translation Of Pom34 Mrnasupporting

confidence: 79%

“…We therefore tested whether the interaction of the mRNA-binding protein Scp160 with Smy2 and Eap1 could restrict translation inhibition to a specific subset of mRNAs, which may bind to SESA through the known mRNA-binding protein Scp160 (Frey et al 2001). Attempts to identify mRNAs that were clearly regulated by Scp160 on the level of translation were unsuccessful.…”

Section: Eap1 Allows Bypass Of Mps2 Function By Inhibiting Translatiomentioning

confidence: 99%

“…Fractions were analyzed by immunoblotting using the indicated antibodies. The lower molecular weight band (asterisk) is a cytoplasmic degradation product of Scp160 (Frey et al 2001). POM34 and SEC61 mRNA levels were determined by quantitative RT-PCR from three independent experiments.…”

Section: Sesa Inhibits Translation Of Pom34 Mrnamentioning

confidence: 99%

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

Sezen¹,

Seedorf²,

Schiebel³

2009

Genes Dev.

Self Cite

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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Section: Sesa Inhibits Translation Of Pom34 Mrnasupporting

confidence: 79%

Section: Eap1 Allows Bypass Of Mps2 Function By Inhibiting Translatiomentioning

confidence: 99%

See 1 more Smart Citation

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

Sezen¹,

Seedorf²,

Schiebel³

2009

Genes Dev.

Self Cite

134

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show abstract

“…2d). Functionally, this contact site appears important because RACK1 interacts with the polysomeassociated protein Scp160, which promotes mRNA binding 15,16 . RACK1 is involved in the PKC (protein kinase C) dependent phosphorylation of initiation factor 4E, which promotes polysome-dependent de novo protein synthesis 17 .…”

Section: Resultsmentioning

confidence: 99%

The molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomes

et al. 2014

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During protein synthesis, several ribosomes bind to a single messenger RNA (mRNA) forming large macromolecular assemblies called polyribosomes. Here we report the detailed molecular structure of a 100 MDa eukaryotic poly-ribosome complex derived from cryo electron tomography, sub-tomogram averaging and pseudo-atomic modelling by crystal structure fitting. The structure allowed the visualization of the three functional parts of the polysome assembly, the central core region that forms a rather compact left-handed supramolecular helix, and the more open regions that harbour the initiation and termination sites at either ends. The helical region forms a continuous mRNA channel where the mRNA strand bridges neighbouring exit and entry sites of the ribosomes and prevents mRNA looping between ribosomes. This structure provides unprecedented insights into protein-and RNAmediated inter-ribosome contacts that involve conserved sites through 40S subunits and long protruding RNA expansion segments, suggesting a role in stabilizing the overall polyribosomal assembly.

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“…Notably, we reported that the eIF4E-binding protein Eap1p functions as a translation initiation inhibitor in cells treated with CPZ and in mutants that block secretory or endocytic pathways (e.g., sec4 and end3). Interestingly, Eap1p was shown to interact genetically and biochemically with Scp160p (Mendelsohn et al 2003), a ribosomal protein localized to the endoplasmic reticulum (Frey et al 2001). It will be thus interesting to determine if Eap1p is essentially dedicated to the control of the expression of genes whose products are transported along the secretory pathway.…”

Section: Figmentioning

confidence: 99%

Membrane stress is coupled to a rapid translational control of gene expression in chlorpromazine-treated cells

et al. 2007

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Chlorpromazine (CPZ) is a small permeable cationic amphiphilic molecule that inserts into membrane bilayers and binds to anionic lipids such as poly-phosphoinositides (PIs). Since PIs play important roles in many cellular processes, including signaling and membrane traYcking pathways, it has been proposed that CPZ aVects cellular growth functions by preventing the recruitment of proteins with speciWc PI-binding domains. In this study, we have investigated the biological eVects of CPZ in the yeast Saccharomyces cerevisiae. We screened a collection of approximately 4,800 gene knockout mutants, and found that mutants defective in membrane traYcking between the late-Golgi and endosomal compartments are highly sensitive to CPZ. Microscopy and transport analyses revealed that CPZ aVects membrane structure of organelles, blocks membrane transport and activates the unfolded protein response (UPR). In addition, CPZ-treatment induces phosphorylation of the translation initiation factor (eIF2 ), which reduces the general rate of protein synthesis and stimulates the production of Gcn4p, a major transcription factor that is activated in response to environmental stresses. Altogether, our results reveal that membrane stress within the cells rapidly activates an important gene expression program, which is followed by a general inhibition of protein synthesis. Remarkably, the increase of phosphorylated eIF2 and protein synthesis inhibition were also detected in CPZ-treated NIH-3T3 Wbroblasts, suggesting the existence of a conserved mechanism of translational regulation that operates during a membrane stress.

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Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner

Cited by 102 publications

References 50 publications

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

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

The molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomes

Membrane stress is coupled to a rapid translational control of gene expression in chlorpromazine-treated cells

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