The yeast Cbk1 kinase regulates mRNA localization via the mRNA-binding protein Ssd1

Kurischko, Cornelia; Kim, Hong Kyung; Kuravi, Venkata K.; Pratzka, Juliane; Luca, Francis C.

doi:10.1083/jcb.201011061

Cited by 57 publications

(142 citation statements)

References 61 publications

(152 reference statements)

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“…In brief, Ssd1 is an RNAseII-related protein broadly conserved in fungi that appears to lack catalytic activity; it has been implicated in numerous processes. It binds specific mRNAs and suppresses their translation, and Cbk1 efficiently directly negatively regulates this Ssd1 function in vivo (Hogan et al 2008;Jansen et al 2009;Kurischko et al 2011a). This is critical for cell wall remodeling during bud growth; however, the Ssd1 translational control system's important role in cell morphogenesis outside of the process of mother/ daughter separation is not discussed further in this chapter.…”

Section: Ram Network Controls Translation Of Cell Separation Proteinsmentioning

confidence: 99%

“…Ssd1 likely assembles a translationally silent mRNP in the nucleus: it associates with unspliced and centromeric mRNAs, interacts with the phosphorylated Cterminal tail of RNA polymerase II, and requires a sequence that can function as an NLS (Phatnani et al 2004;Jansen et al 2006;Hogan et al 2008;Kurischko et al 2011b). The mechanisms and precise function of Ssd1's control of translation remain poorly understood, but since RAM network proteins concentrate at the bud neck during cell separation, the Ssd1 circuit could allow the cytokinesis site to exert posttranscriptional control over the expression of proteins needed at different stages of the process (Nelson et al 2003;Jansen et al 2006;Kurischko et al 2011a).…”

Section: Ram Network Controls Translation Of Cell Separation Proteinsmentioning

confidence: 99%

“…Translation rate measurements show that Ssd1-associated messages are significantly suppressed when Cbk1 activity is acutely blocked (Jansen et al 2009). Ssd1 can localize to cytoplasmic granules known as P-bodies, which are associated with translational suppression (Balagopal and Parker 2009;Jansen et al 2009;Kurischko et al 2011a), but Ssd1 can clearly carry out its translational repression function in cells lacking these structures. Ssd1 likely assembles a translationally silent mRNP in the nucleus: it associates with unspliced and centromeric mRNAs, interacts with the phosphorylated Cterminal tail of RNA polymerase II, and requires a sequence that can function as an NLS (Phatnani et al 2004;Jansen et al 2006;Hogan et al 2008;Kurischko et al 2011b).…”

Section: Ram Network Controls Translation Of Cell Separation Proteinsmentioning

confidence: 99%

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Mitotic Exit and Separation of Mother and Daughter Cells

2012

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Productive cell proliferation involves efficient and accurate splitting of the dividing cell into two separate entities. This orderly process reflects coordination of diverse cytological events by regulatory systems that drive the cell from mitosis into G1. In the budding yeast Saccharomyces cerevisiae, separation of mother and daughter cells involves coordinated actomyosin ring contraction and septum synthesis, followed by septum destruction. These events occur in precise and rapid sequence once chromosomes are segregated and are linked with spindle organization and mitotic progress by intricate cell cycle control machinery. Additionally, critical parts of the mother/daughter separation process are asymmetric, reflecting a form of fate specification that occurs in every cell division. This chapter describes central events of budding yeast cell separation, as well as the control pathways that integrate them and link them with the cell cycle.

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Section: Ram Network Controls Translation Of Cell Separation Proteinsmentioning

confidence: 99%

Section: Ram Network Controls Translation Of Cell Separation Proteinsmentioning

confidence: 99%

Section: Ram Network Controls Translation Of Cell Separation Proteinsmentioning

confidence: 99%

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Mitotic Exit and Separation of Mother and Daughter Cells

2012

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“…The resulting RNA transcripts are also subject to further regulation at the levels of RNA processing, transport, localization, translation, and degradation. The added dimensions of regulation provided by RNAbinding proteins (RBPs) enable more precise temporal, spatial, and stoichiometric control of protein production (Wang et al 2002;Paquin et al 2007;Jansen et al 2009;Kurischko et al 2011). Specific RBPs bind to distinct sets of mRNAs, typically encoding proteins destined for similar subcellular localizations or with related biological functions, suggesting a model in which concerted, combinatorial binding of specific mRNAs by specific sets of RBPs can affect the post-transcriptional fate of potentially every mRNA in the cell (Hieronymus and Silver 2003;Gerber et al 2004;Ong et al 2004;Keene 2007a,b;Hogan et al 2008).…”

mentioning

confidence: 99%

Quantitative proteomic analysis reveals concurrent RNA–protein interactions and identifies new RNA-binding proteins in Saccharomyces cerevisiae

et al. 2013

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A growing body of evidence supports the existence of an extensive network of RNA-binding proteins (RBPs) whose combinatorial binding affects the post-transcriptional fate of every mRNA in the cell-yet we still do not have a complete understanding of which proteins bind to mRNA, which of these bind concurrently, and when and where in the cell they bind. We describe here a method to identify the proteins that bind to RNA concurrently with an RBP of interest, using quantitative mass spectrometry combined with RNase treatment of affinity-purified RNA-protein complexes. We applied this method to the known RBPs Pab1, Nab2, and Puf 3. Our method significantly enriched for known RBPs and is a clear improvement upon previous approaches in yeast. Our data reveal that some reported protein-protein interactions may instead reflect simultaneous binding to shared RNA targets. We also discovered more than 100 candidate RBPs, and we independently confirmed that 77% (23/30) bind directly to RNA. The previously recognized functions of the confirmed novel RBPs were remarkably diverse, and we mapped the RNA-binding region of one of these proteins, the transcriptional coactivator Mbf1, to a region distinct from its DNA-binding domain. Our results also provided new insights into the roles of Nab2 and Puf 3 in post-transcriptional regulation by identifying other RBPs that bind simultaneously to the same mRNAs. While existing methods can identify sets of RBPs that interact with common RNA targets, our approach can determine which of those interactions are concurrent-a crucial distinction for understanding post-transcriptional regulation.

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“…We have previously found that a multicopy SSD1 encoding an RNA-binding protein suppressed the growth defect caused by the ccr4⌬ khd1⌬ double mutation (16). Since the RNA-binding protein Ssd1 is involved in the regulation of many genes as well as Khd1 (17,34,35), the Pbp1 and Rpl12 proteins may also involve the expression of multiple genes in a negative effect on cell growth in the ccr4⌬ khd1⌬ double mutant cells. Since Rpl12a and Rpl12b stabilize the structure of the P-protein stalk by interacting with the P0/P1/P2 complex (32,33), the rpl12a⌬ and rpl12b⌬ mutations as well as the pbp1⌬ mutation decrease the translation of multiple target mRNAs that influence cell growth.…”

Section: Discussionmentioning

confidence: 99%

Pbp1 Is Involved in Ccr4- and Khd1-Mediated Regulation of Cell Growth through Association with Ribosomal Proteins Rpl12a and Rpl12b

Kimura

Irie

2013

Eukaryot Cell

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The Saccharomyces cerevisiae Pbp1 [poly(A)-binding protein (Pab1)-binding protein] is believed to be involved in RNA metabolism and regulation of translation, since Pbp1 regulates a length of poly(A) tail and is involved in stress granule (SG) formation. However, a physiological function of Pbp1 remains unclear, since the pbp1⌬ mutation has no obvious effect on cell growth. In this study, we showed that PBP1 genetically interacts with CCR4 and KHD1, which encode a cytoplasmic deadenylase and an RNA-binding protein, respectively. Ccr4 and Khd1 modulate a signal from Rho1 in the cell wall integrity pathway by regulating the expression of RhoGEF and RhoGAP, and the double deletion of CCR4 and KHD1 confers a severe growth defect displaying cell lysis. We found that the pbp1⌬ mutation suppressed the growth defect caused by the ccr4⌬ khd1⌬ mutation. The pbp1⌬ mutation also suppressed the growth defect caused by double deletion of POP2, encoding another cytoplasmic deadenylase, and KHD1. Deletion of the gene encoding previously known Pbp1-interacting factor Lsm12, Pbp4, or Mkt1 did not suppress the growth defect of the ccr4⌬ khd1⌬ mutant, suggesting that Pbp1 acts independently of these factors in this process. We then screened novel Pbp1-interacting factors and found that Pbp1 interacts with ribosomal proteins Rpl12a and Rpl12b. Similarly to the pbp1⌬ mutation, the rpl12a⌬ and rpl12b⌬ mutations also suppressed the growth defect caused by the ccr4⌬ khd1⌬ mutation. Our results suggest that Pbp1 is involved in the Ccr4-and Khd1-mediated regulation of cell growth through the association with Rpl12a and Rpl12b.

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The yeast Cbk1 kinase regulates mRNA localization via the mRNA-binding protein Ssd1

Abstract: In the absence of Cbk1 phosphorylation Ssd1-associated mRNAs are redirected from sites of polarized cell growth to stress granules and P-bodies.

Cited by 57 publications

References 61 publications

Mitotic Exit and Separation of Mother and Daughter Cells

Mitotic Exit and Separation of Mother and Daughter Cells

Quantitative proteomic analysis reveals concurrent RNA–protein interactions and identifies new RNA-binding proteins in Saccharomyces cerevisiae

Pbp1 Is Involved in Ccr4- and Khd1-Mediated Regulation of Cell Growth through Association with Ribosomal Proteins Rpl12a and Rpl12b

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