Article
The cAMP-dependent protein kinase signaling pathway is a key regulator of P body foci formation.
Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Molecular cell (impact factor:
14.61).
09/2011;
43(6):973-81.
DOI:10.1016/j.molcel.2011.06.032
Source: PubMed
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Article: ARE-mRNA degradation requires the 5'-3' decay pathway.
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ABSTRACT: As an important mode of suppressing gene expression, messenger RNAs containing an AU-rich element (ARE) in the 3' untranslated region are rapidly degraded in the cytoplasm. ARE-mediated mRNA decay (AMD) is initiated by deadenylation, and in vitro studies have indicated that subsequent degradation occurs in the 3'-5' direction through a complex of exonucleases termed the exosome. An alternative pathway of mRNA degradation occurs at processing bodies, cytoplasmic foci that contain decapping enzymes, the 5'-3' exonuclease Xrn1 and the Lsm1-7 heptamer. To determine which of the two pathways is important for AMD in live cells, we targeted components of both pathways using short interfering RNA in human HT1080 cells. We show that Xrn1 and Lsm1 are essential for AMD. On the other side, out of three exosome components tested, only knockdown of PmScl-75 caused a strong inhibition of AMD. Our results show that mammalian cells, similar to yeast, require the 5'-3' Xrn1 pathway to degrade ARE-mRNAs.EMBO Reports 02/2006; 7(1):72-7. · 7.36 Impact Factor -
Article: Cloning and characterization of the high-affinity cAMP phosphodiesterase of Saccharomyces cerevisiae.
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ABSTRACT: A gene, PDE2, has been cloned from the yeast Saccharomyces cerevisiae that, when present in high copy, reverses the phenotypic effects of RAS2Val19, a mutant form of the RAS2 gene that renders yeast cells sensitive to heat shock and starvation. It has previously been shown that the RAS proteins are potent activators of yeast adenylate cyclase. We report here that PDE2 encodes a high-affinity cAMP phosphodiesterase that shares sequence homology with animal cell phosphodiesterases. These results therefore imply that the effects of RAS2Val19 are mediated through its changes in cAMP concentration.Proceedings of the National Academy of Sciences 01/1987; 83(24):9303-7. · 9.68 Impact Factor -
Article: "Sleeping beauty": quiescence in Saccharomyces cerevisiae.
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ABSTRACT: The cells of organisms as diverse as bacteria and humans can enter stable, nonproliferating quiescent states. Quiescent cells of eukaryotic and prokaryotic microorganisms can survive for long periods without nutrients. This alternative state of cells is still poorly understood, yet much benefit is to be gained by understanding it both scientifically and with reference to human health. Here, we review our knowledge of one "model" quiescent cell population, in cultures of yeast grown to stationary phase in rich media. We outline the importance of understanding quiescence, summarize the properties of quiescent yeast cells, and clarify some definitions of the state. We propose that the processes by which a cell enters into, maintains viability in, and exits from quiescence are best viewed as an environmentally triggered cycle: the cell quiescence cycle. We synthesize what is known about the mechanisms by which yeast cells enter into quiescence, including the possible roles of the protein kinase A, TOR, protein kinase C, and Snf1p pathways. We also discuss selected mechanisms by which quiescent cells maintain viability, including metabolism, protein modification, and redox homeostasis. Finally, we outline what is known about the process by which cells exit from quiescence when nutrients again become available.Microbiology and Molecular Biology Reviews 07/2004; 68(2):187-206. · 13.02 Impact Factor
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Keywords
assembly process
cAMP-dependent protein kinase
conserved constituent
discrete sites
eukaryotic cells
general relevance
larger P body aggregates
larger ribonucleoprotein
long-term survival
mechanisms regulating foci formation
mRNA processing
mRNAs
P bodies
P body foci
phosphorylating Pat1
processing bodies
quiescent cells
RNP assemblies
RNP complex
stationary phase cells