The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules

Wilczynska, Ania; Aigueperse, Christelle; Kress, Michel; Dautry, François; Weil, Dominique

doi:10.1242/jcs.01692

Cited by 273 publications

(329 citation statements)

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“…Because an association of DDX6 and SGs has been demonstrated recently (Wilczynska et al, 2005), we further investigated whether DDX6 and ATXN2, which itself is a component of SGs (Ralser et al, 2005a), colocalize under stress conditions. We primarily used the cell line DU145, because DU145 cells were previously used for studying the assembly of SGs (Kedersha et al, 1999(Kedersha et al, , 2000.…”

Section: Ddx6 Interacts With the Lsm/lsmad Domain Of Atxn2mentioning

confidence: 98%

“…Whereas DDX6 localizes to distinct cytoplasmic foci representing P-bodies (Cougot et al, 2004;Wilczynska et al, 2005), ATXN2 seems to be evenly distributed throughout the cytoplasm of mammalian cells, for example, COS-1, HEK293T, and SH-SY5Y; no obvious accumulation of endogenous ATXN2 in particular cellular structures was observed (Ralser et al, 2005a,c; Figure 2A, control). Because an association of DDX6 and SGs has been demonstrated recently (Wilczynska et al, 2005), we further investigated whether DDX6 and ATXN2, which itself is a component of SGs (Ralser et al, 2005a), colocalize under stress conditions. We primarily used the cell line DU145, because DU145 cells were previously used for studying the assembly of SGs (Kedersha et al, 1999(Kedersha et al, , 2000.…”

Section: Ddx6 Interacts With the Lsm/lsmad Domain Of Atxn2mentioning

confidence: 99%

“…Interestingly, under conditions of certain environmental stresses, P-bodies can localize to cytoplasmic stress granules (SGs) (Kedersha et al, 2005;Wilczynska et al, 2005). These cellular structures represent other ribonucleoprotein granules that seem to be in a dynamic equilibrium with polysomes as well and assemble and disassemble very rapidly in the cytoplasm of plant and mammalian cells after subjected to environmental stresses .…”

Section: Introductionmentioning

confidence: 99%

“…SGs contain several ribonucleoproteins and a number of mRNAstabilizing and -destabilizing factors such as elongation initiation factors, ribosomal subunits, RNA binding proteins, RNA stability factors, the poly(A)-binding protein (PABP) as well as the proteins TIA-1 and TIAR, which are essential for This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06 -12-1120) on February 7, 2007. SG assembly . Recently, the RasGAP-associated endoribonuclease G3BP and the translational regulator CPEB have been shown to be part of SGs and induce the assembly of SGs if overexpressed (Tourriere et al, 2003;Wilczynska et al, 2005). Interestingly, the survival motor neuron protein involved in the disorder spinal muscular atrophy and ataxin-2 (ATXN2) involved in the neurodegenerative disorder spinocerebellar ataxia type 2 (SCA2) are components of these cellular structures as well (Hua and Zhou, 2004;Ralser et al, 2005a).…”

Section: Introductionmentioning

confidence: 99%

“…P-bodies represent dynamic structures that are in an equilibrium with polysomes and contain nontranslating mRNA . Remarkably, recent work demonstrated that mRNA molecules entering P-bodies can also be stored and return to a translational active state in yeast .Interestingly, under conditions of certain environmental stresses, P-bodies can localize to cytoplasmic stress granules (SGs) (Kedersha et al, 2005;Wilczynska et al, 2005). These cellular structures represent other ribonucleoprotein granules that seem to be in a dynamic equilibrium with polysomes as well and assemble and disassemble very rapidly in the cytoplasm of plant and mammalian cells after subjected to environmental stresses .…”

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confidence: 99%

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Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules

Nonhoff

Ralser

Welzel

et al. 2007

MBoC

308

320

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Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation. INTRODUCTIONAn essential step in the control of global gene expression in eukaryotes is the regulation of mRNA translation and degradation. Shortening of the poly(A) tail is the initial step to trigger mRNA for decay in two major mRNA degradation pathways in eukaryotic cells (Bernstein and Ross, 1989;Peltz et al., 1991;Decker and Parker, 1994;Beelman and Parker, 1995). In one pathway, the deadenylated mRNA is degraded by a cytoplasmic protein complex, the exosome, consisting of a number of exonucleases with 3Ј-5Ј activity (Butler, 2002). In the other pathway, shortening of the poly(A) tail leads to the removal of the cap structure of the mRNA by the decapping proteins DCP1 and DCP2 facilitating 5Ј-3Ј degradation of the mRNA through the exoribonuclease XRN1 (Beelman and Parker, 1995;Butler, 2002). These proteins colocalize in discrete cytoplasmic foci in mammalian cells, termed processing bodies or P-bodies (also known as DCP1-or GW182-bodies), indicating that mRNA decay is restricted to distinct cytoplasmic compartments in mammalian cells (van Dijk et al., 2002;Cougot et al., 2004). The human protein CCR4, which is involved in mRNA deadenylation, the decapping stimulating LSm proteins LSm1-7, the DEAD/Hbox RNA helicase DDX6 (also known as RCK/p54), GW182, and Ge-1 are components of P-bodies (Bouveret et al., 2000;Eystathioy et al., 2002;Ingelfinger et al., 2002; LykkeAndersen, 2002;Cougot et al., 2004;Yu et al., 2005). Moreover, the RNA-associated protein 55, hEDC3, Hedls as well as factors of the RISC complex localize to P-bodies in mammalian cells (Fenger-Gron et al., 2005;Liu et al., 2005;Sen and Blau, 2005;Yang et al., 2006). P-bodies represent dynamic structures that are in an equilibrium with polysomes and contain nontranslating mRNA . Remarkably, recent work demonstrated that mRNA molecules entering P-bodies can a...

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Section: Ddx6 Interacts With the Lsm/lsmad Domain Of Atxn2mentioning

confidence: 98%

Section: Ddx6 Interacts With the Lsm/lsmad Domain Of Atxn2mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules

Nonhoff

Ralser

Welzel

et al. 2007

MBoC

308

320

View full text Add to dashboard Cite

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mRNPs meet stress granules

Sheinberger

Shav‐Tal

2017

FEBS Letters

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Edited by Wilhelm JustStress granules are cytoplasmic structures that form in response to a variety of cellular stresses. They contain mRNAs and many proteins including numerous types of RNA-binding proteins, and have been studied in connection to major cellular events such as protein synthesis as well as disease. Despite the well-known fact that stress granules encapsulate mRNPs (mRNA-protein complexes), much of the research has naturally focused on the protein components of stress granules. The specific details of mRNP entry into and exit from stress granules and the functional reasons for these dynamics are not fully understood. Here, we review studies that have concentrated on the aspects of mRNP accumulation in stress granules and produced quantitative data concerning mRNP/stress granule interactions.

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Cpeb1 expression is post‐transcriptionally regulated by AUF1, CPEB1, and microRNAs

Hayashi

Tanaka

et al. 2021

FEBS Open Bio

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Cytoplasmic polyadenylation element binding protein 1 (CPEB1) regulates the translation of numerous mRNAs. We previously showed that AU-rich binding factor 1 (AUF1) regulates Cpeb1 expression through the 3' untranslated region (3'UTR). To investigate the molecular basis of the regulatory potential of the Cpeb1 3'UTR, here we performed reporter analyses that examined expression levels of Gfp reporter mRNA containing the Cpeb1 3'UTR. Our findings indicate that CPEB1 represses the translation of Cpeb1 mRNA, and that miR-145a-5p and let-7b-5p are involved in the reduction of Cpeb1 expression in the absence of AUF1. These results suggest that Cpeb1 expression is post-transcriptionally regulated by AUF1, CPEB1, and microRNAs.

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The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules

Cited by 273 publications

References 33 publications

Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules

Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules

mRNPs meet stress granules

Cpeb1 expression is post‐transcriptionally regulated by AUF1, CPEB1, and microRNAs

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