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Article ; Online: Available for a limited time only: Regulating gene expression through mRNA turnover.

Gallouzi, Imed Eddine / von Roretz, Christopher

Seminars in cell & developmental biology

2014 Volume 34, Page(s) 1

MeSH term(s)	Animals ; Gene Expression Regulation ; Humans ; RNA Stability ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	RNA, Messenger
Language	English
Publishing date	2014-10
Publishing country	England
Document type	Editorial ; Introductory Journal Article
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2014.06.008
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Article ; Online: Transportin 2 regulates apoptosis through the RNA-binding protein HuR.

von Roretz, Christopher / Macri, Angelo M / Gallouzi, Imed-Eddine

The Journal of biological chemistry

2011 Volume 286, Issue 29, Page(s) 25983–25991

Abstract: In response to severe stress, apoptotic cell death is engaged. Apoptosis is a well orchestrated process that involves the activation and implication of many factors. In this study, we identified a role for the nuclear trafficking factor TRN2 (transportin ...

Abstract	In response to severe stress, apoptotic cell death is engaged. Apoptosis is a well orchestrated process that involves the activation and implication of many factors. In this study, we identified a role for the nuclear trafficking factor TRN2 (transportin 2) in cell death. TRN2 is normally responsible for the nuclear import of the RNA-binding protein HuR. During apoptosis, however, HuR accumulates in the cytoplasm. This is due to the caspase-mediated cleavage of the cytoplasmic fraction of HuR. One of the cleavage fragments generated by this processing of HuR interacts with TRN2 and thus blocks the re-import of HuR into the nucleus. This concentrates HuR in the cytoplasm, advancing apoptosis. Therefore, increasing or decreasing the levels of TRN2 has an inverse consequential effect on cell death, demonstrating for the first time the role of a nucleocytoplasmic transport factor in apoptosis.
MeSH term(s)	Apoptosis ; Gene Knockdown Techniques ; HeLa Cells ; Humans ; Protein Transport ; RNA, Small Interfering/genetics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; beta Karyopherins/deficiency ; beta Karyopherins/genetics ; beta Karyopherins/metabolism
Chemical Substances	RNA, Small Interfering ; RNA-Binding Proteins ; TNPO2 protein, human ; beta Karyopherins
Language	English
Publishing date	2011-06-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.216184
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Article ; Online: Protein kinase RNA/FADD/caspase-8 pathway mediates the proapoptotic activity of the RNA-binding protein human antigen R (HuR).

von Roretz, Christopher / Gallouzi, Imed-Eddine

The Journal of biological chemistry

2010 Volume 285, Issue 22, Page(s) 16806–16813

Abstract: The RNA-binding protein human antigen R (HuR) has been implicated in apoptosis in multiple ways. Several studies have shown that in response to a variety of stresses HuR promotes the expression of proapoptotic mRNAs, whereas others reported its ... ...

Abstract	The RNA-binding protein human antigen R (HuR) has been implicated in apoptosis in multiple ways. Several studies have shown that in response to a variety of stresses HuR promotes the expression of proapoptotic mRNAs, whereas others reported its regulatory effect on antiapoptotic messages. We recently showed that in response to severe stress, HuR is cleaved to generate two cleavage products (CPs), HuR-CP1 (24 kDa) and HuR-CP2 (8 kDa), by which it promotes apoptotic cell death. Here, we show that this cleavage event is dependent on protein kinase RNA (PKR). Surprisingly, although in response to the apoptotic inducer staurosporine PKR itself is not phosphorylated, PKR triggers the cleavage of HuR via its downstream effector FADD that in turn activates the caspase-8/caspase-3 pathway. This effect, however, does not require the phosphorylation of the eukaryotic translation initiation factor 2alpha. Additionally, we observed that these HuR-CPs are sufficient to trigger cell death in the absence of activation of the PKR pathway. Therefore, our results support a model whereby in response to lethal stress, PKR, without being phosphorylated, activates the FADD/caspase-8/caspase-3 pathway to trigger HuR cleavage, and the HuR-CPs are then capable of promoting apoptosis.
MeSH term(s)	Animals ; Antigens, Surface/metabolism ; Apoptosis ; Caspase 8/metabolism ; Cell Line ; ELAV Proteins ; ELAV-Like Protein 1 ; Fas-Associated Death Domain Protein/metabolism ; HeLa Cells ; Humans ; Mice ; Mice, Knockout ; Models, Biological ; Phosphorylation ; Protein Binding ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; eIF-2 Kinase/chemistry
Chemical Substances	Antigens, Surface ; ELAV Proteins ; ELAV-Like Protein 1 ; ELAVL1 protein, human ; FADD protein, human ; Fas-Associated Death Domain Protein ; RNA-Binding Proteins ; eIF-2 Kinase (EC 2.7.11.1) ; Caspase 8 (EC 3.4.22.-)
Language	English
Publishing date	2010-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M109.087320
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Article ; Online: Planning your every move: the role of β-actin and its post-transcriptional regulation in cell motility.

Artman, Lise / Dormoy-Raclet, Virginie / von Roretz, Christopher / Gallouzi, Imed-Eddine

Seminars in cell & developmental biology

2014 Volume 34, Page(s) 33–43

Abstract: Cell motility is a tightly regulated process that involves the polymerization of actin subunits. The formation of actin filaments is controlled through a variety of protein factors that accelerate or perturb the polymerization process. As is the case for ...

Abstract	Cell motility is a tightly regulated process that involves the polymerization of actin subunits. The formation of actin filaments is controlled through a variety of protein factors that accelerate or perturb the polymerization process. As is the case for most biological events, cell movement is also controlled at the level of gene expression. Growing research explains how the β-actin isoform of actin is particularly regulated through post-transcriptional events. This includes the discovery of multiple sites in the 3' untranslated region of β-actin mRNA to which RNA-binding proteins can associate. The control such proteins have on β-actin expression, and as a result, cell migration, continues to develop, and presents a thorough process that involves guiding an mRNA out of the nucleus, to a specific cytosolic destination, and then controlling the translation and decay of this message. In this review we will provide an overview on the recent progress regarding the mechanisms by which actin polymerization modulates cell movement and invasion and we will discuss the importance of post-transcriptional regulatory events in β-actin mediated effects on these processes.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/genetics ; Actins/metabolism ; Animals ; Cell Movement ; Gene Expression Regulation ; Humans ; Polyadenylation ; Protein Biosynthesis ; Protein Multimerization ; RNA Transport ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Signal Transduction
Chemical Substances	Actins ; RNA, Messenger
Language	English
Publishing date	2014-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2014.05.012
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Article: Protein Kinase RNA/FADD/Caspase-8 Pathway Mediates the Proapoptotic Activity of the RNA-binding Protein Human Antigen R (HuR)

von Roretz, Christopher / Gallouzi, Imed-Eddine

Journal of biological chemistry. 2010 May 28, v. 285, no. 22

2010

Abstract	The RNA-binding protein human antigen R (HuR) has been implicated in apoptosis in multiple ways. Several studies have shown that in response to a variety of stresses HuR promotes the expression of proapoptotic mRNAs, whereas others reported its regulatory effect on antiapoptotic messages. We recently showed that in response to severe stress, HuR is cleaved to generate two cleavage products (CPs), HuR-CP1 (24 kDa) and HuR-CP2 (8 kDa), by which it promotes apoptotic cell death. Here, we show that this cleavage event is dependent on protein kinase RNA (PKR). Surprisingly, although in response to the apoptotic inducer staurosporine PKR itself is not phosphorylated, PKR triggers the cleavage of HuR via its downstream effector FADD that in turn activates the caspase-8/caspase-3 pathway. This effect, however, does not require the phosphorylation of the eukaryotic translation initiation factor 2α. Additionally, we observed that these HuR-CPs are sufficient to trigger cell death in the absence of activation of the PKR pathway. Therefore, our results support a model whereby in response to lethal stress, PKR, without being phosphorylated, activates the FADD/caspase-8/caspase-3 pathway to trigger HuR cleavage, and the HuR-CPs are then capable of promoting apoptosis.
Language	English
Dates of publication	2010-0528
Size	p. 16806-16813.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article ; Online: Decoding ARE-mediated decay: is microRNA part of the equation?

von Roretz, Christopher / Gallouzi, Imed-Eddine

The Journal of cell biology

2008 Volume 181, Issue 2, Page(s) 189–194

Abstract: Messenger ribonucleic acids (mRNAs) containing adenine/uridine-rich elements (AREs) in their 3' untranslated region are particularly labile, allowing for the regulation of expression for growth factors, oncoproteins, and cytokines. The regulators, ... ...

Abstract	Messenger ribonucleic acids (mRNAs) containing adenine/uridine-rich elements (AREs) in their 3' untranslated region are particularly labile, allowing for the regulation of expression for growth factors, oncoproteins, and cytokines. The regulators, effectors, and location of ARE-mediated decay (AMD) have been investigated by many groups in recent years, and several links have been found between AMD and microRNA-mediated decay. We highlight these similarities, along with recent advances in the field of AMD, and also mention how there is still much left unknown surrounding this specialized mode of mRNA decay.
MeSH term(s)	3' Untranslated Regions/genetics ; Adenine/analysis ; Animals ; Gene Expression Regulation ; Humans ; Kinetics ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Models, Genetic ; Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Transcription, Genetic ; Uridine/analysis
Chemical Substances	3' Untranslated Regions ; MicroRNAs ; RNA, Messenger ; Adenine (JAC85A2161) ; Uridine (WHI7HQ7H85)
Language	English
Publishing date	2008-04-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.200712054
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Article: Decoding ARE-mediated decay: is microRNA part of the equation?

von Roretz, Christopher / Gallouzi, Imed-Eddine

Journal of cell biology. 2008 Apr. 21, v. 181, no. 2

2008

Abstract	Messenger ribonucleic acids (mRNAs) containing adenine/uridine-rich elements (AREs) in their 3' untranslated region are particularly labile, allowing for the regulation of expression for growth factors, oncoproteins, and cytokines. The regulators, effectors, and location of ARE-mediated decay (AMD) have been investigated by many groups in recent years, and several links have been found between AMD and microRNA-mediated decay. We highlight these similarities, along with recent advances in the field of AMD, and also mention how there is still much left unknown surrounding this specialized mode of mRNA decay.
Language	English
Dates of publication	2008-0421
Size	p. 189-194.
Publishing place	The Rockefeller University Press
Document type	Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
Database	NAL-Catalogue (AGRICOLA)

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Article: HuR and myogenesis: Being in the right place at the right time

von Roretz, Christopher / Beauchamp, Pascal / Di Marco, Sergio / Gallouzi, Imed-Eddine

Biochimica et biophysica acta. Molecular cell research. 2011 Sept., v. 1813, no. 9

2011

Abstract: The process of muscle cell differentiation into myotubes, termed myogenesis, depends on a complex coordination of myogenic factors, many of which are regulated post-transcriptionally. HuR, an mRNA-binding protein, is responsible for regulating the ... ...

Abstract	The process of muscle cell differentiation into myotubes, termed myogenesis, depends on a complex coordination of myogenic factors, many of which are regulated post-transcriptionally. HuR, an mRNA-binding protein, is responsible for regulating the expression of several such myogenic factors by stabilizing their mRNAs. The critical role for HuR in myogenesis also involves the nucleocytoplasmic shuttling ability of this protein. Indeed, in order to perform its stabilizing functions, HuR must accumulate in the cytoplasm. This requires its dissociation from the import factor Transportin 2 (TRN2) which is actually caused by the cleavage of a portion of cytoplasmic HuR. In this review, we describe the roles of HuR during myogenesis, and the mechanisms regulating its cytoplasmic accumulation. This article is part of a Special Issue entitled: Regulation of Signaling and Cellular Fate through Modulation of Nuclear Protein Import.
Keywords	cell differentiation ; coordination compounds ; cytoplasm ; dissociation ; messenger RNA ; muscle development ; muscles ; protein transport
Language	English
Dates of publication	2011-09
Size	p. 1663-1667.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	283444-3
ISSN	0167-4889
ISSN	0167-4889
DOI	10.1016/j.bbamcr.2011.01.036
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Article ; Online: Turnover of AU-rich-containing mRNAs during stress: a matter of survival.

von Roretz, Christopher / Di Marco, Sergio / Mazroui, Rachid / Gallouzi, Imed-Eddine

Wiley interdisciplinary reviews. RNA

2011 Volume 2, Issue 3, Page(s) 336–347

Abstract: Cells undergo various adaptive measures in response to stress. Among these are specific changes in the posttranscriptional regulation of various genes. In particular, the turnover of mRNA is modified to either increase or decrease the abundance of ... ...

Abstract	Cells undergo various adaptive measures in response to stress. Among these are specific changes in the posttranscriptional regulation of various genes. In particular, the turnover of mRNA is modified to either increase or decrease the abundance of certain target messages. Some of the best-studied mRNAs that are affected by stress are those that contain adenine/uridine-rich elements (AREs) in their 3'-untranslated regions. ARE-containing mRNAs are involved in many important cellular processes and are normally labile, but in response to stress they are differentially regulated through the concerted efforts of ARE-binding proteins (AUBPs) such as HuR, AUF1, tristetraprolin, BRF1, and KSRP, along with microRNA-mediated effects. Additionally, the fate of ARE-containing mRNAs is modified by inducing their localization to stress granules or mRNA processing bodies. Coordination of these various mechanisms controls the turnover of ARE-containing mRNAs, and thereby enables proper responses to cellular stress. In this review, we discuss how AUBPs regulate their target mRNAs in response to stress, along with the involvement of cytoplasmic granules in this process.
MeSH term(s)	3' Untranslated Regions ; Adenine/chemistry ; Base Composition ; Cytoplasmic Granules/metabolism ; ELAV Proteins/metabolism ; MicroRNAs/metabolism ; Models, Biological ; RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Stress, Physiological ; Tristetraprolin/metabolism ; Uracil/chemistry
Chemical Substances	3' Untranslated Regions ; ELAV Proteins ; MicroRNAs ; RNA, Messenger ; RNA-Binding Proteins ; Tristetraprolin ; adenine-uracil dimers ; Uracil (56HH86ZVCT) ; Adenine (JAC85A2161)
Language	English
Publishing date	2011-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2634714-3
ISSN	1757-7012 ; 1757-7004
ISSN (online)	1757-7012
ISSN	1757-7004
DOI	10.1002/wrna.55
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Article: HuR and myogenesis: being in the right place at the right time.

von Roretz, Christopher / Beauchamp, Pascal / Di Marco, Sergio / Gallouzi, Imed-Eddine

Biochimica et biophysica acta

2011 Volume 1813, Issue 9, Page(s) 1663–1667

Abstract	The process of muscle cell differentiation into myotubes, termed myogenesis, depends on a complex coordination of myogenic factors, many of which are regulated post-transcriptionally. HuR, an mRNA-binding protein, is responsible for regulating the expression of several such myogenic factors by stabilizing their mRNAs. The critical role for HuR in myogenesis also involves the nucleocytoplasmic shuttling ability of this protein. Indeed, in order to perform its stabilizing functions, HuR must accumulate in the cytoplasm. This requires its dissociation from the import factor Transportin 2 (TRN2) which is actually caused by the cleavage of a portion of cytoplasmic HuR. In this review, we describe the roles of HuR during myogenesis, and the mechanisms regulating its cytoplasmic accumulation. This article is part of a Special Issue entitled: Regulation of Signaling and Cellular Fate through Modulation of Nuclear Protein Import.
MeSH term(s)	Active Transport, Cell Nucleus/physiology ; Animals ; Antigens, Surface/genetics ; Antigens, Surface/physiology ; Caspases/physiology ; Cell Differentiation/physiology ; ELAV Proteins ; ELAV-Like Protein 1 ; Gene Knockdown Techniques ; Humans ; Karyopherins/physiology ; Muscle Cells/cytology ; Muscle Cells/physiology ; Muscle Development/physiology ; Protein Processing, Post-Translational ; RNA-Binding Proteins/antagonists & inhibitors ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/physiology ; Signal Transduction/physiology
Chemical Substances	Antigens, Surface ; ELAV Proteins ; ELAV-Like Protein 1 ; ELAVL1 protein, human ; Karyopherins ; RNA-Binding Proteins ; Caspases (EC 3.4.22.-)
Language	English
Publishing date	2011-09
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2011.01.036
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