RapamycinFungusV1, Main, Exploration, bibRecord, 000208

The DEAD-box RNA helicase Ded1 has a role in the translational response to TORC1 inhibition.

Identifieur interne : 000208 ( Main/Exploration ); précédent : 000207; suivant : 000209

The DEAD-box RNA helicase Ded1 has a role in the translational response to TORC1 inhibition.

Auteurs : Peyman P. Aryanpur [États-Unis] ; David M. Renner [États-Unis] ; Emily Rodela [États-Unis] ; Telsa M. Mittelmeier [États-Unis] ; Aaron Byrd [États-Unis] ; Timothy A. Bolger [États-Unis]

Source :

Molecular biology of the cell [ 1939-4586 ] ; 2019.

RBID : pubmed:31141444

Descripteurs français

English descriptors

KwdEn :
- 5' Untranslated Regions (MeSH), Cytoplasm (metabolism), DEAD-box RNA Helicases (genetics), DEAD-box RNA Helicases (metabolism), Eukaryotic Initiation Factor-4F (metabolism), Nucleic Acid Conformation (MeSH), Peptide Chain Elongation, Translational (MeSH), Protein Biosynthesis (MeSH), RNA, Messenger (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Transcription Factors (antagonists & inhibitors), Transcription Factors (genetics), Transcription Factors (metabolism).
MESH :
- chemical , antagonists & inhibitors : Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , genetics : DEAD-box RNA Helicases, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : DEAD-box RNA Helicases, Eukaryotic Initiation Factor-4F, RNA, Messenger, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical : 5' Untranslated Regions.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cytoplasm, Saccharomyces cerevisiae.
- Nucleic Acid Conformation, Peptide Chain Elongation, Translational, Protein Biosynthesis.

Abstract

Ded1 is a DEAD-box RNA helicase with essential roles in translation initiation. It binds to the eukaryotic initiation factor 4F (eIF4F) complex and promotes 48S preinitiation complex assembly and start-site scanning of 5' untranslated regions of mRNAs. Most prior studies of Ded1 cellular function were conducted in steady-state conditions during nutrient-rich growth. In this work, however, we examine its role in the translational response during target of rapamycin (TOR)C1 inhibition and identify a novel function of Ded1 as a translation repressor. We show that C-terminal mutants of DED1 are defective in down-regulating translation following TORC1 inhibition using rapamycin. Furthermore, following TORC1 inhibition, eIF4G1 normally dissociates from translation complexes and is degraded, and this process is attenuated in mutant cells. Mapping of the functional requirements for Ded1 in this translational response indicates that Ded1 enzymatic activity and interaction with eIF4G1 are required, while homo-oligomerization may be dispensable. Our results are consistent with a model wherein Ded1 stalls translation and specifically removes eIF4G1 from translation preinitiation complexes, thus removing eIF4G1 from the translating mRNA pool and leading to the codegradation of both proteins. Shared features among DED1 orthologues suggest that this role is conserved and may be implicated in pathologies such as oncogenesis.

DOI: 10.1091/mbc.E18-11-0702
PubMed: 31141444
PubMed Central: PMC6743465

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000265
to stream Main, to step Curation: 000265

Le document en format XML

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<term>DEAD-box RNA Helicases (genetics)</term>
<term>DEAD-box RNA Helicases (metabolism)</term>
<term>Eukaryotic Initiation Factor-4F (metabolism)</term>
<term>Nucleic Acid Conformation (MeSH)</term>
<term>Peptide Chain Elongation, Translational (MeSH)</term>
<term>Protein Biosynthesis (MeSH)</term>
<term>RNA, Messenger (metabolism)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (antagonists & inhibitors)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Transcription Factors (antagonists & inhibitors)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (métabolisme)</term>
<term>Biosynthèse des protéines (MeSH)</term>
<term>Conformation d'acide nucléique (MeSH)</term>
<term>Cytoplasme (métabolisme)</term>
<term>DEAD-box RNA helicases (génétique)</term>
<term>DEAD-box RNA helicases (métabolisme)</term>
<term>Facteur-4F d'initiation eucaryote (métabolisme)</term>
<term>Facteurs de transcription (antagonistes et inhibiteurs)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Régions 5' non traduites (MeSH)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Élongation de la traduction (MeSH)</term>
</keywords>
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<term>Transcription Factors</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DEAD-box RNA Helicases</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
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<term>Eukaryotic Initiation Factor-4F</term>
<term>RNA, Messenger</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>5' Untranslated Regions</term>
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<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>DEAD-box RNA helicases</term>
<term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
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<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term>
<term>Cytoplasme</term>
<term>DEAD-box RNA helicases</term>
<term>Facteur-4F d'initiation eucaryote</term>
<term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
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<term>Protein Biosynthesis</term>
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<term>Régions 5' non traduites</term>
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<front><div type="abstract" xml:lang="en">Ded1 is a DEAD-box RNA helicase with essential roles in translation initiation. It binds to the eukaryotic initiation factor 4F (eIF4F) complex and promotes 48S preinitiation complex assembly and start-site scanning of 5' untranslated regions of mRNAs. Most prior studies of Ded1 cellular function were conducted in steady-state conditions during nutrient-rich growth. In this work, however, we examine its role in the translational response during target of rapamycin (TOR)C1 inhibition and identify a novel function of Ded1 as a translation repressor. We show that C-terminal mutants of <i>DED1</i>
 are defective in down-regulating translation following TORC1 inhibition using rapamycin. Furthermore, following TORC1 inhibition, eIF4G1 normally dissociates from translation complexes and is degraded, and this process is attenuated in mutant cells. Mapping of the functional requirements for Ded1 in this translational response indicates that Ded1 enzymatic activity and interaction with eIF4G1 are required, while homo-oligomerization may be dispensable. Our results are consistent with a model wherein Ded1 stalls translation and specifically removes eIF4G1 from translation preinitiation complexes, thus removing eIF4G1 from the translating mRNA pool and leading to the codegradation of both proteins. Shared features among <i>DED1</i>
 orthologues suggest that this role is conserved and may be implicated in pathologies such as oncogenesis.</div>
</front>
</TEI>
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<Month>06</Month>
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<ArticleTitle>The DEAD-box RNA helicase Ded1 has a role in the translational response to TORC1 inhibition.</ArticleTitle>
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<Abstract><AbstractText>Ded1 is a DEAD-box RNA helicase with essential roles in translation initiation. It binds to the eukaryotic initiation factor 4F (eIF4F) complex and promotes 48S preinitiation complex assembly and start-site scanning of 5' untranslated regions of mRNAs. Most prior studies of Ded1 cellular function were conducted in steady-state conditions during nutrient-rich growth. In this work, however, we examine its role in the translational response during target of rapamycin (TOR)C1 inhibition and identify a novel function of Ded1 as a translation repressor. We show that C-terminal mutants of <i>DED1</i>
 are defective in down-regulating translation following TORC1 inhibition using rapamycin. Furthermore, following TORC1 inhibition, eIF4G1 normally dissociates from translation complexes and is degraded, and this process is attenuated in mutant cells. Mapping of the functional requirements for Ded1 in this translational response indicates that Ded1 enzymatic activity and interaction with eIF4G1 are required, while homo-oligomerization may be dispensable. Our results are consistent with a model wherein Ded1 stalls translation and specifically removes eIF4G1 from translation preinitiation complexes, thus removing eIF4G1 from the translating mRNA pool and leading to the codegradation of both proteins. Shared features among <i>DED1</i>
 orthologues suggest that this role is conserved and may be implicated in pathologies such as oncogenesis.</AbstractText>
</Abstract>
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The DEAD-box RNA helicase Ded1 has a role in the translational response to TORC1 inhibition.

The DEAD-box RNA helicase Ded1 has a role in the translational response to TORC1 inhibition.

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