RapamycinFungusV1, Main, Exploration, bibRecord, 000277

Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).

Identifieur interne : 000277 ( Main/Exploration ); précédent : 000276; suivant : 000278

Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).

Auteurs : Rui Sun [États-Unis] ; Erdong Cheng [États-Unis] ; Celestino Velásquez [États-Unis] ; Yuan Chang [États-Unis] ; Patrick S. Moore [États-Unis]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2019.

RBID : pubmed:31201269

Descripteurs français

KwdFr :
- Cellules HeLa (MeSH), Cystéine (analogues et dérivés), Cystéine (pharmacologie), Facteur-4E d'initiation eucaryote (métabolisme), Facteur-4G d'initiation eucaryote (métabolisme), Humains (MeSH), Interphase (MeSH), Isoformes de protéines (génétique), Isoformes de protéines (métabolisme), Liaison aux protéines (MeSH), Mitose (effets des médicaments et des substances chimiques), Phosphorylation (MeSH), Protéines adaptatrices de la transduction du signal (déficit), Protéines adaptatrices de la transduction du signal (génétique), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines du cycle cellulaire (déficit), Protéines du cycle cellulaire (génétique), Protéines du cycle cellulaire (métabolisme), Édition de gène (MeSH).
MESH :
- analogues et dérivés : Cystéine.
- déficit : Protéines adaptatrices de la transduction du signal, Protéines du cycle cellulaire.
- effets des médicaments et des substances chimiques : Mitose.
- génétique : Isoformes de protéines, Protéines adaptatrices de la transduction du signal, Protéines du cycle cellulaire.
- métabolisme : Facteur-4E d'initiation eucaryote, Facteur-4G d'initiation eucaryote, Isoformes de protéines, Protéines adaptatrices de la transduction du signal, Protéines du cycle cellulaire.
- pharmacologie : Cystéine.
- Cellules HeLa, Humains, Interphase, Liaison aux protéines, Phosphorylation, Édition de gène.

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (deficiency), Adaptor Proteins, Signal Transducing (genetics), Adaptor Proteins, Signal Transducing (metabolism), Cell Cycle Proteins (deficiency), Cell Cycle Proteins (genetics), Cell Cycle Proteins (metabolism), Cysteine (analogs & derivatives), Cysteine (pharmacology), Eukaryotic Initiation Factor-4E (metabolism), Eukaryotic Initiation Factor-4G (metabolism), Gene Editing (MeSH), HeLa Cells (MeSH), Humans (MeSH), Interphase (MeSH), Mitosis (drug effects), Phosphorylation (MeSH), Protein Binding (MeSH), Protein Isoforms (genetics), Protein Isoforms (metabolism).
MESH :
- chemical , analogs & derivatives : Cysteine.
- chemical , deficiency : Adaptor Proteins, Signal Transducing, Cell Cycle Proteins.
- chemical , genetics : Adaptor Proteins, Signal Transducing, Cell Cycle Proteins, Protein Isoforms.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Cell Cycle Proteins, Eukaryotic Initiation Factor-4E, Eukaryotic Initiation Factor-4G, Protein Isoforms.
- chemical , pharmacology : Cysteine.
- drug effects : Mitosis.
- Gene Editing, HeLa Cells, Humans, Interphase, Phosphorylation, Protein Binding.

Abstract

Eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) inhibits cap-dependent translation in eukaryotes by competing with eIF4G for an interaction with eIF4E. Phosphorylation at Ser-83 of 4E-BP1 occurs during mitosis through the activity of cyclin-dependent kinase 1 (CDK1)/cyclin B rather than through canonical mTOR kinase activity. Here, we investigated the interaction of eIF4E with 4E-BP1 or eIF4G during interphase and mitosis. We observed that 4E-BP1 and eIF4G bind eIF4E at similar levels during interphase and mitosis. The most highly phosphorylated mitotic 4E-BP1 isoform (δ) did not interact with eIF4E, whereas a distinct 4E-BP1 phospho-isoform, EB-γ, phosphorylated at Thr-70, Ser-83, and Ser-101, bound to eIF4E during mitosis. Two-dimensional gel electrophoretic analysis corroborated the identity of the phosphorylation marks on the eIF4E-bound 4E-BP1 isoforms and uncovered a population of phosphorylated 4E-BP1 molecules lacking Thr-37/Thr-46-priming phosphorylation. Moreover, proximity ligation assays for phospho-4E-BP1 and eIF4E revealed different in situ interactions during interphase and mitosis. The eIF4E:eIF4G interaction was not inhibited but rather increased in mitotic cells, consistent with active translation initiation during mitosis. Phosphodefective substitution of 4E-BP1 at Ser-83 did not change global translation or individual mRNA translation profiles as measured by single-cell nascent protein synthesis and eIF4G RNA immunoprecipitation sequencing. Mitotic 5'-terminal oligopyrimidine RNA translation was active and, unlike interphase translation, resistant to mTOR inhibition. Our findings reveal the phosphorylation profiles of 4E-BP1 isoforms and their interactions with eIF4E throughout the cell cycle and indicate that 4E-BP1 does not specifically inhibit translation initiation during mitosis.

DOI: 10.1074/jbc.RA119.008512
PubMed: 31201269
PubMed Central: PMC6682726

Affiliations:

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Le document en format XML

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<term>Adaptor Proteins, Signal Transducing (genetics)</term>
<term>Adaptor Proteins, Signal Transducing (metabolism)</term>
<term>Cell Cycle Proteins (deficiency)</term>
<term>Cell Cycle Proteins (genetics)</term>
<term>Cell Cycle Proteins (metabolism)</term>
<term>Cysteine (analogs & derivatives)</term>
<term>Cysteine (pharmacology)</term>
<term>Eukaryotic Initiation Factor-4E (metabolism)</term>
<term>Eukaryotic Initiation Factor-4G (metabolism)</term>
<term>Gene Editing (MeSH)</term>
<term>HeLa Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Interphase (MeSH)</term>
<term>Mitosis (drug effects)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Isoforms (genetics)</term>
<term>Protein Isoforms (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa (MeSH)</term>
<term>Cystéine (analogues et dérivés)</term>
<term>Cystéine (pharmacologie)</term>
<term>Facteur-4E d'initiation eucaryote (métabolisme)</term>
<term>Facteur-4G d'initiation eucaryote (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Interphase (MeSH)</term>
<term>Isoformes de protéines (génétique)</term>
<term>Isoformes de protéines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Mitose (effets des médicaments et des substances chimiques)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protéines adaptatrices de la transduction du signal (déficit)</term>
<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines du cycle cellulaire (déficit)</term>
<term>Protéines du cycle cellulaire (génétique)</term>
<term>Protéines du cycle cellulaire (métabolisme)</term>
<term>Édition de gène (MeSH)</term>
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</keywords>
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<term>Cell Cycle Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term>
<term>Cell Cycle Proteins</term>
<term>Protein Isoforms</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term>
<term>Cell Cycle Proteins</term>
<term>Eukaryotic Initiation Factor-4E</term>
<term>Eukaryotic Initiation Factor-4G</term>
<term>Protein Isoforms</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cysteine</term>
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<keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Cystéine</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Mitosis</term>
</keywords>
<keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines du cycle cellulaire</term>
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</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Isoformes de protéines</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines du cycle cellulaire</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur-4E d'initiation eucaryote</term>
<term>Facteur-4G d'initiation eucaryote</term>
<term>Isoformes de protéines</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines du cycle cellulaire</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Cystéine</term>
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<keywords scheme="MESH" xml:lang="en"><term>Gene Editing</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Interphase</term>
<term>Phosphorylation</term>
<term>Protein Binding</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term>
<term>Humains</term>
<term>Interphase</term>
<term>Liaison aux protéines</term>
<term>Phosphorylation</term>
<term>Édition de gène</term>
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<front><div type="abstract" xml:lang="en">Eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) inhibits cap-dependent translation in eukaryotes by competing with eIF4G for an interaction with eIF4E. Phosphorylation at Ser-83 of 4E-BP1 occurs during mitosis through the activity of cyclin-dependent kinase 1 (CDK1)/cyclin B rather than through canonical mTOR kinase activity. Here, we investigated the interaction of eIF4E with 4E-BP1 or eIF4G during interphase and mitosis. We observed that 4E-BP1 and eIF4G bind eIF4E at similar levels during interphase and mitosis. The most highly phosphorylated mitotic 4E-BP1 isoform (δ) did not interact with eIF4E, whereas a distinct 4E-BP1 phospho-isoform, EB-γ, phosphorylated at Thr-70, Ser-83, and Ser-101, bound to eIF4E during mitosis. Two-dimensional gel electrophoretic analysis corroborated the identity of the phosphorylation marks on the eIF4E-bound 4E-BP1 isoforms and uncovered a population of phosphorylated 4E-BP1 molecules lacking Thr-37/Thr-46-priming phosphorylation. Moreover, proximity ligation assays for phospho-4E-BP1 and eIF4E revealed different <i>in situ</i>
 interactions during interphase and mitosis. The eIF4E:eIF4G interaction was not inhibited but rather increased in mitotic cells, consistent with active translation initiation during mitosis. Phosphodefective substitution of 4E-BP1 at Ser-83 did not change global translation or individual mRNA translation profiles as measured by single-cell nascent protein synthesis and eIF4G RNA immunoprecipitation sequencing. Mitotic 5'-terminal oligopyrimidine RNA translation was active and, unlike interphase translation, resistant to mTOR inhibition. Our findings reveal the phosphorylation profiles of 4E-BP1 isoforms and their interactions with eIF4E throughout the cell cycle and indicate that 4E-BP1 does not specifically inhibit translation initiation during mitosis.</div>
</front>
</TEI>
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<DateCompleted><Year>2020</Year>
<Month>03</Month>
<Day>16</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>16</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>294</Volume>
<Issue>31</Issue>
<PubDate><Year>2019</Year>
<Month>08</Month>
<Day>02</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).</ArticleTitle>
<Pagination><MedlinePgn>11840-11852</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA119.008512</ELocationID>
<Abstract><AbstractText>Eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) inhibits cap-dependent translation in eukaryotes by competing with eIF4G for an interaction with eIF4E. Phosphorylation at Ser-83 of 4E-BP1 occurs during mitosis through the activity of cyclin-dependent kinase 1 (CDK1)/cyclin B rather than through canonical mTOR kinase activity. Here, we investigated the interaction of eIF4E with 4E-BP1 or eIF4G during interphase and mitosis. We observed that 4E-BP1 and eIF4G bind eIF4E at similar levels during interphase and mitosis. The most highly phosphorylated mitotic 4E-BP1 isoform (δ) did not interact with eIF4E, whereas a distinct 4E-BP1 phospho-isoform, EB-γ, phosphorylated at Thr-70, Ser-83, and Ser-101, bound to eIF4E during mitosis. Two-dimensional gel electrophoretic analysis corroborated the identity of the phosphorylation marks on the eIF4E-bound 4E-BP1 isoforms and uncovered a population of phosphorylated 4E-BP1 molecules lacking Thr-37/Thr-46-priming phosphorylation. Moreover, proximity ligation assays for phospho-4E-BP1 and eIF4E revealed different <i>in situ</i>
 interactions during interphase and mitosis. The eIF4E:eIF4G interaction was not inhibited but rather increased in mitotic cells, consistent with active translation initiation during mitosis. Phosphodefective substitution of 4E-BP1 at Ser-83 did not change global translation or individual mRNA translation profiles as measured by single-cell nascent protein synthesis and eIF4G RNA immunoprecipitation sequencing. Mitotic 5'-terminal oligopyrimidine RNA translation was active and, unlike interphase translation, resistant to mTOR inhibition. Our findings reveal the phosphorylation profiles of 4E-BP1 isoforms and their interactions with eIF4E throughout the cell cycle and indicate that 4E-BP1 does not specifically inhibit translation initiation during mitosis.</AbstractText>
<CopyrightInformation>© 2019 Sun et al.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sun</LastName>
<ForeName>Rui</ForeName>
<Initials>R</Initials>
<Identifier Source="ORCID">0000-0003-2571-1012</Identifier>
<AffiliationInfo><Affiliation>Department of Microbiology and Molecular Genetics, University of Pittsburgh, Pittsburgh, Pennsylvania 15213.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Cancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, Pennsylvania 15213.</Affiliation>
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).

Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).

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