Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).
Identifieur interne : 000255 ( Main/Corpus ); précédent : 000254; suivant : 000256Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).
Auteurs : Rui Sun ; Erdong Cheng ; Celestino Velásquez ; Yuan Chang ; Patrick S. MooreSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2019.
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
Links to Exploration step
pubmed:31201269Le document en format XML
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<series><title level="j">The Journal of biological chemistry</title>
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<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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<term>Protein Isoforms</term>
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<term>Eukaryotic Initiation Factor-4E</term>
<term>Eukaryotic Initiation Factor-4G</term>
<term>Protein Isoforms</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cysteine</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Mitosis</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>
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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>
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<ArticleTitle>Mitosis-related phosphorylation of the eukaryotic translation suppressor 4E-BP1 and its interaction with eukaryotic translation initiation factor 4E (eIF4E).</ArticleTitle>
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<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>
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<ForeName>Rui</ForeName>
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<AffiliationInfo><Affiliation>Department of Pathology, University of Pittsburgh, Pittsburgh, Pennsylvania 15213.</Affiliation>
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<AffiliationInfo><Affiliation>Cancer Virology Program, UPMC Hillman Cancer Center, Pittsburgh, Pennsylvania 15213.</Affiliation>
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