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Article

Characterization of the Raptor/4E-BP1 interaction by chemical cross-linking coupled with mass spectrometry analysis.

The Journal of biological chemistry - 21 Feb 2014

Coffman Kimberly, Yang Bing, Lu Jie, Tetlow Ashley L, Pelliccio Emelia, Lu Shan, Guo Da-Chuan, Tang Chun, Dong Meng-Qiu, Tamanoi Fuyuhiko

Abstract excerpt

mTORC1 plays critical roles in the regulation of protein synthesis, growth, and proliferation in response to nutrients, growth factors, and energy conditions. One of the substrates of mTORC1 is 4E-BP1, whose phosphorylation by mTORC1 reverses its inhibitory action on eIF4E, resulting in the promotion of protein synthesis. Raptor in mTOR complex 1 is believed to recruit 4E-BP1, facilitating phosphorylation of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 24403073
DOI: 10.1074/jbc.M113.482067
PMCID: PMC3931034

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Characterization of the Raptor/4E-BP1 interaction by chemical cross-linking coupled with mass spectrometry analysis.PMID 24403073Read ↗

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Hierarchical phosphorylation of the translation inhibitor 4E-BP1.Semantic proximity Read ↗

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Target of rapamycin (TOR)-signaling and RAIP motifs play distinct roles in the mammalian TOR-dependent phosphorylation of initiation factor 4E-binding protein 1.Semantic proximity Read ↗

The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity.Semantic proximity Read ↗

Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action.Semantic proximity Read ↗

Mechanistic target of rapamycin complex 1 (mTORC1)-mediated phosphorylation is governed by competition between substrates for interaction with raptor.Semantic proximity Read ↗

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