Non-translational Connections of eEF1B in the Cytoplasm and Nucleus of Cancer Cells

Negrutskii, B. S.

doi:10.3389/fmolb.2020.00056

Cited by 10 publications

(8 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…WT*, 36*, 55*,79*, FM*same as before but the samples were taken after pull down procedure. eEF1A binding to other subunits of the eEF1B complex [34]. Thus, in the case of eEF1Bγ, we actually observed the interaction of eEF1A2 with the eEF1B complex.…”

Section: Resultssupporting

confidence: 53%

Methylation of human elongation factor eEF1A2 is not essential for eEF1A2-eEF1B interaction

et al. 2020

View full text Add to dashboard Cite

Aim. Study on a possible role of methylation of lysine residues of еЕF1А2 in its interactions with the elongation translation complex eEF1B. Methods. Mutagenesis, cloning, 293 human cell culture, BRET (bioluminescence resonance energy transfer), cell transfection, HaloTag pull down of protein complexes, Western blot, densitometry. Results. Five mutants of eEF1A2 with a single substitution of methylable lysine residue for arginine and the mutant with all five lysine residues mutated were generated. BRET analysis and HaloTag pull down experiments of isolated protein complexes have shown no differences in interactions of eEF1B subunits with eEF1A2 and its unmethylable mutants. Conclusion. Methylation of eEF1A2 apparently does not influence the interactions of eEF1A2 with eEF1B subunits.

show abstract

Section: Resultssupporting

confidence: 53%

Methylation of human elongation factor eEF1A2 is not essential for eEF1A2-eEF1B interaction

et al. 2020

View full text Add to dashboard Cite

show abstract

“…eEF1B has also been found in the nuclei of human cells. The interactome of nuclear eEF1Bβ indicates a putative role in transcription, splicing, and DNA damage response, whereas the interactome of nuclear eEF1Bγ suggests a role in the splicing and control of mRNA stability [236]. Moreover, eEF1Bγ binds the Rpb3 subunit of RNAP II and is recruited to the promoters of genes encoding vimentin, Che1 (AATF), and p53 in human cells [237,238].…”

Section: Roles Of Ctas In Transcriptional Regulationmentioning

confidence: 99%

Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus

Kachaev

Ivashchenko

Kozlov

et al. 2021

Cells

View full text Add to dashboard Cite

Components of the translation apparatus, including ribosomal proteins, have been found in cell nuclei in various organisms. Components of the translation apparatus are involved in various nuclear processes, particularly those associated with genome integrity control and the nuclear stages of gene expression, such as transcription, mRNA processing, and mRNA export. Components of the translation apparatus control intranuclear trafficking; the nuclear import and export of RNA and proteins; and regulate the activity, stability, and functional recruitment of nuclear proteins. The nuclear translocation of these components is often involved in the cell response to stimulation and stress, in addition to playing critical roles in oncogenesis and viral infection. Many components of the translation apparatus are moonlighting proteins, involved in integral cell stress response and coupling of gene expression subprocesses. Thus, this phenomenon represents a significant interest for both basic and applied molecular biology. Here, we provide an overview of the current data regarding the molecular functions of translation factors and ribosomal proteins in the cell nucleus.

show abstract

“…It has been reported that the subunits involved into eEF1B can interact with several protein partners in human cancer cells (56). However, only translationally controlled tumor protein (TCTP) was shown to bind the CAR domain of eEF1B␤ (57) that resulted in inhibition of its guaninenucleotide exchange activity (58).…”

Section: Discussionmentioning

confidence: 99%

Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly

Bondarchuk

Shalak

Lozhko

et al. 2022

Nucleic Acids Research

View full text Add to dashboard Cite

Protein synthesis in eukaryotic cell is spatially and structurally compartmentalized that ensures high efficiency of this process. One of the distinctive features of higher eukaryotes is the existence of stable multi-protein complexes of aminoacyl-tRNA synthetases and translation elongation factors. Here, we report a quaternary organization of the human guanine-nucleotide exchange factor (GEF) complex, eEF1B, comprising α, β and γ subunits that specifically associate into a heterotrimeric form eEF1B(αβγ)3. As both the eEF1Bα and eEF1Bβ proteins have structurally conserved GEF domains, their total number within the complex is equal to six. Such, so far, unique structural assembly of the guanine-nucleotide exchange factors within a stable complex may be considered as a ‘GEF hub’ that ensures efficient maintenance of the translationally active GTP-bound conformation of eEF1A in higher eukaryotes.

show abstract

Non-translational Connections of eEF1B in the Cytoplasm and Nucleus of Cancer Cells

Cited by 10 publications

References 76 publications

Methylation of human elongation factor eEF1A2 is not essential for eEF1A2-eEF1B interaction

Methylation of human elongation factor eEF1A2 is not essential for eEF1A2-eEF1B interaction

Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus

Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly

Contact Info

Product

Resources

About