Identification of a Specific Translational Machinery via TCTP–EF1A2 Interaction Regulating NF1-associated Tumor Growth by Affinity Purification and Data-independent Mass Spectrometry Acquisition (AP-DIA)*

Kobayashi, Daiki; Tokuda, Takaho; Sato, Kyosuke; Okanishi, Hiroki; Nagayama, Megumi; Hirayama-Kurogi, Mio; Ohtsuki, Sumio; Araki, Nobuhito

doi:10.1074/mcp.ra118.001014

Cited by 15 publications

(12 citation statements)

References 45 publications

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“…A variation of this mechanism was proposed very recently by a Japanese group interested in mechanisms involved in formation of neurofibromatosis type 1 (NF1)-associated tumors. Their work confirmed the interaction of TCTP with EF1A, as well as with its GEF complex consisting of EF1B, EF1G, and EF1D [7]. In addition, this paper showed that the interaction of TCTP with EF1A2, an isoform of EF1A preferentially expressed in neuronal tissue and skeletal muscle, is much stronger compared to that with the normal isoform, EF1A1.…”

Section: Regulation Of Protein Synthesis and Degradationsupporting

confidence: 52%

“…A more specific study demonstrated the interaction of TCTP with translation elongation factor eEF1A and its guanine nucleotide exchange factor (GEF), eEF1B [24]. Subsequently, the interaction of TCTP with elongation factors of the EF1 family and with other components of the translational apparatus was confirmed both in human cells [7,25] and in Drosophila [15]. Consistent with this is the observation that the genes of ribosomal proteins, elongation factors, and of TCTP all belong to the class of 'TOP genes', whose mRNAs have a common signature, the 5 -terminal oligo-pyrimidine tract (5 -TOP) [26], and are therefore translationally regulated [27].…”

Section: Regulation Of Protein Synthesis and Degradationmentioning

confidence: 94%

“…Compilations of the many interaction partners of TCTP have been published in the above-mentioned book [4][5][6]. A more recent study, using current proteomics approaches combined with in silico network and gene ontology enrichment analysis, identified 113 interacting proteins [7], which were allocated to the following gene network clusters: translation, stress response, cytoskeleton, signal transduction, proteasomes, nucleosomes and transcription, RNA binding and metabolic enzymes. These clusters can be roughly associated with the following three core biological processes.…”

Section: Importance Of Tctp In Core Cell Biological and Stress Reactionsmentioning

confidence: 99%

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Dysregulation of TCTP in Biological Processes and Diseases

Bommer

Telerman

2020

Cells

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Translationally controlled tumor protein (TCTP), also called histamine releasing factor (HRF) or fortilin, is a multifunctional protein present in almost all eukaryotic organisms. TCTP is involved in a range of basic cell biological processes, such as promotion of growth and development, or cellular defense in response to biological stresses. Cellular TCTP levels are highly regulated in response to a variety of physiological signals, and regulatory mechanism at various levels have been elucidated. Given the importance of TCTP in maintaining cellular homeostasis, it is not surprising that dysregulation of this protein is associated with a range of disease processes. Here, we review recent progress that has been made in the characterisation of the basic biological functions of TCTP, in the description of mechanisms involved in regulating its cellular levels and in the understanding of dysregulation of TCTP, as it occurs in disease processes such as cancer.

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Section: Regulation Of Protein Synthesis and Degradationsupporting

confidence: 52%

Section: Regulation Of Protein Synthesis and Degradationmentioning

confidence: 94%

Section: Importance Of Tctp In Core Cell Biological and Stress Reactionsmentioning

confidence: 99%

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Dysregulation of TCTP in Biological Processes and Diseases

Bommer

Telerman

2020

Cells

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“…eEF1A2 revealed oncogenic properties [13,14]. An increased expression of eEF1B subunits was also found in different cancers [15,16].…”

Section: Structure and Function Of Biopolymersmentioning

confidence: 93%

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

et al. 2020

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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.

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“…The remaining AK fingerprint protein (G3NUU3) encodes translationally controlled tumor protein 1 (TCTP1). TCTP1 is involved in calcium signaling and the regulation of growth and energy metabolism during stress 9 . Its higher abundance in the AK population likely reflects the osmotic stress encountered by this population when entering low salinity brackish water from a marine environment or being exposed to tidal salinity fluctuations.…”

Section: /20mentioning

confidence: 99%

Identification of key proteins involved in stickleback environmental adaption with system-level analysis

Hall

Kueltz

Almaas

2020

Preprint

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Using abundance measurements of 1,490 proteins from four separate populations of three-spined sticklebacks, we implemented a system-level approach to correlate proteome dynamics with environmental salinity and temperature and the fish's population and morphotype. We identified sets of robust and accurate fingerprints that predict environmental salinity, temperature, morphotype and the population sample origin, observing that proteins with specific functions are enriched in these fingerprints. Highly apparent functions represented in all fingerprints include ion transport, proteostasis, growth, and immunity, suggesting that these functions are most diversified in populations inhabiting different environments. Applying a differential network approach, we analyzed the network of protein interactions that differs between populations. Looking at specific population combinations of differential interaction, we identify sets of connected proteins. We find that these sets and their corresponding enriched functions reflect key processes that have diverged between the four populations. Moreover, the extent of divergence, i.e. the number of enriched functions that differ between populations, is highest when all three environmental parameters are different between two populations. Key nodes in the differential interaction network signify functions that are also inherent in the fingerprints, most prominently proteostasis-related functions. However, the differential interaction network also reveals additional functions that have diverged between populations, notably cytoskeletal organization and morphogenesis. Having such a large proteomic dataset, the strength of these analyses is that the results are purely data-driven, not based on previous findings and hypotheses about adaptation. With such an unbiased approach applied on a large proteomic dataset, we find the strongest signals given by the data, making it possible to develop more discriminatory and complex biomarkers for specific contexts of interest.

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Identification of a Specific Translational Machinery via TCTP–EF1A2 Interaction Regulating NF1-associated Tumor Growth by Affinity Purification and Data-independent Mass Spectrometry Acquisition (AP-DIA)*

Cited by 15 publications

References 45 publications

Dysregulation of TCTP in Biological Processes and Diseases

Dysregulation of TCTP in Biological Processes and Diseases

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

Identification of key proteins involved in stickleback environmental adaption with system-level analysis

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