TCTP protects from apoptotic cell death by antagonizing bax function

Susini, Laurent; Besse, Stéphanie; Duflaut, Dominique; Lespagnol, Alexandra; Beekman, Chantal; Fiucci, Giusy; Atkinson, R. Andrew; Busso, Didier; Poussin, P; Marine, Jean–Christophe; Martinou, Jean‐Claude; Cavarelli, Jean; Moras, Dino; Amson, Robert; Telerman, Adam

doi:10.1038/cdd.2008.18

Cited by 181 publications

(211 citation statements)

References 39 publications

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“…The three-dimensional structures of the following TCTP proteins were solved and are deposited in the databases: The solution structures of fission yeast (Thaw et al 2001) and human TCTP (Feng et al 2007a), as well as the crystal structures of Plasmodium knowlesi (Vedadi et al 2007) and human TCTP (Susini et al 2008) at 2 Å resolution. A mutant version of human TCTP showing a structure very similar to the normal protein (Dong et al 2009) can be found as well.…”

Section: Molecular Structure Conservation and Interactionsmentioning

confidence: 99%

“…Since then, the anti-apoptotic activity of TCTP has been reported on numerous occasions and in a range of different settings, which will be discussed below. Major support for the cytoprotective role of TCTP came from gene-knockout studies in mice, which demonstrated that TCTP-knockout was embryonic lethal, due to excessive apoptosis at an early embryonic state (Susini et al 2008;Chen et al 2007a;Koide et al 2009). The following mechanisms have been proposed to underlie the anti-apoptotic activity of TCTP/fortilin: …”

Section: Anti-apoptotic Activity: Discovery and Mechanismsmentioning

confidence: 99%

“…This study demonstrated that TCTP has a BH3-like domain. Binding to such BH3 domains (Bcl2 homology domain 3) typically inhibits anti-apoptotic proteins; however, TCTP's BH3-like domain actually activates the anti-apoptotic activity of Bcl-XL (Thebault et al 2016 (Susini et al 2008). They also showed that TCTP, with its α-helical domain, is able to insert itself into the mitochondrial membrane and to prevent the dimerisation and activation of Bax.…”

Section: Stress Responsementioning

confidence: 99%

“…The most impressive evidence for the importance of TCTP in early development was provided by TPT1-gene-knockouts in mice, which resulted in embryonic lethality (Susini et al 2008;Chen et al 2007a;Koide et al 2009). The explanation typically given for this effect was 'excessive apoptosis at an early embryonic state' (Susini et al 2008;Chen et al 2007a), whereas another report reasons that the lack of TCTP results in an overactivity of the BMP4 (bone morphogenetic protein 4) pathway, which is normally inhibited by TCTP (Koide et al 2009). The authors of this paper also show that in Xenopus embryos TCTP/fortilin is particularly important for the formation of neural tissue, even in the brain.…”

Section: Roles For Tctp In Early Developmentmentioning

confidence: 99%

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The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Bommer

2017

Results and Problems in Cell Differentiation

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The Translational Controlled Tumour Protein TCTP (gene symbol TPT1, also called P21, P23, Q23, fortilin or histamine-releasing factor, HRF) is a highly conserved protein present in essentially all eukaryotic organisms and involved in many fundamental cell biological and disease processes. It was first discovered about 35 years ago, and it took an extended period of time for its multiple functions to be revealed, and even today we do not yet fully understand all the details. Having witnessed most of this history, in this chapter, I give a brief overview and review the current knowledge on the structure, biological functions, disease involvements and cellular regulation of this protein. TCTP is able to interact with a large number of other proteins and is therefore involved in many core cell biological processes, predominantly in the response to cellular stresses, such as oxidative stress, heat shock, genotoxic stress, imbalance of ion metabolism as well as other conditions. Mechanistically, TCTP acts as an anti-apoptotic protein, and it is involved in DNA-damage repair and in cellular autophagy. Thus, broadly speaking, TCTP can be considered a cytoprotective protein. In addition, TCTP facilitates cell division through stabilising the mitotic spindle and cell growth through modulating growth signalling pathways and through its interaction with the proteosynthetic machinery of the cell. Due to its activities, both as an anti-apoptotic protein and in promoting cell growth and division, TCTP is also essential in the early development of both animals and plants. Apart from its involvement in various biological processes at the cellular level, TCTP can also act as an extracellular protein and as such has been involved in modulating whole-body defence processes, namely in the mammalian immune system. Extracellular TCTP, typically in its dimerised form, is able to induce the release of cytokines and other signalling molecules from various types of immune cells. There are also several examples, where TCTP was shown to be involved in antiviral/antibacterial defence in lower animals. In plants, the protein appears to have a protective effect against phytotoxic stresses, such as flooding, draught, too high or low temperature, salt stress or exposure to heavy metals. The finding for the latter stress condition is corroborated by earlier reports that TCTP levels are considerably up-regulated upon exposure of earthworms to high levels of heavy metals. Given the involvement of TCTP in many biological processes aimed at maintaining cellular or whole-body homeostasis, it is not surprising that dysregulation of TCTP levels may promote a range of disease processes, foremost cancer. Indeed a large body of evidence now supports a role of TCTP in at least the most predominant types of human cancers. Typically, this can be ascribed to both the anti-apoptotic activity of the protein and to its function in promoting cell growth and division. However, TCTP also appears to be involved in the later stages of cancer progression, such ...

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Section: Molecular Structure Conservation and Interactionsmentioning

confidence: 99%

Section: Anti-apoptotic Activity: Discovery and Mechanismsmentioning

confidence: 99%

Section: Stress Responsementioning

confidence: 99%

Section: Roles For Tctp In Early Developmentmentioning

confidence: 99%

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The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Bommer

2017

Results and Problems in Cell Differentiation

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“…TCTP is a growth-regulating protein implicated in the TSC1-TSC2-mTOR pathway 21 and protects cells from apoptotic cell death by antagonizing bax function. 22,23 In addition, TCTP has been suggested as a predictive marker for colon adenocarcinoma progression and tumor metastasis. 24 The increased expression of TCTP in FTC versus FA was confirmed by Western blot analysis (Figure 4).…”

Section: Differential Protein Expression In Fa and Ftcmentioning

confidence: 99%

Dissecting Molecular Events in Thyroid Neoplasia Provides Evidence for Distinct Evolution of Follicular Thyroid Adenoma and Carcinoma

Krause¹,

Prawitt²,

Eszlinger³

et al. 2011

The American Journal of Pathology

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Benign hypofunctional cold thyroid nodules (CTNs) are a frequent scintiscan finding and need to be distinguished from thyroid carcinomas. The origin of CTNs with follicular morphologic features is unresolved. The DNA damage response might act as a physiologic barrier, inhibiting the progression of preneoplastic lesions to neoplasia. We investigated the following in hypofunctional follicular adenoma (FA) and follicular thyroid cancer (FTC): i) the mutation rate of frequently activated oncogenes, ii) the activation of DNA damage response checkpoints, and iii) the differential proteomic pattern between FA and FTC. Both FTC and FA, which did not harbor RAS, phosphoinositide-3-kinase, or PAX/peroxisome proliferator activated receptor-␥ mutations, express various proteins in common and others that are more distinctly expressed in FTC rather than in FA or normal thyroid tissue. This finding is in line with the finding of constitutive DNA damage checkpoint activation (p-Chk2, ␥-H2AX) and evidence for replicative stress causing genomic instability (increased cyclin E, retinoblastoma, or E2F1 mRNA expression) in FTC but not FA. We discuss the findings of the increased expression of translationally controlled tumor protein, phosphatase 2A inhibitor, and DJ-1 in FTC compared with FA identified by proteomics and their potential implication in follicular thyroid carcinogenesis. Our present findings argue for the definition of FA as a truly benign entity and against progressive development of FA to FTC.

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Temporal proteome profiling of taxol‐induced mitotic arrest and apoptosis

et al. 2010

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Taxol (Paclitaxel) is a mitotic inhibitor widely used in cancer therapy. Temporal proteome profiling was performed to study changes of proteins during the different cellular states of HeLa cells caused by exposure to taxol. The changes of proteins over time could be associated with various cellular processes such as mitotic arrest, an intermediate between mitotic arrest and apoptosis, apoptosis, and late apoptosis. Calumenin, stress-induced phosphoprotein 1 (STIP1), and translationally controlled tumor protein (TCTP) were assigned to mitotic arrest and selected for further experiments using immunoblotting and subcellular fractionation. Calumenin translocated from membranes to the cytosol during mitotic arrest and late apoptosis, but was significantly reduced in the cytosol during apoptosis. Translocation of STIP1 to the nucleus was observed at apoptosis and to the cytoskeleton at late apoptosis. TCTP increased in the cytosol at mitotic arrest and in membranes at apoptosis. In addition, the quantitative time courses of Bim isoforms revealed differences between BimL and BimS in comparison with BimEL. In summary, temporal proteome profiling of HeLa cells incubated with taxol allowed the assignment of proteins to certain processes and additional experiments with complementary approaches enabled a more comprehensive understanding of spatial changes of selected proteins during mitotic arrest and apoptosis.

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TCTP protects from apoptotic cell death by antagonizing bax function

Cited by 181 publications

References 39 publications

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Dissecting Molecular Events in Thyroid Neoplasia Provides Evidence for Distinct Evolution of Follicular Thyroid Adenoma and Carcinoma

Temporal proteome profiling of taxol‐induced mitotic arrest and apoptosis

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