Translationally controlled tumor protein

Translationally controlled tumor protein was first discovered in 1989 as a cDNA sequence obtained from a human mammary carcinoma cDNA library with proves derived from the translationally controlled, growth-related mouse tumor protein TCTP.{{cite journal | vauthors = Gross B, Gaestel M, Böhm H, Bielka H | title = cDNA sequence coding for a translationally controlled human tumor protein | journal = Nucleic Acids Research | volume = 17 | issue = 20 | pages = 8367 | date = October 1989 | pmid = 2813067 | doi=10.1093/nar/17.20.8367 | pmc=334973}} TCTP was originally described as a growth related protein of tumor cells. Its mRNA accumulates in translationally repressed postpolysomal mRNP-complexes.{{cite journal | vauthors = Chitpatima ST, Makrides S, Bandyopadhyay R, Brawerman G | title = Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells | journal = Nucleic Acids Research | volume = 16 | issue = 5 | pages = 2350 | date = March 1988 | pmid = 3357792 | doi=10.1093/nar/16.5.2350 | pmc=338237}}

Research in 1997 shown that TCTP is not a tumor- or tissue-specific protein, but is expressed ubiquitously from plants to mammals.{{cite journal | vauthors = Sanchez JC, Schaller D, Ravier F, Golaz O, Jaccoud S, Belet M, Wilkins MR, James R, Deshusses J, Hochstrasser D | title = Translationally controlled tumor protein: a protein identified in several nontumoral cells including erythrocytes | journal = Electrophoresis | volume = 18 | issue = 1 | pages = 150–5 | date = January 1997 | pmid = 9059837 | doi = 10.1002/elps.1150180127 | s2cid = 25500696 }}{{cite journal | vauthors = Bhisutthibhan J, Pan XQ, Hossler PA, Walker DJ, Yowell CA, Carlton J, Dame JB, Meshnick SR | title = The Plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin | journal = The Journal of Biological Chemistry | volume = 273 | issue = 26 | pages = 16192–8 | date = June 1998 | pmid = 9632675 | doi=10.1074/jbc.273.26.16192| doi-access = free }}{{cite journal | vauthors = Yan L, Fei K, Bridge D, Sarras MP | title = A cnidarian homologue of translationally controlled tumor protein (P23/TCTP) | journal = Development Genes and Evolution | volume = 210 | issue = 10 | pages = 507–11 | date = October 2000 | pmid = 11180799 | doi = 10.1007/s004270000088| s2cid = 10631675 }}{{cite journal | vauthors = Sage-Ono K, Ono M, Harada H, Kamada H | title = Dark-induced accumulation of mRNA for a homolog of translationally controlled tumor protein (TCTP) in Pharbitis | journal = Plant & Cell Physiology | volume = 39 | issue = 3 | pages = 357–60 | date = March 1998 | pmid = 9588028 | doi=10.1093/oxfordjournals.pcp.a029377| doi-access = free }} Later studies show TCTP involvement in a protozoan Trypanosoma brucei.{{cite journal | vauthors = Jojic B, Amodeo S, Bregy I, Ochsenreiter T | title = Distinct 3' UTRs regulate the life-cycle-specific expression of two TCTP paralogs in Trypanosoma brucei | journal = Journal of Cell Science | volume = 131 | issue = 9 | date = May 2018 | pmid = 29661850 | pmc = 5992589 | doi = 10.1242/jcs.206417 }}{{cite journal | vauthors = Jojic B, Amodeo S, Ochsenreiter T | title = The translationally controlled tumor protein TCTP is involved in cell cycle progression and heat stress response in the bloodstream form of Trypanosoma brucei | journal = Microbial Cell | volume = 5 | issue = 10 | pages = 460–468 | date = August 2018 | pmid = 30386790 | pmc = 6206406 | doi = 10.15698/mic2018.10.652 }}

TCTP is a 20–25 kDa protein abundantly and ubiquitously expressed in the cell. The protein is transcribed in more than 500 different tissues and cell types; hTCTP gene is one of the top 10 most ubiquitously expressed genes in humans by examining 1753 libraries from kinds of tissues,{{cite journal | vauthors = Thompson HG, Harris JW, Wold BJ, Quake SR, Brody JP | title = Identification and confirmation of a module of coexpressed genes | journal = Genome Research | volume = 12 | issue = 10 | pages = 1517–22 | date = October 2002 | pmid = 12368243 | doi = 10.1101/gr.418402 | pmc = 187523 }} but differed considerably in their quantity and ratio of expression. The expression is lower in kidney and renal cells. This indicates an extensive transcriptional control and involvement of tissue-specific factors.{{cite journal | vauthors = Bommer UA, Thiele BJ | title = The translationally controlled tumour protein (TCTP) | journal = The International Journal of Biochemistry & Cell Biology | volume = 36 | issue = 3 | pages = 379–85 | date = March 2004 | pmid = 14687915 | doi = 10.1016/S1357-2725(03)00213-9 }}

The majority of publications established TCTP to be a cytoplasmic protein but nuclear localisation has also been reported, as well as extracellular activity; however, the process of secretion has not been found.

The abundance and ubiquity indicate that TCTP may have important primary functions. However, a large number of cellular and biochemical functions have been found since 1980s. Most of these functions can be classified into three groups.

TCTP has properties of a tubulin binding protein that associates with microtubules in a cell cycle-dependent manner.{{cite journal | vauthors = Gachet Y, Tournier S, Lee M, Lazaris-Karatzas A, Poulton T, Bommer UA | title = The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle | journal = Journal of Cell Science | volume = 112 | pages = 1257–71 | date = April 1999 | pmid = 10085260 | issue=8| doi = 10.1242/jcs.112.8.1257 | url = https://hal.archives-ouvertes.fr/hal-02381728/file/JCS%20P23.pdf }}{{cite journal | vauthors = Yarm FR | title = Plk phosphorylation regulates the microtubule-stabilizing protein TCTP | journal = Molecular and Cellular Biology | volume = 22 | issue = 17 | pages = 6209–21 | date = September 2002 | pmid = 12167714 | pmc = 134017 | doi = 10.1128/MCB.22.17.6209-6221.2002 }}

The transient overexpression of TCTP in HeLa cells prevented them from undergoing etoposide-induced apoptosis. Expressing TCTP in U2OS (human bone osteosarcoma epithelial cells) protected them from cell death induced by etoposide over various concentrations and durations of exposure. TCTP overexpression inhibited caspase-3-like activity as assessed by the cleavage of fluorogenic substrate.

Expression levels of TCTP were down-regulated at the mRNA and protein levels during tumor suppression and by the activation of p53 and Siah-1 very well known anti-tumor genes.{{cite journal | vauthors = Cans C, Passer BJ, Shalak V, Nancy-Portebois V, Crible V, Amzallag N, Allanic D, Tufino R, Argentini M, Moras D, Fiucci G, Goud B, Mirande M, Amson R, Telerman A | title = Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 24 | pages = 13892–7 | date = November 2003 | pmid = 14623968 | doi = 10.1073/pnas.2335950100 | pmc=283517| bibcode = 2003PNAS..10013892C | doi-access = free }}{{cite journal | vauthors = Rinnerthaler M, Jarolim S, Heeren G, Palle E, Perju S, Klinger H, Bogengruber E, Madeo F, Braun RJ, Breitenbach-Koller L, Breitenbach M, Laun P | title = MMI1 (YKL056c, TMA19), the yeast orthologue of the translationally controlled tumor protein (TCTP) has apoptotic functions and interacts with both microtubules and mitochondria | journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics | volume = 1757 | issue = 5–6 | pages = 631–8 | date = 2016-06-01 | pmid = 16806052 | doi = 10.1016/j.bbabio.2006.05.022 | doi-access = free }} Down-regulation of TCTP can induce tumor reversion, and in combination with some drugs that decrease the level of TCTP and will lead to kill tumor cells.{{cite journal | vauthors = Tuynder M, Fiucci G, Prieur S, Lespagnol A, Géant A, Beaucourt S, Duflaut D, Besse S, Susini L, Cavarelli J, Moras D, Amson R, Telerman A | title = Translationally controlled tumor protein is a target of tumor reversion | language = en | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 43 | pages = 15364–9 | date = October 2004 | pmid = 15489264 | doi = 10.1073/pnas.0406776101 | pmc=523462| bibcode = 2004PNAS..10115364T | doi-access = free }} TCTP knockdown in primary mammary tumor cells, results in increased p53 expression and a decreased number of stem-like cancer cells.{{cite journal | vauthors = Amson R, Pece S, Lespagnol A, Vyas R, Mazzarol G, Tosoni D, Colaluca I, Viale G, Rodrigues-Ferreira S, Wynendaele J, Chaloin O, Hoebeke J, Marine JC, Di Fiore PP, Telerman A | title = Reciprocal repression between P53 and TCTP | language = en | journal = Nature Medicine | volume = 18 | issue = 1 | pages = 91–9 | date = January 2012 | pmid = 22157679 | doi = 10.1038/nm.2546 | s2cid = 22984419 }}

Reducing TCTP (dTCTP) levels in Drosophila reduces cell size, cell number and organ size, which mimics Drosophila Rheb (dRheb) mutant phenotypes; human TCTP (hTCTP) shows similar biochemical properties compared to dTCTP.

TCTP caused histamine release from the human basophils of a subpopulation of donors, and this release was dependent on IgE.{{cite journal | vauthors = Bheekha-Escura R, MacGlashan DW, Langdon JM, MacDonald SM | title = Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line, AML14-3D10 | journal = Blood | volume = 96 | issue = 6 | pages = 2191–8 | date = September 2000 | doi = 10.1182/blood.V96.6.2191 | pmid = 10979965 }}

The expression of TCTP is regulated at two distinct levels, depletion of the ER calcium causes an increase in TCTP mRNA abundance, increased cytosolic calcium concentrations regulate gene expression at the post-transcriptional level.{{cite journal | vauthors = Xu A, Bellamy AR, Taylor JA | title = Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level | journal = The Biochemical Journal | volume = 342 | issue = 3 | pages = 683–9 | date = September 1999 | pmid = 10477280 | pmc = 1220510 | doi=10.1042/0264-6021:3420683}}{{cite journal | vauthors = Haghighat NG, Ruben L | title = Purification of novel calcium binding proteins from Trypanosoma brucei: properties of 22-, 24- and 38-kilodalton proteins | journal = Molecular and Biochemical Parasitology | volume = 51 | issue = 1 | pages = 99–110 | date = March 1992 | pmid = 1565142 | doi=10.1016/0166-6851(92)90205-x}}

Downregulation of the protein levels by siRNA in HTR-8/SVneo (Homo sapiens placenta cells) was associated with a reduced cellular calcium-uptake activity and buffering capacity.

Translationally controlled tumor protein has a role in tumor reversion and development.{{cite journal | vauthors = Hsu YC, Chern JJ, Cai Y, Liu M, Choi KW | title = Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase | journal = Nature | volume = 445 | issue = 7129 | pages = 785–8 | year = 2007 | pmid = 17301792 | doi = 10.1038/nature05528 | bibcode = 2007Natur.445..785H | s2cid = 4302643 }}{{cite journal | vauthors = Tuynder M, Susini L, Prieur S, Besse S, Fiucci G, Amson R, Telerman A | title = Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 23 | pages = 14976–81 | year = 2002 | pmid = 12399545 | pmc = 137530 | doi = 10.1073/pnas.222470799 | bibcode = 2002PNAS...9914976T | doi-access = free }}

TCTP is a regulator of the cancer stem cell compartment,{{cite journal | vauthors = Amson R, Pece S, Lespagnol A, Vyas R, Mazzarol G, Tosoni D, Colaluca I, Viale G, Rodrigues-Ferreira S, Wynendaele J, Chaloin O, Hoebeke J, Marine JC, Di Fiore PP, Telerman A | title = Reciprocal repression between P53 and TCTP | journal = Nature Medicine | volume = 18 | issue = 1 | pages = 91–9 | date = December 2011 | pmid = 22157679 | doi = 10.1038/nm.2546 | s2cid = 22984419 }} the tumor reversion,{{cite journal | vauthors = Tuynder M, Susini L, Prieur S, Besse S, Fiucci G, Amson R, Telerman A | title = Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 23 | pages = 14976–81 | date = November 2002 | pmid = 12399545 | doi = 10.1073/pnas.222470799 | pmc=137530| bibcode = 2002PNAS...9914976T | doi-access = free }}{{cite journal | vauthors = Tuynder M, Fiucci G, Prieur S, Lespagnol A, Géant A, Beaucourt S, Duflaut D, Besse S, Susini L, Cavarelli J, Moras D, Amson R, Telerman A | title = Translationally controlled tumor protein is a target of tumor reversion | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 43 | pages = 15364–9 | date = October 2004 | pmid = 15489264 | doi = 10.1073/pnas.0406776101 | pmc=523462| bibcode = 2004PNAS..10115364T | doi-access = free }} tumor progression and certain forms of inflammatory diseases. Moreover, TCTP was described as a pro-survival protein antagonizing BAX function.{{cite journal | vauthors = Susini L, Besse S, Duflaut D, Lespagnol A, Beekman C, Fiucci G, Atkinson AR, Busso D, Poussin P, Marine JC, Martinou JC, Cavarelli J, Moras D, Amson R, Telerman A | title = TCTP protects from apoptotic cell death by antagonizing bax function | journal = Cell Death and Differentiation | volume = 15 | issue = 8 | pages = 1211–20 | date = August 2008 | pmid = 18274553 | doi = 10.1038/cdd.2008.18 |author-link1 = Laurent Susini | doi-access = free }}

Sequence alignment of TCTP sequences from more than 30 different species reveals a high degree of conservation over a long period of evolution.

The solution structure of TCTP from yeast, Schizosaccharomyces pombe has been determined by NMR spectroscopy which indicated that this protein is structurally similar to two small guanine nucleotide-free chaperones, namely Mss4 and Dss4.{{cite journal | vauthors = Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ | title = Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones | journal = Nature Structural Biology | volume = 8 | issue = 8 | pages = 701–4 | date = August 2001 | pmid = 11473261 | doi = 10.1038/90415 | s2cid = 6451004 }} TCTP and Mss4/Dss4 are now therefore structurally grouped into one protein superfamily.

Translationally controlled tumor protein (TCTP) is involved in a wide range of molecular interactions with biological and nonbiological partners of various chemical compositions such as proteins, peptides, nucleic acids, carbohydrates, or small molecules. TCTP is therefore an important and versatile binding platform. Many of these protein–protein interactions have been validated, albeit only few received an in-depth structural characterization. In TCTP/tpt1 - Remodeling Signaling from Stem Cell to Disease, focus is on the structural analysis of TCTP and the review of the available literature regarding its interaction network from a structural perspective.{{cite book | vauthors = Telerman A, Amson R | title = TCTP/Tpt1 - Remodeling Signaling from Stem Cell to Disease | chapter = Structural Insights into TCTP and Its Interactions with Ligands and Proteins | series = Results and Problems in Cell Differentiation | volume = 64 | pages = 9–46 | doi = 10.1007/978-3-319-67591-6_2| pmid = 29149402 | year = 2017 | isbn = 978-3-319-67590-9 | url = https://hal.archives-ouvertes.fr/hal-02309075/file/chapitre_TCTP_4Hal.pdf }}

The structure of TCTP has a very complex topology composed of three alpha helices, and eleven beta strands arranged in two small beta-sheets, one larger than the other.{{cite journal |vauthors=Gao J, Ma Y, Yang G, Li G |title=Translationally controlled tumor protein: the mediator promoting cancer invasion and migration and its potential clinical prospects |journal=J Zhejiang Univ Sci B |volume=23 |issue=8 |pages=642–654 |date=August 2022 |pmid=35953758 |pmc=9381325 |doi=10.1631/jzus.B2100910 |url=}}

TCTP is reported to interact with dozens of other proteins, which relates to its functions in many cellular and biological mechanisms.{{cite book | vauthors = Assrir A, Malard F, Lescop E | title = TCTP/Tpt1 - Remodeling Signaling from Stem Cell to Disease | chapter = Structural Insights into TCTP and Its Interactions with Ligands and Proteins | journal = Results Probl Cell Differ. | series = Results and Problems in Cell Differentiation | volume = 64 | pages = 9–46 | date = 2016 | pmid = 29149402 | doi = 10.1007/978-3-319-67591-6_2 | isbn = 978-3-319-67590-9 }} TCTP has been shown for example to interact with:

• Apoptosis regulator BAX
• Mcl-1{{cite journal | vauthors = Liu H, Peng HW, Cheng YS, Yuan HS, Yang-Yen HF | title = Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP | journal = Molecular and Cellular Biology | volume = 25 | issue = 8 | pages = 3117–26 | date = April 2005 | pmid = 15798198 | doi = 10.1128/MCB.25.8.3117-3126.2005 | pmc=1069602}}
• Bcl-xL{{cite journal | vauthors = Thébault S, Agez M, Chi X, Stojko J, Cura V, Telerman SB, Maillet L, Gautier F, Billas-Massobrio I, Birck C, Troffer-Charlier N, Karafin T, Honoré J, Senff-Ribeiro A, Montessuit S, Johnson CM, Juin P, Cianférani S, Martinou JC, Andrews DW, Amson R, Telerman A, Cavarelli J | title = TCTP contains a BH3-like domain, which instead of inhibiting, activates Bcl-xL | journal = Scientific Reports | volume = 6 | pages = 19725 | date = January 2016 | pmid = 26813996 | doi = 10.1038/srep19725 | pmc=4728560| bibcode = 2016NatSR...619725T }}

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{{refend}}

• {{PDBe-KB2|P13693|Human Translationally-controlled tumor protein}}
• {{PDBe-KB2|P63028|Mouse Translationally-controlled tumor protein}}

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