Translationally controlled tumour protein

TCTP

translationally controlled tumor-associated protein p23fyp from schizosaccharomyces pombe
Identifiers
Symbol TCTP
Pfam PF00838
Pfam clan CL0080
InterPro IPR018105
PROSITE PDOC00768
SCOP 1h7y
SUPERFAMILY 1h7y
Translationally Controlled Tumour Protein
Identifiers
Symbol FLJ27337,tpt1,HRF, p02, p23, p21
OMIM 600763

In molecular biology, the protein TCTP, is short for translationally controlled tumour protein (TCTP).The translationally controlled tumour protein, commonly known as TCTP, is a highly conserved protein among many eukaryotic organisms.[1] TCTP is involved in a variety of cellular activities, including microtubule stabilization, calcium-binding activities, and apoptosis.[1] The Mammalian translationally controlled tumour protein (TCTP) (or P23) is a protein which has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour,[2][3] but which is also expressed in normal cells. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TCTP has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TCTP production is thought to be controlled at the translational as well as the transcriptional level.[4]

Conservation

TCTP is a hydrophilic protein of 18 to 20 kD. TCTPs do not share significant sequence similarity with any other class of proteins. Recently, the structure of TCTP was determined and exhibited significant structural similarity to the human protein Mss4, which is a guanine nucleotide-free chaperone of the Rab protein.[5] Translationally controlled tumor protein (TCTP) is a highly conserved protein found in eukaryotes, across animal and plant kingdoms and even in yeast. Close homologues have been found in plants,[6] earthworm,[7] Caenorhabditis elegans (F52H2.11), Hydra, Saccharomyces cerevisiae (YKL056c) [8] and Schizosaccharomyces pombe (SpAC1F12.02c). Mammalian TCTP is ubiquitously expressed in various tissues and cell types.

Function

Translationally-controlled tumor-associated protein (TCTP) has many roles in cellular processes, most notably in the following:

In essence, TCTP functions as molecule that prevents cell death. It reduces cellular stress working as a heat shock protein and a molecular chaperone. It prevents cell death by binding to calcium, an ion that causes cell death. Furthermore, the N-terminal domain of TCTP inhibits apoptosis by binding to apoptotic factors and by inhibiting p53 tumour suppressor-dependent apoptosis by downregulating it.[9]

TCTP interacts with F-actin and mitotic spindle [10] and regulates cell shape by interacting with the cytoskeleton. Since most cellular processes, such as the cell cycle and cancer, involve changes in the cytoskeleton; it becomes apparent why TCTP is important. Moreover, if the gene encoding TCTP is knocked-out in mice, it becomes embryonic lethal, and they die in utero (in the womb).[11]

Translationally Controlled Tumor Protein (TCTP/tpt1) is a regulator of the cancer stem cell compartment,[12] the tumor reversion program,[13][14] tumor progression and certain forms of inflammatory diseases.[15] Susini L et al. described TCTP as a pro-survival protein by antagonizing BAX function [16]

Structure

This structure has a very complex topology composed of four beta-sheets and three alpha helices.[5]

Interactions

TCTP has been shown to interact with:

References

  1. 1 2 Bommer UA, Thiele BJ (March 2004). "The translationally controlled tumour protein (TCTP)". The International Journal of Biochemistry & Cell Biology. 36 (3): 379–85. doi:10.1016/S1357-2725(03)00213-9. PMID 14687915.
  2. ↑ Böhm H, Benndorf R, Gaestel M, Gross B, Nürnberg P, Kraft R, Otto A, Bielka H (August 1989). "The growth-related protein P23 of the Ehrlich ascites tumor: translational control, cloning and primary structure". Biochemistry International. 19 (2): 277–86. PMID 2479380.
  3. ↑ Chitpatima ST, Makrides S, Bandyopadhyay R, Brawerman G (March 1988). "Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells". Nucleic Acids Research. 16 (5): 2350. doi:10.1093/nar/16.5.2350. PMC 338237Freely accessible. PMID 3357792.
  4. ↑ Thiele H, Berger M, Skalweit A, Thiele BJ (September 2000). "Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP)". European Journal of Biochemistry / FEBS. 267 (17): 5473–81. doi:10.1046/j.1432-1327.2000.01609.x. PMID 10951206.
  5. 1 2 Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ (August 2001). "Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones". Nature Structural Biology. 8 (8): 701–4. doi:10.1038/90415. PMID 11473261.
  6. ↑ Pay A, Heberle-Bors E, Hirt H (June 1992). "An alfalfa cDNA encodes a protein with homology to translationally controlled human tumor protein". Plant Molecular Biology. 19 (3): 501–3. doi:10.1007/bf00023399. PMID 1623194.
  7. ↑ Stürzenbaum SR, Kille P, Morgan AJ (July 1998). "Identification of heavy metal induced changes in the expression patterns of the translationally controlled tumour protein (TCTP) in the earthworm Lumbricus rubellus1". Biochimica et Biophysica Acta. 1398 (3): 294–304. doi:10.1016/s0167-4781(98)00077-3. PMID 9655922.
  8. ↑ Rasmussen SW (April 1994). "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins". Yeast. 10 Suppl A: S63–8. doi:10.1002/yea.320100008. PMID 8091862.
  9. ↑ Nagano-Ito M, Ichikawa S (2012). "Biological effects of Mammalian translationally controlled tumor protein (TCTP) on cell death, proliferation, and tumorigenesis". Biochemistry Research International. 2012: 204960. doi:10.1155/2012/204960. PMC 3364544Freely accessible. PMID 22675633.
  10. ↑ Gachet Y, Tournier S, Lee M, Lazaris-Karatzas A, Poulton T, Bommer UA (April 1999). "The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle". Journal of Cell Science. 112 ( Pt 8) (8): 1257–71. PMID 10085260.
  11. ↑ Bazile F, Pascal A, Arnal I, Le Clainche C, Chesnel F, Kubiak JZ (April 2009). "Complex relationship between TCTP, microtubules and actin microfilaments regulates cell shape in normal and cancer cells". Carcinogenesis. 30 (4): 555–65. doi:10.1093/carcin/bgp022. PMC 2831045Freely accessible. PMID 19168579.
  12. ↑ 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 (January 2012). "Reciprocal repression between P53 and TCTP". Nature Medicine. 18 (1): 91–9. doi:10.1038/nm.2546. PMID 22157679.
  13. ↑ Tuynder M, Susini L, Prieur S, Besse S, Fiucci G, Amson R, Telerman A (November 2002). "Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1". Proceedings of the National Academy of Sciences of the United States of America. 99 (23): 14976–81. doi:10.1073/pnas.222470799. PMC 137530Freely accessible. PMID 12399545.
  14. ↑ 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 (October 2004). "Translationally controlled tumor protein is a target of tumor reversion". Proceedings of the National Academy of Sciences of the United States of America. 101 (43): 15364–9. doi:10.1073/pnas.0406776101. PMC 523462Freely accessible. PMID 15489264.
  15. ↑ MacDonald SM, Rafnar T, Langdon J, Lichtenstein LM (August 1995). "Molecular identification of an IgE-dependent histamine-releasing factor". Science. 269 (5224): 688–90. doi:10.1126/science.7542803. PMID 7542803.
  16. 1 2 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 (August 2008). "TCTP protects from apoptotic cell death by antagonizing bax function". Cell Death and Differentiation. 15 (8): 1211–20. doi:10.1038/cdd.2008.18. PMID 18274553.
  17. ↑ Liu H, Peng HW, Cheng YS, Yuan HS, Yang-Yen HF (April 2005). "Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP". Molecular and Cellular Biology. 25 (8): 3117–26. doi:10.1128/MCB.25.8.3117. PMID 15798198.
  18. ↑ 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 (January 2016). "TCTP contains a BH3-like domain, which instead of inhibiting, activates Bcl-xL". Scientific Reports. 6: 19725. doi:10.1038/srep19725. PMID 26813996.

This article incorporates text from the public domain Pfam and InterPro IPR018105

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