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Gene Review

TAZ  -  tafazzin

Homo sapiens

Synonyms: BTHS, CMD3A, EFE, EFE2, G4.5, ...
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Disease relevance of TAZ


High impact information on TAZ

  • Different mRNAs can be produced by alternative splicing of the primary G4.5 transcript, encoding novel proteins that differ at the N terminus and in the central region [4].
  • We now report the identification of unique mutations in one of the genes in this region, termed G4.5, expressed at high level in cardiac and skeletal muscle [4].
  • A novel X-linked gene, G4.5. is responsible for Barth syndrome [4].
  • Two genes have been identified for the X-linked forms (dystrophin and tafazzin), whereas three other genes (actin, lamin A/C, and desmin) cause autosomal dominant DCM; seven other loci for autosomal dominant DCM have been mapped but the genes have not been identified [5].
  • Truncation mutants of TBX5 identified in patients with Holt-Oram syndrome were markedly impaired in their ability to associate with and be stimulated by TAZ [6].

Chemical compound and disease context of TAZ


Biological context of TAZ

  • Novel missense mutation (R94S) in the TAZ ( G4.5) gene in a Japanese patient with Barth syndrome [9].
  • Sequence homology of the TAZ gene to a highly conserved superclass of acyltransferases (Neuwald's hypothesis) predicts a glycerophospholipid as the missing end product [10].
  • Molecular analysis of the TAZ (G4.5) gene showed the c.877G > A mutation leading to the G197R amino acid substitution in patient 1, and the new splice donor c.829 + 1G > A genetic lesion in patient 2 [11].
  • A linkage study of the X chromosome localized INVM to the Xq28 region near the BTHS locus, suggesting that these disorders are allelic [2].
  • We screened the G4.5 gene for mutations in this family with SSCP and direct sequencing and found a novel glycine-to-arginine substitution at position 197 [2].

Anatomical context of TAZ

  • The TAZ gene encodes Tafazzin, a putative phospholipid acyltranferase that is involved in the remodeling of cardiolipin, a phospholipid unique to the inner mitochondrial membrane [12].
  • RT-PCR and transcription-coupled in vitro translation analysis were undertaken to determine the expression of alternatively spliced TAZ mRNA in mouse tissues and human cell lines [13].
  • Only two tafazzin transcripts, both lacking exon 5, were expressed in murine tissues, whereas four tafazzin transcripts, all lacking exon 5, were observed in human umbilical vein vascular endothelial cells and U937 human monoblasts indicating a species-specific difference in the expression of TAZ mRNAs in mouse and humans [13].
  • Our results showed a clear decrease of CL in combination with a marked increase of MLCL in fibroblasts from BTHS patients when compared with controls [14].
  • Differentiation of U937 human monoblasts into macrophages did not alter expression of the tafazzin transcripts indicating that TAZ expression is independent of monocyte differentiation [13].

Associations of TAZ with chemical compounds

  • Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism [1].
  • Here, we investigated the effects of Tafazzin, and hence cardiolipin deficiency in lymphoblasts from patients with Barth Syndrome, using blue-native polyacrylamide gel electrophoresis [12].
  • At G4.5, DHEA did not induce formation of DNA ladder until it reached 200 microM [15].
  • DHEA inhibited cell growth by causing cell cycle arrest primarily in the G0--G1 phase, and the effect was more pronounced at zero glucose (no glucose added, G0) than high glucose (4.5 mg/ml of the medium, G4.5) [15].
  • TA and zeranol (Z) were tested singly and in combination (TAZ) [8].

Physical interactions of TAZ


Other interactions of TAZ


Analytical, diagnostic and therapeutic context of TAZ


  1. Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism. Vaz, F.M., Houtkooper, R.H., Valianpour, F., Barth, P.G., Wanders, R.J. J. Biol. Chem. (2003) [Pubmed]
  2. Neonatal, lethal noncompaction of the left ventricular myocardium is allelic with Barth syndrome. Bleyl, S.B., Mumford, B.R., Thompson, V., Carey, J.C., Pysher, T.J., Chin, T.K., Ward, K. Am. J. Hum. Genet. (1997) [Pubmed]
  3. The X-linked gene G4.5 is responsible for different infantile dilated cardiomyopathies. D'Adamo, P., Fassone, L., Gedeon, A., Janssen, E.A., Bione, S., Bolhuis, P.A., Barth, P.G., Wilson, M., Haan, E., Orstavik, K.H., Patton, M.A., Green, A.J., Zammarchi, E., Donati, M.A., Toniolo, D. Am. J. Hum. Genet. (1997) [Pubmed]
  4. A novel X-linked gene, G4.5. is responsible for Barth syndrome. Bione, S., D'Adamo, P., Maestrini, E., Gedeon, A.K., Bolhuis, P.A., Toniolo, D. Nat. Genet. (1996) [Pubmed]
  5. Mutations in the human delta-sarcoglycan gene in familial and sporadic dilated cardiomyopathy. Tsubata, S., Bowles, K.R., Vatta, M., Zintz, C., Titus, J., Muhonen, L., Bowles, N.E., Towbin, J.A. J. Clin. Invest. (2000) [Pubmed]
  6. A WW domain protein TAZ is a critical coactivator for TBX5, a transcription factor implicated in Holt-Oram syndrome. Murakami, M., Nakagawa, M., Olson, E.N., Nakagawa, O. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  7. Phospholipid abnormalities in children with Barth syndrome. Schlame, M., Kelley, R.I., Feigenbaum, A., Towbin, J.A., Heerdt, P.M., Schieble, T., Wanders, R.J., DiMauro, S., Blanck, T.J. J. Am. Coll. Cardiol. (2003) [Pubmed]
  8. Growth and carcass composition of female turkeys implanted with anabolic agents and fed high-protein and low-protein diets. Castaldo, D.J., Jones, J.E., Maurice, D.V. Archiv für Tierernährung. (1990) [Pubmed]
  9. Novel missense mutation (R94S) in the TAZ ( G4.5) gene in a Japanese patient with Barth syndrome. Sakamoto, O., Kitoh, T., Ohura, T., Ohya, N., Iinuma, K. J. Hum. Genet. (2002) [Pubmed]
  10. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome) (MIM 302060). Barth, P.G., Wanders, R.J., Vreken, P., Janssen, E.A., Lam, J., Baas, F. J. Inherit. Metab. Dis. (1999) [Pubmed]
  11. Barth syndrome presenting with acute metabolic decompensation in the neonatal period. Donati, M.A., Malvagia, S., Pasquini, E., Morrone, A., Marca, G.L., Garavaglia, B., Toniolo, D., Zammarchi, E. J. Inherit. Metab. Dis. (2006) [Pubmed]
  12. Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. McKenzie, M., Lazarou, M., Thorburn, D.R., Ryan, M.T. J. Mol. Biol. (2006) [Pubmed]
  13. Complex expression pattern of the Barth syndrome gene product tafazzin in human cell lines and murine tissues. Lu, B., Kelher, M.R., Lee, D.P., Lewin, T.M., Coleman, R.A., Choy, P.C., Hatch, G.M. Biochem. Cell Biol. (2004) [Pubmed]
  14. Monolysocardiolipin in cultured fibroblasts is a sensitive and specific marker for Barth Syndrome. van Werkhoven, M.A., Thorburn, D.R., Gedeon, A.K., Pitt, J.J. J. Lipid Res. (2006) [Pubmed]
  15. DHEA inhibits cell growth and induces apoptosis in BV-2 cells and the effects are inversely associated with glucose concentration in the medium. Yang, N.C., Jeng, K.C., Ho, W.M., Chou, S.J., Hu, M.L. J. Steroid Biochem. Mol. Biol. (2000) [Pubmed]
  16. The transcriptional co-activator TAZ interacts differentially with transcriptional enhancer factor-1 (TEF-1) family members. Mahoney, W.M., Hong, J.H., Yaffe, M.B., Farrance, I.K. Biochem. J. (2005) [Pubmed]
  17. Infantile dilated X-linked cardiomyopathy, G4.5 mutations, altered lipids, and ultrastructural malformations of mitochondria in heart, liver, and skeletal muscle. Bissler, J.J., Tsoras, M., Göring, H.H., Hug, P., Chuck, G., Tombragel, E., McGraw, C., Schlotman, J., Ralston, M.A., Hug, G. Lab. Invest. (2002) [Pubmed]
  18. Role of neutrophil elastase in bone marrow failure syndromes: molecular genetic revival of the chalone hypothesis. Horwitz, M., Benson, K.F., Duan, Z., Person, R.E., Wechsler, J., Williams, K., Albani, D., Li, F.Q. Curr. Opin. Hematol. (2003) [Pubmed]
  19. X-linked fetal cardiomyopathy caused by a novel mutation in the TAZ gene. Brady, A.N., Shehata, B.M., Fernhoff, P.M. Prenat. Diagn. (2006) [Pubmed]
  20. X chromosome inactivation in carriers of Barth syndrome. Orstavik, K.H., Orstavik, R.E., Naumova, A.K., D'Adamo, P., Gedeon, A., Bolhuis, P.A., Barth, P.G., Toniolo, D. Am. J. Hum. Genet. (1998) [Pubmed]
  21. Quantitative and compositional study of cardiolipin in platelets by electrospray ionization mass spectrometry: application for the identification of Barth syndrome patients. Valianpour, F., Wanders, R.J., Barth, P.G., Overmars, H., van Gennip, A.H. Clin. Chem. (2002) [Pubmed]
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