From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Aliases TAZ, BTHS, CMD3A, EFE, EFE2, G4.5, LVNCX, Taz1, tafazzin
External IDs MGI: 109626 HomoloGene: 37264 GeneCards: TAZ
Gene location (Human)
X chromosome (human)
Chr. X chromosome (human)[1]
X chromosome (human)
Genomic location for TAZ
Genomic location for TAZ
Band Xq28 Start 154,411,518 bp[1]
End 154,421,726 bp[1]
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)



Location (UCSC) Chr X: 154.41 – 154.42 Mb Chr X: 74.28 – 74.29 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Tafazzin is a protein that in humans is encoded by the TAZ gene.[5] Tafazzin is highly expressed in cardiac and skeletal muscle. It is involved in the metabolism of cardiolipin.[6]

Tafazzin functions as a phospholipid-lysophospholipid transacylase.[7][8]


The mutation of the tafazzin gene is associated with a number of clinical disorders including Barth syndrome (BTHS) (type II 3-Methylglutaconic aciduria), dilated cardiomyopathy (DCM), hypertrophic DCM, endocardial fibroelastosis, and left ventricular noncompaction (LVNC). Tafazzin is responsible for remodeling of a phospholipid cardiolipin (CL),[9] the signature lipid of the mitochondrial inner membrane. As a result, BTHS patients exhibit defects in CL metabolism, including aberrant CL fatty acyl composition, accumulation of monolysocardiolipin (MLCL) and reduced total CL levels.[10][11]


The protein was identified by Italian scientists Silvia Bione et al. in 1996.[12] Owing to the complex procedure required for the identification of tafazzin, the protein was named after "Tafazzi", a masochistic comic character in an Italian television show.


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000102125 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009995 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ "Entrez Gene: tafazzin". 
  6. ^ Malhotra A, Xu Y, Ren M, Schlame M (April 2009). "Formation of molecular species of mitochondrial cardiolipin. 1. A novel transacylation mechanism to shuttle fatty acids between sn-1 and sn-2 positions of multiple phospholipid species". Biochim. Biophys. Acta. 1791 (4): 314–20. doi:10.1016/j.bbalip.2009.01.004. PMC 2679859Freely accessible. PMID 19416660. 
  7. ^ Xu Y, Zhang S, Malhotra A, et al. (October 2009). "Characterization of Tafazzin Splice Variants from Humans and Fruit Flies". J. Biol. Chem. 284 (42): 29230–9. doi:10.1074/jbc.M109.016642. PMC 2781466Freely accessible. PMID 19700766. 
  8. ^ Xu Y, Malhotra A, Ren M, Schlame M (December 2006). "The enzymatic function of tafazzin". J. Biol. Chem. 281 (51): 39217–24. doi:10.1074/jbc.M606100200. PMID 17082194. 
  9. ^ Neuwald AF (August 1997). "Barth syndrome may be due to an acyltransferase deficiency". Curr. Biol. 7 (8): R465–6. doi:10.1016/S0960-9822(06)00237-5. PMID 9259571. 
  10. ^ Barth PG, Wanders RJ, Vreken P, Janssen EA, Lam J, Baas F (June 1999). "X-linked cardioskeletal myopathy and neutropenia (Barth syndrome) (MIM 302060)". J. Inherit. Metab. Dis. 22 (4): 555–67. doi:10.1023/A:1005568609936. PMID 10407787. 
  11. ^ Valianpour F, Mitsakos V, Schlemmer D, Towbin JA, Taylor JM, Ekert PG, Thorburn DR, Munnich A, Wanders RJ, Barth PG, Vaz FM (June 2005). "Monolysocardiolipins accumulate in Barth syndrome but do not lead to enhanced apoptosis". J. Lipid Res. 46 (6): 1182–95. doi:10.1194/jlr.M500056-JLR200. PMID 15805542. 
  12. ^ Bione S, D'Adamo P, Maestrini E, Gedeon AK, Bolhuis PA, Toniolo D (April 1996). "A novel X-linked gene, G4.5. is responsible for Barth syndrome". Nat. Genet. 12 (4): 385–9. doi:10.1038/ng0496-385. PMID 8630491. 

Further reading[edit]

External links[edit]