Tafazzin

TAZ
Identifiers
AliasesTAZ, BTHS, CMD3A, EFE, EFE2, G4.5, LVNCX, Taz1, tafazzin
External IDsMGI: 109626 HomoloGene: 37264 GeneCards: TAZ
Gene location (Human)
Chr.X chromosome (human)[1]
BandXq28Start154,411,518 bp[1]
End154,421,726 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

6901

66826

Ensembl

ENSG00000102125

ENSMUSG00000009995

UniProt

Q16635

n/a

RefSeq (mRNA)

NM_001173547
NM_001242615
NM_001242616
NM_001290738
NM_181516

RefSeq (protein)

NP_000107
NP_001290394
NP_851828
NP_851829
NP_851830

n/a

Location (UCSC)Chr X: 154.41 – 154.42 MbChr X: 74.28 – 74.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Tafazzin
Identifiers
Symbol TAZ
InterPro IPR000872
Membranome 459

Tafazzin is a protein that in humans is encoded by the TAZ gene.[5] Tafazzin is highly expressed in cardiac and skeletal muscle, and functions as a phospholipid-lysophospholipid transacylase (it belongs to phospholipid:diacylglycerol acyltransferases).[6][7] It catalyzes remodeling of immature cardiolipin to its mature composition containing a predominance of tetralinoleoyl moieties.[8] Several different isoforms of the tafazzin protein are produced from the TAZ gene. A long form and a short form of each of these isoforms is produced; the short form lacks a hydrophobic leader sequence and may exist as a cytoplasmic protein rather than being membrane-bound. Other alternatively spliced transcripts have been described but the full-length nature of all these transcripts is not known. Most isoforms are found in all tissues, but some are found only in certain types of cells.[9][5] Mutations in the TAZ gene have been associated with mitochondrial deficiency, Barth syndrome, dilated cardiomyopathy (DCM), hypertrophic DCM, endocardial fibroelastosis, left ventricular noncompaction (LVNC), breast cancer, papillary thyroid carcinoma, non-small cell lung cancer, glioma, gastric cancer, thyroid neoplasms, and rectal cancer.[5][10][11][12]

Structure

The TAZ gene is located on the q arm of chromosome X at position 28 and it spans 10,208 base pairs.[5] The TAZ gene produces a 21.3 kDa protein composed of 184 amino acids.[13][14] The structure of the encoded protein has been found to differ at their N terminus and the central region, which are two functionally notable regions. A 30 residue hydrophobic stretch at the N terminus may function as a membrane anchor, which does not exist in the shortest forms of tafazzins. The second region is a variable exposed loop located between amino acids 124 and 195 in the central region. This hydrophilic region is known to interact with other proteins. TAZ has no known resemblance to other proteins.[15]

It is important to note that TAZ shares about 50% sequence similarity with fellow transcriptional co-activator YAP, though TAZ contains both an N-terminal phosphodegron and a C-terminal phosphodegradon, while YAP only contains the C-terminal phosphodegradon. These domains are important for the tight regulation of YAP/TAZ in the Hippo pathway.[10]

Function

The TAZ gene provides instructions for producing a protein called tafazzin, which is located in structures called mitochondria, which are the energy-producing centers of cells. Tafazzin is involved in altering a fat (lipid) called cardiolipin (CL), which plays critical roles in the mitochondrial inner membrane.[9]

Transacylase (remodeling)

After its synthesis, cardiolipin cannot exert its proper functions until it is actively remodeled. The remodeling process of cardiolipin involves reaching a final acyl composition. TAZ interacts with an immature cardiolipin by adding a fatty acid called linoleic acid, which catalyzes the remodeling of the cardiolipin. The remodeling is achieved by transacylation or the deacylation-reacylation cycle. The deacylation-reacylation cycle, also known as the Lands cycle begins with a deacylation mediated by a phospholipase and ends which forms monolyso-CL (MLCL). The cycle ends with a CoA-dependent reacylation. In contrast, transacylation involves the transfer of a linoleic acid (LA) group from phosphatidylcholine (PC) to MLCL. Such enzymatic activity forms lyso-PC and CL, and enriches the specific acyl chain of cardiolipin. The process has been shown to be specific for linoleoyl-containing PC. Such remodeling processes converts cardiolipin into a mature composition that contains a predominance of tetralinoleoyl moieties. The process enables the proper function of cardiolipin.[8][9][16]

Cardiolipin in mitochondrial structure and function

Cardiolipin is a complex glycerophospholipid which contains 4 acyl groups linked to three glycerol moietie localized in the mitochondrial inner membrane. These acyl groups include oleic acid and linoleic acid. Due to this composition, cardiolipin exhibits a conical structure, which allows for membrane curvature called cristae. Such qualities allow CL to play essential roles in maintaining mitochondrial shape, energy production, and protein transport within cells.[9] During apoptosis and similar processes, CL is known to act as a platform for proteins and other machinery involved.

Influence of cardiolipin on the respiratory chain

Cardiolipin has been shown to assist in energy production of the mitochondria. Several proteins in the mitochondrial respiratory chain require CL for optimal function.[17] CL has been found to be involved in the stabilization of each respiratory chain complex, enabling efficient electron transport.[18] CL assists in forming super-complexes with proteins localized in the inner mitochondrial matrix, which include the ATP/ADP translocase, pyruvate carrier, carnitine carrier, and all of the respiratory chain complexes (I, III,IV, V). [19][20] CL also enables trapping of protons in the intermembrane space, aiding ATP synthase to carry out its function of channeling protons into the mitochondrial matrix.[16]

Hippo signaling pathway

Additionally, TAZ, along with YAP, are transcription co-activators involved in the Hippo signaling pathway and many of its functions. The Hippo signaling pathway is involved in development and homeostasis, contributing to tissue growth, differentiation, organ size control, and regeneration. The pathway has been best studied in Drosophila, however, it has been shown to be highly conserved and functionally important in regulation across species, including mammals.[21] TAZ is important for normal development and homeostasis through its involvement in the regulation of gene expression, cell proliferation, apoptosis, organ size and development, stem cell differentiation, and epithelial-mesenchymal transition (EMT).

Due to its function, the dysregulation of the Hippo pathway, and specifically, increased TAZ protein levels have been associated with tumorigenesis, oncogenic activity, and various cancers. Due to this, TAZ is highly regulated by multiple proteins involved in the Hippo pathway. The tumor suppressor LATS kinase has been shown to inhibit TAZ through C-terminal phosphodegron phosphorylation that results in cytoplasmic retention, ubiquitylation, and degradation. This can also occur through the phosphorylation of the TAZ N-terminal phosphodegron by GSK3. High levels of cellular PI3K signaling, however, can inhibit this GSK3-mediated degradation and these conditions have been associated with an increase in tumorigenesis.[10] Tumor suppression of TAZ has also been shown to involve SCFβ-TrCP E3 ubiquitin ligase and CK1ϵ, which both contribute to the cytoplasmic retention and degradation of TAZ, preventing its aggregation in the nucleus where it would affect transcription and impact impact various cellular processes.[22]

Finally, YAP/TAZ and the Hippo pathway have also been analyzed for their impact on innate immunity through their inhibition of TBK1, although this process is not well understood.[23]

Model organisms

Since TAZ is highly important in multiple cellular processes and a part of several highly complex pathways, scientists have used animal models to study its functions and effects. Drosophila studies have indicated the YAP/TAZ inhibit TBK1, which is involved in the anti-viral response by preventing its binding and function. Degradation of YAP/TAZ thus boosts the TBK1 anti-viral response, however, without YAP/TAZ, RNA/DNA sensing is diminished, which in turn lessens the ability of the innate immune system to response to invaders. Although this process is still being understood, it may be important in understanding the links between cellular signaling status and defense against viruses.[23] Other studies with knock-out mice have demonstrated the impact that hyperactive TAZ can have on tumorigenesis, various cancers, polycystic kidney disease and emphysema.[10]

Clinical significance

Mutations in the TAZ gene have been associated with a number of mitochondrial deficiencies and associated disorders including Barth syndrome, dilated cardiomyopathy (DCM), hypertrophic DCM, endocardial fibroelastosis, and left ventricular noncompaction (LVNC).[5] TAZ has also been associated with and various cancers, including breast cancer, papillary thyroid carcinoma and non-small cell lung cancer, glioma, gastric cancer, thyroid neoplasms, and rectal cancer.[10][11][12]

Barth Syndrome

Barth syndrome is an X-linked disease caused by mutations in the TAZ gene.[24][25] More than 160 mutations in the TAZ gene have been found to this disease. It is a rare condition that occurs almost exclusively in males. TAZ gene mutations that cause barth syndrome result in the production of tafazzin proteins with little or no function. As a result, linoleic acid is not added to cardiolipin, which causes problems with normal mitochondrial shape and functions such as energy production and protein transport. Tissues with high energy demands, such as the heart and other muscles, are most susceptible to cell death due to reduced energy production in mitochondria. Additionally, affected white blood cells have abnormally shaped mitochondria, which could impair their ability to grow (proliferate) and mature (differentiate), leading to a weakened immune system and recurrent infections. Dysfunctional mitochondria likely lead to other signs and symptoms of Barth syndrome.[9]

Common clinical manifestations include:[9][24][25]

Additional features include hypertrophic cardiomyopathy, isolated left ventricular non-compaction, ventricular arrhythmia, motor delay, poor appetite, fatigue and exercise intolerance, hypoglycemia, lactic acidosis, hyperammonemia, and dramatic late catch-up growth after growth delay throughout childhood.[24] [25]

A c.348C>T mutation resulted in dilated cardiomyopathy with noncompaction of the ventricular myocardium.[26] A frame shift mutation of c.227delC displayed symptoms of neutropenia, cardiomegaly, and other common symptoms of Bath Syndrome.[27] Another a c.C153G mutation resulted in severe metabolic acidosis, cardiomegaly, and other major symptoms of Barth syndrome.[28]

In conclusion, tafazzin is responsible for remodeling of a phospholipid cardiolipin (CL),[29] the signature lipid of the mitochondrial inner membrane. Therefore, a dysfunctioning tafazzin has been found to lead to an impaired mitochondrial respiratory chain. As a result, Barth syndrome patients exhibit defects in cardiolipin metabolism, including aberrant cardiolipin fatty acyl composition, accumulation of monolysocardiolipin (MLCL) and reduced total cardiolipin levels.[30][31] This may lead to acute metabolic decompensation and sudden death. Cardiac transplantation is the only possibility at the present time.[28]

Dilated cardiomyopathy (DCM)

Some mutations in the TAZ gene cause dilated cardiomyopathy without the other features of Barth syndrome. Dilated cardiomyopathy is a condition in which the heart becomes weakened and enlarged and cannot pump blood efficiently, often resulting in heart failure. The decreased blood flow can lead to swelling in the legs and abdomen, fluid in the lungs, and an increased risk of blood clots.[9]

Isolated noncompaction of left ventricular myocardium (INVM)

Mutations in the TAZ gene can cause a heart condition called isolated noncompaction of left ventricular myocardium (INVM). This condition occurs when the lower left chamber of the heart (left ventricle) does not develop correctly. In INVM, the heart muscle is weakened and cannot pump blood efficiently. Abnormal heart rhythms (arrhythmias) can also occur. INVM frequently causes heart failure.[9]

Cancer

Highly elevated TAZ activity has been linked to tumorigenesis and oncogenic activity. It has also been associated with and various cancers, including breast cancer, papillary thyroid carcinoma and non-small cell lung cancer, and glioma.[10] In breast cancer, TAZ has been shown to be required for cancer cells to sustain self-renewal and create tumors.[32] Additionally, TAZ has been found to be highly expressed in gastric cancer cells resistant to cisplatin. This resistance was identified to be due to the acquired ability of the cancer cells to undergo epithelial-mesenchymal transition (EMT). The findings that TAZ is involved in inducing EMT as well as its high levels in these cancer cells may point to its involvement in gastric cancer.[10][11] High expression of TAZ was also found in rectal cancer and thyroid neoplasms, indicating that TAZ may promote tumorigenesis and inhibit apoptosis.[12] In a study of 140 Swedish rectal cancer patients, high levels of TAZ was linked to rectal cancer development. Additionally, the levels of TAZ were connected to the radiotherapy response of the patients, potentially offering insight into cancer recurrence in patients.[33] A potential link between PI3K and TAZ indicates a possible association between PI3K signaling and TAZ as both were highly elevated in PTEN mutant cancer cells.[10]

Interactions

TAZ has been shown to have protein-protein interactions with the following and more.[34][24]

TAZ has also been shown to have multiple interactions with proteins involved in the Hippo pathway, innate immunity, and with proteins involved in its regulation.

In the cytoplasm, TAZ has been shown to interact with LATS1/2 kinases, GSK3 in response to PI3K signaling, SCFβ-TrCP E3 ubiquitin ligase, and CK1ϵ.[10][22]

Once in the nucleus, TAZ acts as an activator and interacts with TEADs and other transcription factors.[35]

History

The protein was identified by Italian scientists Silvia Bione et al. in 1996.[15] 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.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000102125 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000009995 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 3 4 5 "Entrez Gene: tafazzin". This article incorporates text from this source, which is in the public domain.
  6. ↑ Xu Y, Zhang S, Malhotra A, Edelman-Novemsky I, Ma J, Kruppa A, Cernicica C, Blais S, Neubert TA, Ren M, Schlame M (October 2009). "Characterization of tafazzin splice variants from humans and fruit flies". The Journal of Biological Chemistry. 284 (42): 29230–9. doi:10.1074/jbc.M109.016642. PMC 2781466. PMID 19700766.
  7. ↑ Xu Y, Malhotra A, Ren M, Schlame M (December 2006). "The enzymatic function of tafazzin". The Journal of Biological Chemistry. 281 (51): 39217–24. doi:10.1074/jbc.M606100200. PMID 17082194.
  8. 1 2 Acehan D, Vaz F, Houtkooper RH, James J, Moore V, Tokunaga C, Kulik W, Wansapura J, Toth MJ, Strauss A, Khuchua Z (January 2011). "Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome". The Journal of Biological Chemistry. 286 (2): 899–908. doi:10.1074/jbc.M110.171439. PMC 3020775. PMID 21068380.
  9. 1 2 3 4 5 6 7 8 "TAZ". Genetics Home Reference. NCBI. This article incorporates text from this source, which is in the public domain.
  10. 1 2 3 4 5 6 7 8 9 Huang W, Lv X, Liu C, Zha Z, Zhang H, Jiang Y, Xiong Y, Lei QY, Guan KL (July 2012). "The N-terminal phosphodegron targets TAZ/WWTR1 protein for SCFβ-TrCP-dependent degradation in response to phosphatidylinositol 3-kinase inhibition". The Journal of Biological Chemistry. 287 (31): 26245–53. doi:10.1074/jbc.M112.382036. PMC 3406709. PMID 22692215.
  11. 1 2 3 Ge L, Li DS, Chen F, Feng JD, Li B, Wang TJ (July 2017). "TAZ overexpression is associated with epithelial-mesenchymal transition in cisplatin-resistant gastric cancer cells". International Journal of Oncology. 51 (1): 307–315. doi:10.3892/ijo.2017.3998. PMID 28534974.
  12. 1 2 3 Chen M, Zhang Y, Zheng PS (2017). "Tafazzin (TAZ) promotes the tumorigenicity of cervical cancer cells and inhibits apoptosis". PloS One. 12 (5): e0177171. doi:10.1371/journal.pone.0177171. PMC 5425199. PMID 28489874.
  13. ↑ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (October 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
  14. ↑ "TAZ Tafazzin". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).
  15. 1 2 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". Nature Genetics. 12 (4): 385–9. doi:10.1038/ng0496-385. PMID 8630491.
  16. 1 2 Houtkooper RH, Turkenburg M, Poll-The BT, Karall D, Pérez-Cerdá C, Morrone A, Malvagia S, Wanders RJ, Kulik W, Vaz FM (October 2009). "The enigmatic role of tafazzin in cardiolipin metabolism". Biochimica et Biophysica Acta. 1788 (10): 2003–14. doi:10.1016/j.bbamem.2009.07.009. PMID 19619503.
  17. ↑ Houtkooper RH, Vaz FM (August 2008). "Cardiolipin, the heart of mitochondrial metabolism". Cellular and Molecular Life Sciences. 65 (16): 2493–506. doi:10.1007/s00018-008-8030-5. PMID 18425414.
  18. ↑ Brandner K, Mick DU, Frazier AE, Taylor RD, Meisinger C, Rehling P (November 2005). "Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome". Molecular Biology of the Cell. 16 (11): 5202–14. doi:10.1091/mbc.e05-03-0256. PMID 16135531.
  19. ↑ Barth, PG; Valianpour, F; Bowen, VM; Lam, J; Duran, M; Vaz, FM; Wanders, RJ (1 May 2004). "X-linked cardioskeletal myopathy and neutropenia (Barth syndrome): an update". American journal of medical genetics. Part A. 126A (4): 349–54. doi:10.1002/ajmg.a.20660. PMID 15098233.
  20. ↑ Hoffmann B, Stöckl A, Schlame M, Beyer K, Klingenberg M (January 1994). "The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants". The Journal of Biological Chemistry. 269 (3): 1940–4. PMID 8294444.
  21. ↑ Liu B, Zheng Y, Yin F, Yu J, Silverman N, Pan D (January 2016). "Toll Receptor-Mediated Hippo Signaling Controls Innate Immunity in Drosophila". Cell. 164 (3): 406–19. doi:10.1016/j.cell.2015.12.029. PMC 4733248. PMID 26824654.
  22. 1 2 Liu CY, Zha ZY, Zhou X, Zhang H, Huang W, Zhao D, Li T, Chan SW, Lim CJ, Hong W, Zhao S, Xiong Y, Lei QY, Guan KL (November 2010). "The hippo tumor pathway promotes TAZ degradation by phosphorylating a phosphodegron and recruiting the SCF{beta}-TrCP E3 ligase". The Journal of Biological Chemistry. 285 (48): 37159–69. doi:10.1074/jbc.M110.152942. PMC 2988322. PMID 20858893.
  23. 1 2 Zhang Q, Meng F, Chen S, Plouffe SW, Wu S, Liu S, Li X, Zhou R, Wang J, Zhao B, Liu J, Qin J, Zou J, Feng XH, Guan KL, Xu P (April 2017). "Hippo signalling governs cytosolic nucleic acid sensing through YAP/TAZ-mediated TBK1 blockade". Nature Cell Biology. 19 (4): 362–374. doi:10.1038/ncb3496. PMC 5398908. PMID 28346439.
  24. 1 2 3 4 "TAZ - Tafazzin - Homo sapiens (Human) - TAZ gene & protein". Retrieved 2018-08-24.
  25. 1 2 3 "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
  26. ↑ Ferri L, Dionisi-Vici C, Taurisano R, Vaz FM, Guerrini R, Morrone A (November 2016). "When silence is noise: infantile-onset Barth syndrome caused by a synonymous substitution affecting TAZ gene transcription". Clinical Genetics. 90 (5): 461–465. doi:10.1111/cge.12756. PMID 26853223.
  27. ↑ Kim GB, Kwon BS, Bae EJ, Noh CI, Seong MW, Park SS (May 2013). "A novel mutation of the TAZ gene in Barth syndrome: acute exacerbation after contrast-dye injection". Journal of Korean Medical Science. 28 (5): 784–7. doi:10.3346/jkms.2013.28.5.784. PMC 3653095. PMID 23678274.
  28. 1 2 Yen TY, Hwu WL, Chien YH, Wu MH, Lin MT, Tsao LY, Hsieh WS, Lee NC (August 2008). "Acute metabolic decompensation and sudden death in Barth syndrome: report of a family and a literature review". European Journal of Pediatrics. 167 (8): 941–4. doi:10.1007/s00431-007-0592-y. PMID 17846786.
  29. ↑ Neuwald AF (August 1997). "Barth syndrome may be due to an acyltransferase deficiency". Current Biology. 7 (8): R465–6. doi:10.1016/S0960-9822(06)00237-5. PMID 9259571.
  30. ↑ Barth PG, Wanders RJ, Vreken P, Janssen EA, Lam J, Baas F (June 1999). "X-linked cardioskeletal myopathy and neutropenia (Barth syndrome) (MIM 302060)". Journal of Inherited Metabolic Disease. 22 (4): 555–67. doi:10.1023/A:1005568609936. PMID 10407787.
  31. ↑ 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". Journal of Lipid Research. 46 (6): 1182–95. doi:10.1194/jlr.M500056-JLR200. PMID 15805542.
  32. ↑ Cordenonsi M, Zanconato F, Azzolin L, Forcato M, Rosato A, Frasson C, Inui M, Montagner M, Parenti AR, Poletti A, Daidone MG, Dupont S, Basso G, Bicciato S, Piccolo S (November 2011). "The Hippo transducer TAZ confers cancer stem cell-related traits on breast cancer cells". Cell. 147 (4): 759–72. doi:10.1016/j.cell.2011.09.048. PMID 22078877.
  33. ↑ Pathak S, Meng WJ, Zhang H, Gnosa S, Nandy SK, Adell G, Holmlund B, Sun XF (2014). "Tafazzin protein expression is associated with tumorigenesis and radiation response in rectal cancer: a study of Swedish clinical trial on preoperative radiotherapy". PloS One. 9 (5): e98317. doi:10.1371/journal.pone.0098317. PMC 4032294. PMID 24858921.
  34. ↑ Mick DU, Dennerlein S, Wiese H, Reinhold R, Pacheu-Grau D, Lorenzi I, Sasarman F, Weraarpachai W, Shoubridge EA, Warscheid B, Rehling P (December 2012). "MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation". Cell. 151 (7): 1528–41. doi:10.1016/j.cell.2012.11.053. PMID 23260140.
  35. ↑ Zhang H, Liu CY, Zha ZY, Zhao B, Yao J, Zhao S, Xiong Y, Lei QY, Guan KL (May 2009). "TEAD transcription factors mediate the function of TAZ in cell growth and epithelial-mesenchymal transition". The Journal of Biological Chemistry. 284 (20): 13355–62. doi:10.1074/jbc.M900843200. PMC 2679435. PMID 19324877.

Further reading

  • "Mouse model of Barth syndrome". SciBX. 3 (47): 1427. Dec 9, 2010. doi:10.1038/scibx.2010.1427.
  • Soustek MS, Falk DJ, Mah CS, Toth MJ, Schlame M, Lewin AS, Byrne BJ (July 2011). "Characterization of a transgenic short hairpin RNA-induced murine model of Tafazzin deficiency". Human Gene Therapy. 22 (7): 865–71. doi:10.1089/hum.2010.199. PMC 3166794. PMID 21091282.
  • Takeda A, Sudo A, Yamada M, Yamazawa H, Izumi G, Nishino I, Ariga T (November 2011). "Barth syndrome diagnosed in the subclinical stage of heart failure based on the presence of lipid storage myopathy and isolated noncompaction of the ventricular myocardium". European Journal of Pediatrics. 170 (11): 1481–4. doi:10.1007/s00431-011-1576-5. PMID 21932011.
  • Bachou T, Giannakopoulos A, Trapali C, Vazeou A, Kattamis A (2009). "A novel mutation in the G4.5 (TAZ) gene in a Greek patient with Barth syndrome". Blood Cells, Molecules & Diseases. 42 (3): 262–4. doi:10.1016/j.bcmd.2008.11.004. PMID 19261493.
  • Gonzalez IL (May 2005). "Barth syndrome: TAZ gene mutations, mRNAs, and evolution". American Journal of Medical Genetics. Part A. 134 (4): 409–14. doi:10.1002/ajmg.a.30661. PMID 15793838.
  • Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  • Zimmerman RS, Cox S, Lakdawala NK, Cirino A, Mancini-DiNardo D, Clark E, Leon A, Duffy E, White E, Baxter S, Alaamery M, Farwell L, Weiss S, Seidman CE, Seidman JG, Ho CY, Rehm HL, Funke BH (May 2010). "A novel custom resequencing array for dilated cardiomyopathy". Genetics in Medicine. 12 (5): 268–78. doi:10.1097/GIM.0b013e3181d6f7c0. PMC 3018746. PMID 20474083.
  • Malhotra A, Edelman-Novemsky I, Xu Y, Plesken H, Ma J, Schlame M, Ren M (February 2009). "Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome". Proceedings of the National Academy of Sciences of the United States of America. 106 (7): 2337–41. doi:10.1073/pnas.0811224106. PMC 2650157. PMID 19164547.
  • van Werkhoven MA, Thorburn DR, Gedeon AK, Pitt JJ (October 2006). "Monolysocardiolipin in cultured fibroblasts is a sensitive and specific marker for Barth Syndrome". Journal of Lipid Research. 47 (10): 2346–51. doi:10.1194/jlr.D600024-JLR200. PMID 16873891.
  • Acehan D, Xu Y, Stokes DL, Schlame M (January 2007). "Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography". Laboratory Investigation; A Journal of Technical Methods and Pathology. 87 (1): 40–8. doi:10.1038/labinvest.3700480. PMC 2215767. PMID 17043667.
  • Barth PG, Wanders RJ, Vreken P, Janssen EA, Lam J, Baas F (June 1999). "X-linked cardioskeletal myopathy and neutropenia (Barth syndrome) (MIM 302060)". Journal of Inherited Metabolic Disease. 22 (4): 555–67. doi:10.1023/A:1005568609936. PMID 10407787.
  • Claypool SM, Boontheung P, McCaffery JM, Loo JA, Koehler CM (December 2008). "The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome". Molecular Biology of the Cell. 19 (12): 5143–55. doi:10.1091/mbc.E08-09-0896. PMC 2592642. PMID 18799610.
  • Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (January 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • McKenzie M, Lazarou M, Thorburn DR, Ryan MT (August 2006). "Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients". Journal of Molecular Biology. 361 (3): 462–9. CiteSeerX 10.1.1.314.3366. doi:10.1016/j.jmb.2006.06.057. PMID 16857210.
  • Lu B, Kelher MR, Lee DP, Lewin TM, Coleman RA, Choy PC, Hatch GM (October 2004). "Complex expression pattern of the Barth syndrome gene product tafazzin in human cell lines and murine tissues". Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 82 (5): 569–76. doi:10.1139/o04-055. PMID 15499385.
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