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From Wikipedia, the free encyclopedia
  (Redirected from TWIST1)
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Twist family bHLH transcription factor 1
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TWIST1 ; ACS3; BPES2; BPES3; CRS; CRS1; SCS; TWIST; bHLHa38
External IDs OMIM601622 MGI98872 HomoloGene402 GeneCards: TWIST1 Gene
RNA expression pattern
PBB GE TWIST1 213943 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7291 22160
Ensembl ENSG00000122691 ENSMUSG00000035799
UniProt Q15672 P26687
RefSeq (mRNA) NM_000474 NM_011658
RefSeq (protein) NP_000465 NP_035788
Location (UCSC) Chr 7:
19.06 – 19.16 Mb
Chr 12:
33.96 – 33.96 Mb
PubMed search [1] [2]

Twist-related protein 1 (TWIST1) also known as class A basic helix-loop-helix protein 38 (bHLHa38) is a basic helix-loop-helix transcription factor that in humans is encoded by the TWIST1 gene.[1][2]

Function[edit]

Basic helix-loop-helix (bHLH) transcription factors have been implicated in cell lineage determination and differentiation. The protein encoded by this gene is a bHLH transcription factor and shares similarity with another bHLH transcription factor, Dermo1 (a.k.a. TWIST2). The strongest expression of this mRNA is in placental tissue; in adults, mesodermally derived tissues express this mRNA preferentially.[3]

Twist1 is thought to regulate osteogenic lineage.[4]

Clinical significance[edit]

Mutations in the TWIST1 gene are associated with Saethre-Chotzen syndrome,[5][6] breast cancer,[7] and Sézary Syndrome.[8]

As an oncogene[edit]

Twist plays an essential role in cancer metastasis. Over-expression of Twist or methylation of its promoter is common in metastatic carcinomas. Hence targeting Twist has a great promise as a cancer therapeutic.[9] In cooperation with N-Myc, Twist-1 acts as an oncogene in several cancers including neuroblastoma.[7][10]

Twist is activated by a variety of signal transduction pathways, including Akt, signal transducer and activator of transcription 3 (STAT3), mitogen-activated protein kinase, Ras, and Wnt signaling. Activated Twist upregulates N-cadherin and downregulates E-cadherin, which are the hallmarks of EMT. Moreover, Twist plays an important role in some physiological processes involved in metastasis, like angiogenesis, invadopodia, extravasation, and chromosomal instability. Twist also protects cancer cells from apoptotic cell death. In addition, Twist is responsible for the maintenance of cancer stem cells and the development of chemotherapy resistance.[9] Twist1 is extensively studied for its role in head- and neck cancers.[11] Here, Twist1 has been shown to be involved in evading apoptosis, making the tumour cells resistant against chemotherapeutic drugs like cisplatin.[12] Moreover, Twist1 has been shown to be expressed under conditions of hypoxia, corresponding to the observation that hypoxic cells respond less to chemotherapeutic drugs.[11]

Another process in which Twist 1 is involved is tumour metastasis. The underlying mechanism is not completely understood, but it has been implicated in the upregulation of matrix metalloproteinases[13] and inhibition of TIMP.[14]

Recently, targeting Twist has gained interest as a target for cancer therapeutics. The inactivation of Twist by small interfering RNA or chemotherapeutic approach has been demonstrated in vitro. Moreover, several inhibitors which are antagonistic to the upstream or downstream molecules of Twist signaling pathways have also been identified.[9]

Interactions[edit]

Twist transcription factor has been shown to interact with EP300,[15] TCF3[16] and PCAF.[15]

See also[edit]

References[edit]

  1. ^ Bourgeois P, Stoetzel C, Bolcato-Bellemin AL, Mattei MG, Perrin-Schmitt F (December 1996). "The human H-twist gene is located at 7p21 and encodes a B-HLH protein that is 96% similar to its murine M-twist counterpart". Mamm. Genome 7 (12): 915–7. doi:10.1007/s003359900269. PMID 8995765. 
  2. ^ Dollfus H, Kumaramanickavel G, Biswas P, Stoetzel C, Quillet R, Denton M, Maw M, Perrin-Schmitt F (July 2001). "Identification of a new TWIST mutation (7p21) with variable eyelid manifestations supports locus homogeneity of BPES at 3q22". J. Med. Genet. 38 (7): 470–2. doi:10.1136/jmg.38.7.470. PMC 1757180. PMID 11474656. 
  3. ^ "Entrez Gene: TWIST1 twist homolog 1 (acrocephalosyndactyly 3; Saethre-Chotzen syndrome) (Drosophila)". 
  4. ^ Lee MS, Lowe GN, Strong DD, Wergedal JE, Glackin CA (December 1999). "TWIST, a basic helix-loop-helix transcription factor, can regulate the human osteogenic lineage". J. Cell. Biochem. 75 (4): 566–77. doi:10.1002/(SICI)1097-4644(19991215)75:4<566::AID-JCB3>3.0.CO;2-0. PMID 10572240. 
  5. ^ Kress W, Schropp C, Lieb G, Petersen B, Büsse-Ratzka M, Kunz J, Reinhart E, Schäfer WD, Sold J, Hoppe F, Pahnke J, Trusen A, Sörensen N, Krauss J, Collmann H (January 2006). "Saethre-Chotzen syndrome caused by TWIST 1 gene mutations: functional differentiation from Muenke coronal synostosis syndrome". Eur. J. Hum. Genet. 14 (1): 39–48. doi:10.1038/sj.ejhg.5201507. PMID 16251895. 
  6. ^ Howard TD, Paznekas WA, Green ED, Chiang LC, Ma N, Ortiz de Luna RI, Garcia Delgado C, Gonzalez-Ramos M, Kline AD, Jabs EW (January 1997). "Mutations in TWIST, a basic helix-loop-helix transcription factor, in Saethre-Chotzen syndrome". Nat. Genet. 15 (1): 36–41. doi:10.1038/ng0197-36. PMID 8988166. 
  7. ^ a b Martin TA, Goyal A, Watkins G, Jiang WG (June 2005). "Expression of the transcription factors snail, slug, and twist and their clinical significance in human breast cancer". Ann. Surg. Oncol. 12 (6): 488–96. doi:10.1245/ASO.2005.04.010. PMID 15864483. 
  8. ^ van Doorn R, Dijkman R, Vermeer MH, Out-Luiting JJ, van der Raaij-Helmer EM, Willemze R, Tensen CP (August 2004). "Aberrant expression of the tyrosine kinase receptor EphA4 and the transcription factor twist in Sézary syndrome identified by gene expression analysis". Cancer Res. 64 (16): 5578–86. doi:10.1158/0008-5472.CAN-04-1253. PMID 15313894. 
  9. ^ a b c Khan MA, Chen HC, Zhang D, Fu J (July 2013). "Twist: a molecular target in cancer therapeutics". Tumour Biol. 34 (5): 2497–506. doi:10.1007/s13277-013-1002-x. PMID 23873099. 
  10. ^ Puisieux A, Valsesia-Wittmann S, Ansieau S (January 2006). "A twist for survival and cancer progression". Br. J. Cancer 94 (1): 13–7. doi:10.1038/sj.bjc.6602876. PMC 2361066. PMID 16306876. 
  11. ^ a b Wu KJ, Yang MH (December 2011). "Epithelial-mesenchymal transition and cancer stemness: the Twist1-Bmi1 connection". Biosci. Rep. 31 (6): 449–55. doi:10.1042/BSR20100114. PMID 21919891. 
  12. ^ Zhuo WL, Wang Y, Zhuo XL, Zhang YS, Chen ZT (May 2008). "Short interfering RNA directed against TWIST, a novel zinc finger transcription factor, increases A549 cell sensitivity to cisplatin via MAPK/mitochondrial pathway". Biochem. Biophys. Res. Commun. 369 (4): 1098–102. doi:10.1016/j.bbrc.2008.02.143. PMID 18331824. 
  13. ^ Zhao XL, Sun T, Che N, Sun D, Zhao N, Dong XY, Gu Q, Yao Z, Sun BC (March 2011). "Promotion of hepatocellular carcinoma metastasis through matrix metalloproteinase activation by epithelial-mesenchymal transition regulator Twist1". J. Cell. Mol. Med. 15 (3): 691–700. doi:10.1111/j.1582-4934.2010.01052.x. PMID 20219012. 
  14. ^ Okamura H, Yoshida K, Haneji T (July 2009). "Negative regulation of TIMP1 is mediated by transcription factor TWIST1". Int. J. Oncol. 35 (1): 181–6. doi:10.3892/ijo_00000327. PMID 19513566. 
  15. ^ a b Hamamori Y, Sartorelli V, Ogryzko V, Puri PL, Wu HY, Wang JY, Nakatani Y, Kedes L (February 1999). "Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A". Cell 96 (3): 405–13. doi:10.1016/S0092-8674(00)80553-X. PMID 10025406. 
  16. ^ El Ghouzzi V, Legeai-Mallet L, Aresta S, Benoist C, Munnich A, de Gunzburg J, Bonaventure J (March 2000). "Saethre-Chotzen mutations cause TWIST protein degradation or impaired nuclear location". Hum. Mol. Genet. 9 (5): 813–9. doi:10.1093/hmg/9.5.813. PMID 10749989. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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