Tumor Biology

, Volume 37, Issue 8, pp 10909–10915 | Cite as

Fascin 1 promoted the growth and migration of non-small cell lung cancer cells by activating YAP/TEAD signaling

  • Zhigang Liang
  • Ying Wang
  • Zhenya Shen
  • Xiaomei Teng
  • Xinjian Li
  • Chenwei Li
  • Weijie Wu
  • Zenghui Zhou
  • Zishan Wang
Original Article

Abstract

Fascin 1 (Fascin actin-bundling protein 1) is an actin-binding protein. Although several studies have reported the dysregulation of Fascin 1 in non-small cell lung cancer (NSCLC), its functions in the progression of NSCLC and the related molecular mechanism were not fully understood. In this study, the expression of Fascin 1 in NSCLC tissues was determined using quantitative PCR (qPCR), and the roles of Fascin 1 in the progression of NSCLC were investigated. It was found that both the messenger RNA (mRNA) level and the protein level of Fascin 1 were upregulated in NSCLC tissues. Forced expression of Fascin 1 promoted the growth and migration of NSCLC cells, while knocking down the expression of Fascin 1 inhibited the growth, migration, and tumorigenesis of NSCLC cells. Mechanism studies showed that Fascin 1 increased the transcriptional activity of the YAP/TEAD (Yes-associated protein/TEA domain transcriptional factor) complex, and knocking down the expression of Fascin 1 attenuated the expression of target genes downstream the YAP/TEAD complex. In addition, MST1 interacted with Fascin 1. Taken together, Fascin 1 plays an oncogenic role in NSCLC by activating the transcriptional activity of the YAP/TEAD complex.

Keywords

NSCLC Fascin 1 YAP/TEAD signaling Cell growth Migration 

Notes

Compliance with ethical standards

Conflicts of interest

None

References

  1. 1.
    Adams JC. Roles of fascin in cell adhesion and motility. Curr Opin Cell Biol. 2004;16:590–6. doi: 10.1016/j.ceb.2004.07.009.CrossRefPubMedGoogle Scholar
  2. 2.
    Elkhatib N, Neu MB, Zensen C, et al. Fascin plays a role in stress fiber organization and focal adhesion disassembly. Curr Biol. 2014;24:1492–9. doi: 10.1016/j.cub.2014.05.023.CrossRefPubMedGoogle Scholar
  3. 3.
    Yamashiro S, Yamakita Y, Ono S, Matsumura F. Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells. Mol Biol Cell. 1998;9:993–1006.CrossRefPubMedPubMedCentralGoogle Scholar
  4. 4.
    Okenve-Ramos P, Llimargas M. Fascin, may the Forked be with you. Fly (Austin). 2014;8:157–64. doi: 10.4161/fly.34368.CrossRefGoogle Scholar
  5. 5.
    Hashimoto Y, Kim DJ, Adams JC. The roles of fascins in health and disease. J Pathol. 2011;224:289–300. doi: 10.1002/path.2894.CrossRefPubMedGoogle Scholar
  6. 6.
    Kureishy N, Sapountzi V, Prag S, Anilkumar N, Adams JC. Fascins, and their roles in cell structure and function. Bioessays. 2002;24:350–61. doi: 10.1002/bies.10070.CrossRefPubMedGoogle Scholar
  7. 7.
    Bompard G, Sharp SJ, Freiss G, Machesky LM. Involvement of Rac in actin cytoskeleton rearrangements induced by MIM-B. J Cell Sci. 2005;118:5393–403. doi: 10.1242/jcs.02640.CrossRefPubMedGoogle Scholar
  8. 8.
    Omran OM, Al Sheeha M. Cytoskeletal focal adhesion proteins fascin-1 and paxillin are predictors of malignant progression and poor prognosis in human breast cancer. J Environ Pathol Toxicol Oncol. 2015;34:201–12.CrossRefPubMedGoogle Scholar
  9. 9.
    Pelosi G, Pastorino U, Pasini F, et al. Independent prognostic value of fascin immunoreactivity in stage I nonsmall cell lung cancer. Br J Cancer. 2003;88:537–47. doi: 10.1038/sj.bjc.6600731.CrossRefPubMedPubMedCentralGoogle Scholar
  10. 10.
    Roh YH, Kim YH, Choi HJ, Lee KE, Roh MS. Fascin overexpression correlates with positive thrombospondin-1 and syndecan-1 expressions and a more aggressive clinical course in patients with gallbladder cancer. J Hepatobiliary Pancreat Surg. 2009;16:315–21. doi: 10.1007/s00534-009-0046-1.CrossRefPubMedGoogle Scholar
  11. 11.
    Fujii M, Toyoda T, Nakanishi H, et al. TGF-beta synergizes with defects in the Hippo pathway to stimulate human malignant mesothelioma growth. J Exp Med. 2012;209:479–94. doi: 10.1084/jem.20111653.CrossRefPubMedPubMedCentralGoogle Scholar
  12. 12.
    Zhao B, Ye X, Yu J, et al. TEAD mediates YAP-dependent gene induction and growth control. Genes Dev. 2008;22:1962–71. doi: 10.1101/gad.1664408.CrossRefPubMedPubMedCentralGoogle Scholar
  13. 13.
    Badouel C, McNeill H. SnapShot: the hippo signaling pathway. Cell. 2011;145:484-484 e1. doi: 10.1016/j.cell.2011.04.009.CrossRefPubMedGoogle Scholar
  14. 14.
    Kim SJ, Kim DC, Kim MC, et al. Fascin expression is related to poor survival in gastric cancer. Pathol Int. 2012;62:777–84. doi: 10.1111/pin.12012.CrossRefPubMedGoogle Scholar
  15. 15.
    Oh SY, Kim YB, Suh KW, Paek OJ, Moon HY. Prognostic impact of Fascin-1 expression is more significant in advanced colorectal cancer. J Surg Res. 2012;172:102–8. doi: 10.1016/j.jss.2010.07.015.CrossRefPubMedGoogle Scholar
  16. 16.
    Mana-Capelli S, Paramasivam M, Dutta S, McCollum D. Angiomotins link F-actin architecture to Hippo pathway signaling. Mol Biol Cell. 2014;25:1676–85. doi: 10.1091/mbc.E13-11-0701.CrossRefPubMedPubMedCentralGoogle Scholar
  17. 17.
    Fernandez BG, Gaspar P, Bras-Pereira C, Jezowska B, Rebelo SR, Janody F. Actin-capping protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila. Development. 2011;138:2337–46. doi: 10.1242/dev.063545.CrossRefPubMedGoogle Scholar
  18. 18.
    Wang J, Zhang Y, Zhang N, Wang C, Herrler T, Li Q. An updated review of mechanotransduction in skin disorders: transcriptional regulators, ion channels, and microRNAs. Cell Mol Life Sci. 2015;72:2091–106. doi: 10.1007/s00018-015-1853-y.CrossRefPubMedGoogle Scholar
  19. 19.
    Halder G, Dupont S, Piccolo S. Transduction of mechanical and cytoskeletal cues by YAP and TAZ. Nat Rev Mol Cell Biol. 2012;13:591–600. doi: 10.1038/nrm3416.CrossRefPubMedGoogle Scholar
  20. 20.
    Dupont S, Morsut L, Aragona M, et al. Role of YAP/TAZ in mechanotransduction. Nature. 2011;474:179–83. doi: 10.1038/nature10137.CrossRefPubMedGoogle Scholar
  21. 21.
    Adams JC. Fascin-1 as a biomarker and prospective therapeutic target in colorectal cancer. Expert Rev Mol Diagn. 2015;15:41–8. doi: 10.1586/14737159.2015.976557.CrossRefPubMedGoogle Scholar
  22. 22.
    Nakae K, Nishimura Y, Ohba S, Akamatsu Y. Migrastatin acts as a muscarinic acetylcholine receptor antagonist. J Antibiot (Tokyo). 2006;59:685–92. doi: 10.1038/ja.2006.91.CrossRefGoogle Scholar

Copyright information

© International Society of Oncology and BioMarkers (ISOBM) 2016

Authors and Affiliations

  • Zhigang Liang
    • 1
    • 2
  • Ying Wang
    • 1
  • Zhenya Shen
    • 1
  • Xiaomei Teng
    • 1
  • Xinjian Li
    • 2
  • Chenwei Li
    • 2
  • Weijie Wu
    • 2
  • Zenghui Zhou
    • 2
  • Zishan Wang
    • 2
  1. 1.Department of Cardiovascular Surgery of the First Affiliated Hospital & Institute for Cardiovascular ScienceSoochow UniversitySuzhouChina
  2. 2.Department of Thoracic SurgeryNingbo First HospitalNingboChina

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