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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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ECT2

Introduction

Epithelial cell transforming sequence 2 oncogene, also known as ECT2, is a human gene.[1]

The protein encoded by this gene is a transforming protein that is related to Rho-specific exchange factors and yeast cell cycle regulators. The expression of this gene is elevated with the onset of DNA synthesis and remains elevated during G2 and M phases. In situ hybridization analysis showed that expression is at a high level in cells undergoing mitosis in regenerating liver. Thus, this protein is expressed in a cell cycle-dependent manner during liver regeneration, and is thought to have an important role in the regulation of cytokinesis.[1]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: ECT2 epithelial cell transforming sequence 2 oncogene”.
Further reading

Further reading

  • Takai S, Long JE, Yamada K, Miki T (1995). “Chromosomal localization of the human ECT2 proto-oncogene to 3q26.1–>q26.2 by somatic cell analysis and fluorescence in situ hybridization”. Genomics. 27 (1): 220–2. doi:10.1006/geno.1995.1033. PMID 7665179.
  • Miki T, Smith CL, Long JE; et al. (1993). “Oncogene ect2 is related to regulators of small GTP-binding proteins”. Nature. 362 (6419): 462–5. doi:10.1038/362462a0. PMID 8464478.
  • Hillier LD, Lennon G, Becker M; et al. (1997). “Generation and analysis of 280,000 human expressed sequence tags”. Genome Res. 6 (9): 807–28. PMID 8889549.
  • Tatsumoto T, Xie X, Blumenthal R; et al. (1999). “Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis”. J. Cell Biol. 147 (5): 921–8. PMID 10579713.
  • Kimura K, Tsuji T, Takada Y; et al. (2000). “Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation”. J. Biol. Chem. 275 (23): 17233–6. doi:10.1074/jbc.C000212200. PMID 10837491.
  • Wennerberg K, Ellerbroek SM, Liu RY; et al. (2003). “RhoG signals in parallel with Rac1 and Cdc42”. J. Biol. Chem. 277 (49): 47810–7. doi:10.1074/jbc.M203816200. PMID 12376551.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Matsuda A, Suzuki Y, Honda G; et al. (2003). “Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways”. Oncogene. 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501.
  • Saito S, Tatsumoto T, Lorenzi MV; et al. (2004). “Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains”. J. Cell. Biochem. 90 (4): 819–36. doi:10.1002/jcb.10688. PMID 14587037.
  • Hara T, Ishida H, Raziuddin R; et al. (2004). “Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells”. Mol. Biol. Cell. 15 (3): 1172–84. doi:10.1091/mbc.E03-07-0531. PMID 14668487.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Liu XF, Ishida H, Raziuddin R, Miki T (2004). “Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity”. Mol. Cell. Biol. 24 (15): 6665–75. doi:10.1128/MCB.24.15.6665-6675.2004. PMID 15254234.
  • Kim JE, Billadeau DD, Chen J (2005). “The tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesis”. J. Biol. Chem. 280 (7): 5733–9. doi:10.1074/jbc.M409298200. PMID 15545273.
  • Oceguera-Yanez F, Kimura K, Yasuda S; et al. (2005). “Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis”. J. Cell Biol. 168 (2): 221–32. doi:10.1083/jcb.200408085. PMID 15642749.
  • Yüce O, Piekny A, Glotzer M (2007). “An ECT2-centralspindlin complex regulates the localization and function of RhoA”. J. Cell Biol. 170 (4): 571–82. doi:10.1083/jcb.200501097. PMID 16103226.
  • Niiya F, Xie X, Lee KS; et al. (2006). “Inhibition of cyclin-dependent kinase 1 induces cytokinesis without chromosome segregation in an ECT2 and MgcRacGAP-dependent manner”. J. Biol. Chem. 280 (43): 36502–9. doi:10.1074/jbc.M508007200. PMID 16118207.
  • Zhao WM, Fang G (2005). “MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis”. Proc. Natl. Acad. Sci. U.S.A. 102 (37): 13158–63. doi:10.1073/pnas.0504145102. PMID 16129829.
  • Hara T, Abe M, Inoue H; et al. (2006). “Cytokinesis regulator ECT2 changes its conformation through phosphorylation at Thr-341 in G2/M phase”. Oncogene. 25 (4): 566–78. doi:10.1038/sj.onc.1209078. PMID 16170345.
  • Niiya F, Tatsumoto T, Lee KS, Miki T (2006). “Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA”. Oncogene. 25 (6): 827–37. doi:10.1038/sj.onc.1209124. PMID 16247472.
  • Nishimura Y, Yonemura S (2006). “Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis”. J. Cell. Sci. 119 (Pt 1): 104–14. doi:10.1242/jcs.02737. PMID 16352658.

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