Oncogene ect2 is related to regulators of small GTP-binding proteins

@article{Miki1993OncogeneEI,
  title={Oncogene ect2 is related to regulators of small GTP-binding proteins},
  author={Toru Miki and Cherylyn L. Smith and Jason E. Long and Alessandra Eva and Timothy P Fleming},
  journal={Nature},
  year={1993},
  volume={362},
  pages={462-465}
}
WE have developed an efficient expression cloning system that allows rapid isolation of complementary DNAs able to induce the transformed phenotype1, 2. We searched for molecules expressed in epithelial cells and possessing transforming potential to fibro-blasts, and cloned a cDNA for the normal receptor of a growth factor secreted by NIH/3T3 cells3, 4. Here we report a second novel transforming gene, ect2. The isolated cDNA is activated by amino-terminal truncation of the normal product. The… 
Expression Cloning of lsc, a Novel Oncogene with Structural Similarities to the Dbl Family of Guanine Nucleotide Exchange Factors*
TLDR
Results indicate a role for the Rho family of GTPases in mediating the transforming activity of Lsc and are consistent with the exchange specificities that have been attributed to Dbl family members.
Interaction of ect2 and Dbl with Rho-related GTPases.
  • T. Miki
  • Biology
    Methods in enzymology
  • 1995
Expression Cloning of lfc, a Novel Oncogene with Structural Similarities to Guanine Nucleotide Exchange Factors and to the Regulatory Region of Protein Kinase C (*)
TLDR
Although the removal of the PH domain of the Lfc protein completely eliminated its ability to transform NIH 3T3 cells, replacement of this domain with an isoprenylation site restored all of its transforming activity, suggesting that a PH domain-dependent recruitment of the lfc protein to the cellular membrane is a necessary step for cellular transformation.
Assignment1 of the Ect2 protooncogene to mouse chromosome band 3B by in situ hybridization
TLDR
The mouse Ect2 (epithelial cell transforming gene 2) was isolated from Balb/MK mouse epithelial cells using an expression cloning approach and may play a critical role in a signaling pathway towards malignant transformation through controlling the Rho family proteins.
The Dbl family of oncogenes.
The product of the cph oncogene is a truncated, nucleotide-binding protein that enhances cellular survival to stress
TLDR
Syrian hamster full-length cDNAs for the cph oncogene and proto-oncogene are isolated and show increased survival to various forms of stress, strongly suggesting that cph participates in cellular mechanisms of response to stress.
Ostip2, a novel oncoprotein that associates with the Rho exchange factor Ost.
TLDR
Ostip2 is a novel oncoprotein that can interact with the Rho exchange factor Ost, and inoculation of athymic (nude) mice with OSTIP2 transfectants strongly induced tumor formation.
Direct Involvement of the Small GTP-binding Protein Rho in lbc Oncogene Function (*)
TLDR
Results strongly indicate that the lbc oncogene encodes a specific guanine nucleotide exchange factor for Rho and causes cellular transformation through activation of the Rho signaling pathway.
Regulation of the Dbl Proto-oncogene by Heat Shock Cognate Protein 70 (Hsc70)*
TLDR
The molecular chaperone heat shock cognate protein (Hsc70) is identified as a binding partner that preferentially interacts with the proto-oncogenic form of Dbl, and it is proposed that Hsc70 attenuates Dbl activity by maintaining an inactive conformation in which the amino terminus is “folded over the catalytic DH-PH domain.
Protein kinase Cι promotes UBF1–ECT2 binding on ribosomal DNA to drive rRNA synthesis and transformed growth of non-small-cell lung cancer cells
TLDR
Lentiviral shRNA knockdown and reconstitution experiments revealed that both a functional ECT2 BRCT domain and the UBF1 Ser-412 phosphorylation site are required for U BF1-mediated E CT2 recruitment to rDNA, elevated rRNA synthesis, and transformed growth.
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