COLLABORATIVE TRANSFORMATION WITH TWO ONCOGENES; myc COLLABORATING WITH V-src IN PRIMARY CELLS AND WITH AN IMMORTALIZATION-POSITIVE SV40 MUTATED ONCOGENE IN ESTABLISHED RAT CELLS

Ikeda, Masa‐Aki; Yokoyama, Masahiro; Iritani, Akira; Miura, Osamu; Katayama, Nachiko; Yonemoto, Rieko; Fujinaga, Kei; Yamaguchi, Nobuo; Tsuchida, Nobuo

doi:10.1016/b978-0-12-370652-2.50015-3

Cited by 2 publications

(1 citation statement)

References 15 publications

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“…E322K , originally cloned in pGEM ® -T easy vector (Promega, Madison, WI), were PCR-amplified using 5'-TTG ATATCTTATGGCGGCGGCG-3' (forward) and 5'-GGCTC GAGTTAAGATCTGTATCCTGGCTG-3' (reverse) primers, ONCOLOGY REPORTS 20: 957-962, 2008 957 ERK2 CD domain mutation from a human cancer cell line enhanced anchorage-independent cell growth and abnormality in Drosophila To express in mouse cells the NotI fragment of ERK2, originally cloned in pGEM-T easy vector, the cells were cloned in a pLTR-SA vector (14) where the BamHI site was changed to NotI site by blunting the BamHI site followed by NotI linker ligation. A neomycin derivative (G418) gene was inserted.…”

Section: Construction Of Ha-tagged and Ltr Plasmids Erk2 Wt Or Erk2mentioning

confidence: 99%

ERK2 CD domain mutation from a human cancer cell line enhanced anchorage-independent cell growth and abnormality in Drosophila

Mahalingam

Ramanathan²,

Ida³

et al. 1994

Oncol Rep

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Abstract.In a human cancer cell line, we previously found a mutation in codon 322 of the extracellular signal-regulated kinase (ERK2 E322K ), the protein showed a faster migration when compared to wild-type in SDS-PAGE and constitutive phosphorylation. However, the reason for the faster migration, and the biochemical and biological properties of the mutation is unknown. In this study, we report that the amino acid charge-change mutation in the common docking (CD) domain is important for fast migration. In vitro binding of ERK2 E322K to MKP1 and RSK2 was lost, resulting in constitutive activation and possibly contributing to a more efficient colony formation in soft agar. We established transgenic flies by carrying the corresponding CD domain mutation, DERK E335K , which developed smaller and rougher eyes compared with the wild-type. Taken together, these data are consistent with ERK2 E322K loss of contact with downstream effectors and its constitutive activation, presenting an oncogenic potential and weak abnormality in differentiation.

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Section: Construction Of Ha-tagged and Ltr Plasmids Erk2 Wt Or Erk2mentioning

confidence: 99%

ERK2 CD domain mutation from a human cancer cell line enhanced anchorage-independent cell growth and abnormality in Drosophila

Mahalingam

Ramanathan²,

Ida³

et al. 1994

Oncol Rep

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show abstract

Roles of p53 mutation in cell line establishment and identification of the minimum transactivation and transform suppression domains

Hirano

Tsutsumi‐Ishii

Tsuchida

1995

European Journal of Cancer Part B: Oral Oncology

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COLLABORATIVE TRANSFORMATION WITH TWO ONCOGENES; myc COLLABORATING WITH V-src IN PRIMARY CELLS AND WITH AN IMMORTALIZATION-POSITIVE SV40 MUTATED ONCOGENE IN ESTABLISHED RAT CELLS

Cited by 2 publications

References 15 publications

ERK2 CD domain mutation from a human cancer cell line enhanced anchorage-independent cell growth and abnormality in Drosophila

ERK2 CD domain mutation from a human cancer cell line enhanced anchorage-independent cell growth and abnormality in Drosophila

Roles of p53 mutation in cell line establishment and identification of the minimum transactivation and transform suppression domains

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