Control of the Cell Morphology and the S Phase Entry by Mitogen-activated Protein Kinase Kinase

Gotoh, Isamu; Fukuda, Makoto; Adachi, Makoto; Nishida, Eisuke

doi:10.1074/jbc.274.17.11874

Cited by 30 publications

(29 citation statements)

References 39 publications

(53 reference statements)

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“…To further verify the differential MEK-dependent localization of ERK1b, we examined the physical association of ERK1 and ERK1b with wild type MEK. As reported before for ERK2 and Xenopus ERK (8,25), ERK1 was associated with MEK1 in resting cells and the interaction was prevented upon stimulation (Fig. 9B).…”

Section: Erk1b An Erk Isoform With Unique Regulationsupporting

confidence: 51%

ERK1b, a 46-kDa ERK Isoform That Is Differentially Regulated by MEK

Yung

Yao

Hanoch

et al. 2000

Journal of Biological Chemistry

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We identified a 46-kDa ERK, whose kinetics of activation was similar to that of ERK1 and ERK2 in most cell lines and conditions, but showed higher fold activation in response to osmotic shock and epidermal growth factor treatments of Ras-transformed cells. We purified and cloned this novel ERK (ERK1b), which is an alternatively spliced form of ERK1 with a 26-amino acid insertion between residues 340 and 341 of ERK1. When expressed in COS7 cells, ERK1b exhibited kinetics of activation and kinase activity similar to those of ERK1. Unlike the uniform pattern of expression of ERK1 and ERK2, ERK1b was detected only in some of the tissues examined and seems to be abundant in the rat and human heart. Interestingly, in Ras-transformed Rat1 cells, there was a 7-fold higher expression of ERK1b, which was also more responsive than ERK1 and ERK2 to various extracellular treatments. Unlike ERK1 and ERK2, ERK1b failed to interact with MEK1 as judged from its nuclear localization in resting cells overexpressing ERK1b together with MEK1 or by lack of coimmunoprecipitation of the two proteins. Thus, ERK1b is a novel 46-kDa ERK isoform, which seems to be the major ERK isoform that responds to exogenous stimulation in Rastransformed cells probably due to its differential regulation by MEK.

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Section: Erk1b An Erk Isoform With Unique Regulationsupporting

confidence: 51%

ERK1b, a 46-kDa ERK Isoform That Is Differentially Regulated by MEK

Yung

Yao

Hanoch

et al. 2000

Journal of Biological Chemistry

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“…While focal adhesion kinase is associated with cell migration (Lu (Parrizas et al, 1997). Moreover, ERK1/2 activation also promotes endothelial cell proliferation and morphological changes (Gotoh et al, 1999;Wu et al, 2000). Our results further implicate that Etk has an anti-apoptotic/pro-proliferative role in endothelial cells (Figure 6).…”

Section: Discussionsupporting

confidence: 56%

Coordinating Etk/Bmx activation and VEGF upregulation to promote cell survival and proliferation

et al. 2002

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“…In normal cells, conditional MAPK activation is important in gene regulation, promoting G1 cell cycle progression before DNA replication (Gotoh et al, 1999). Many oncogenes, such as Ras, are able to constitutively activate the MAPK pathway, but it is this inappropriate activation of MAPK that may mediate the transformation to invasive phenotype (Lewis et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Temporal and quantitative regulation of mitogen-activated protein kinase (MAPK) modulates cell motility and invasion

et al. 2001

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We have shown that ER-negative and invasive human breast cancer cell lines MDA-MB-468 and MDA-MB-231 have constitutively higher mitogen activated protein kinase (ERK1&2/MAPK) when compared to the ERpositive and non-invasive MCF-7 human breast cancer cells. In MCF-7 cells, TGFa stimulation induced only transient MAPK activation, leading to a transient increase in cell migration. However, MDA 231 and MDA 468 cells, TGFa stimulation induced sustained MAPK activation, which correlated with enhanced cell motility and in vitro invasion. Serum stimulation activates ERK/MAPK activity persistently in both ER-positive and ER-negative breast cancer cells, leading to enhanced and sustained cell migration. Inhibition of MAPK activation by anti-sense MEK expression in MDA-MB-468 cells signi®cantly inhibits cell migration and in vitro invasion. In contrast, MCF-7 cells expressing constitutively activated MEK show a signi®cant increase in MAPK activity and cell migration, but this failed to enhance in vitro invasion. The kinetic pro®les of MAPK activation and inhibition show a relationship between the duration and magnitude of MAPK activation and cell migration in both ER-positive and ER-negative human breast cancer cells. These studies show that cell motility is modulated by the magnitude and the duration of MAPK activation; but increased activation of MAPK may not be su cient to allow in vitro invasion in noninvasive MCF-7 breast cancer cells. Oncogene (2001) 20, 4209 ± 4218.

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Control of the Cell Morphology and the S Phase Entry by Mitogen-activated Protein Kinase Kinase

Cited by 30 publications

References 39 publications

ERK1b, a 46-kDa ERK Isoform That Is Differentially Regulated by MEK

ERK1b, a 46-kDa ERK Isoform That Is Differentially Regulated by MEK

Coordinating Etk/Bmx activation and VEGF upregulation to promote cell survival and proliferation

Temporal and quantitative regulation of mitogen-activated protein kinase (MAPK) modulates cell motility and invasion

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